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KCC2B_HUMAN
ID   KCC2B_HUMAN             Reviewed;         666 AA.
AC   Q13554; A4D2K0; A4D2K1; A4D2K2; A4D2K3; A4D2K4; A4D2K5; A4D2K6; O95437;
AC   O95438; O95599; Q9UGH7; Q9UGH8; Q9UGH9; Q9UNX0; Q9UNX7; Q9UP00; Q9Y5N4;
AC   Q9Y6F4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 3.
DT   03-AUG-2022, entry version 218.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit beta;
DE            Short=CaM kinase II subunit beta;
DE            Short=CaMK-II subunit beta;
DE            EC=2.7.11.17;
GN   Name=CAMK2B; Synonyms=CAM2, CAMK2, CAMKB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7).
RC   TISSUE=Brain;
RX   PubMed=10858498; DOI=10.1016/s0014-5793(00)01634-3;
RA   Wang P., Wu Y., Zhou T.H., Sun Y., Pei G.;
RT   "Identification of alternative splicing variants of the beta subunit of
RT   human Ca(2+)/calmodulin-dependent protein kinase II with different
RT   activities.";
RL   FEBS Lett. 475:107-110(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   TISSUE=Skeletal muscle;
RA   Leddy J.J., Salih M., Tuana B.S.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
RC   TISSUE=Brain;
RA   Li G.Y., Cooper N.G.F.;
RT   "Molecular cloning and sequencing of human calcium/calmodulin dependent
RT   protein kinase II beta subunit.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
RC   TISSUE=Insulinoma;
RX   PubMed=10819240; DOI=10.1007/s001250051330;
RA   Rochlitz H., Voigt A., Lankat-Buttgereit B., Goeke B., Heimberg H.,
RA   Nauck M.A., Schiemann U., Schatz H., Pfeiffer A.F.;
RT   "Cloning and quantitative determination of the human Ca2+/calmodulin-
RT   dependent protein kinase II (CaMK II) isoforms in human beta cells.";
RL   Diabetologia 43:465-473(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis, and Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 302-605 (ISOFORM 2).
RX   PubMed=9060999; DOI=10.1016/s0167-4889(96)00141-3;
RA   Tombes R.M., Krystal G.W.;
RT   "Identification of novel human tumor cell-specific CaMK-II variants.";
RL   Biochim. Biophys. Acta 1355:281-292(1997).
RN   [9]
RP   ACTIVITY REGULATION, SUBUNIT, AND AUTOPHOSPHORYLATION.
RX   PubMed=14722083; DOI=10.1074/jbc.m313597200;
RA   Gaertner T.R., Kolodziej S.J., Wang D., Kobayashi R., Koomen J.M.,
RA   Stoops J.K., Waxham M.N.;
RT   "Comparative analyses of the three-dimensional structures and enzymatic
RT   properties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-
RT   dependent protein kinase II.";
RL   J. Biol. Chem. 279:12484-12494(2004).
RN   [10]
RP   INTERACTION WITH MPDZ.
RX   PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
RA   Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
RT   "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity
RT   and NMDA receptor-dependent synaptic AMPA receptor potentiation.";
RL   Neuron 43:563-574(2004).
RN   [11]
RP   FUNCTION IN SKELETAL MUSCLE, PHOSPHORYLATION AT THR-287, FUNCTION IN
RP   PHOSPHORYLATION OF PLN, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16690701; DOI=10.1113/jphysiol.2006.111757;
RA   Rose A.J., Kiens B., Richter E.A.;
RT   "Ca2+-calmodulin-dependent protein kinase expression and signalling in
RT   skeletal muscle during exercise.";
RL   J. Physiol. (Lond.) 574:889-903(2006).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21529938; DOI=10.1016/j.ceca.2011.02.007;
RA   Wayman G.A., Tokumitsu H., Davare M.A., Soderling T.R.;
RT   "Analysis of CaM-kinase signaling in cells.";
RL   Cell Calcium 50:1-8(2011).
RN   [14]
RP   REVIEW ON FUNCTION IN SKELETAL MUSCLE.
RX   PubMed=15294044; DOI=10.1079/pns2004335;
RA   Chin E.R.;
RT   "The role of calcium and calcium/calmodulin-dependent kinases in skeletal
RT   muscle plasticity and mitochondrial biogenesis.";
RL   Proc. Nutr. Soc. 63:279-286(2004).
RN   [15]
RP   REVIEW ON FUNCTION IN SKELETAL MUSCLE.
RA   Sacchetto R., Bovo E., Damiani E.;
RT   "The Ca2+-calmodulin dependent protein kinase II system of skeletal muscle
RT   sarcoplasmic reticulum.";
RL   Basic Appl. Myol. 15:5-17(2005).
RN   [16]
RP   REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
RX   PubMed=18817731; DOI=10.1016/j.neuron.2008.08.021;
RA   Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.;
RT   "Calmodulin-kinases: modulators of neuronal development and plasticity.";
RL   Neuron 59:914-931(2008).
RN   [17]
RP   REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
RX   PubMed=19996366; DOI=10.1152/physiol.00029.2009;
RA   Okamoto K., Bosch M., Hayashi Y.;
RT   "The roles of CaMKII and F-actin in the structural plasticity of dendritic
RT   spines: a potential molecular identity of a synaptic tag?";
RL   Physiology (Bethesda) 24:357-366(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 11-303 IN COMPLEX WITH INHIBITOR.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human calcium/calmodulin-dependent protein kinase IIb
RT   isoform 1 (CAMK2B).";
RL   Submitted (DEC-2007) to the PDB data bank.
RN   [20]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-489 AND LYS-510.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [21]
RP   INVOLVEMENT IN MRD54, VARIANTS MRD54 29-ARG--GLN-666 DEL; LYS-110; LEU-139;
RP   LYS-237 AND GLU-301, CHARACTERIZATION OF VARIANTS MRD54 LYS-110; LEU-139;
RP   LYS-237 AND GLU-301, AND FUNCTION.
RX   PubMed=29100089; DOI=10.1016/j.ajhg.2017.10.003;
RG   Undiagnosed Diseases Network;
RG   GEM HUGO;
RG   Deciphering Developmental Disorders Study;
RA   Kuery S., van Woerden G.M., Besnard T., Proietti Onori M., Latypova X.,
RA   Towne M.C., Cho M.T., Prescott T.E., Ploeg M.A., Sanders S.,
RA   Stessman H.A.F., Pujol A., Distel B., Robak L.A., Bernstein J.A.,
RA   Denomme-Pichon A.S., Lesca G., Sellars E.A., Berg J., Carre W., Busk O.L.,
RA   van Bon B.W.M., Waugh J.L., Deardorff M., Hoganson G.E., Bosanko K.B.,
RA   Johnson D.S., Dabir T., Holla O.L., Sarkar A., Tveten K., de Bellescize J.,
RA   Braathen G.J., Terhal P.A., Grange D.K., van Haeringen A., Lam C.,
RA   Mirzaa G., Burton J., Bhoj E.J., Douglas J., Santani A.B., Nesbitt A.I.,
RA   Helbig K.L., Andrews M.V., Begtrup A., Tang S., van Gassen K.L.I.,
RA   Juusola J., Foss K., Enns G.M., Moog U., Hinderhofer K., Paramasivam N.,
RA   Lincoln S., Kusako B.H., Lindenbaum P., Charpentier E., Nowak C.B.,
RA   Cherot E., Simonet T., Ruivenkamp C.A.L., Hahn S., Brownstein C.A., Xia F.,
RA   Schmitt S., Deb W., Bonneau D., Nizon M., Quinquis D., Chelly J.,
RA   Rudolf G., Sanlaville D., Parent P., Gilbert-Dussardier B., Toutain A.,
RA   Sutton V.R., Thies J., Peart-Vissers L.E.L.M., Boisseau P., Vincent M.,
RA   Grabrucker A.M., Dubourg C., Tan W.H., Verbeek N.E., Granzow M.,
RA   Santen G.W.E., Shendure J., Isidor B., Pasquier L., Redon R., Yang Y.,
RA   State M.W., Kleefstra T., Cogne B., Petrovski S., Retterer K.,
RA   Eichler E.E., Rosenfeld J.A., Agrawal P.B., Bezieau S., Odent S.,
RA   Elgersma Y., Mercier S.;
RT   "De Novo Mutations in Protein Kinase Genes CAMK2A and CAMK2B Cause
RT   Intellectual Disability.";
RL   Am. J. Hum. Genet. 101:768-788(2017).
RN   [22]
RP   INVOLVEMENT IN MRD54, AND VARIANTS MRD54 LEU-213 AND SER-284.
RX   PubMed=29560374; DOI=10.1002/acn3.528;
RA   Akita T., Aoto K., Kato M., Shiina M., Mutoh H., Nakashima M., Kuki I.,
RA   Okazaki S., Magara S., Shiihara T., Yokochi K., Aiba K., Tohyama J.,
RA   Ohba C., Miyatake S., Miyake N., Ogata K., Fukuda A., Matsumoto N.,
RA   Saitsu H.;
RT   "De novo variants in CAMK2A and CAMK2B cause neurodevelopmental
RT   disorders.";
RL   Ann. Clin. Transl. Neurol. 5:280-296(2018).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that functions
CC       autonomously after Ca(2+)/calmodulin-binding and autophosphorylation,
CC       and is involved in dendritic spine and synapse formation, neuronal
CC       plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in
CC       skeletal muscle. In neurons, plays an essential structural role in the
CC       reorganization of the actin cytoskeleton during plasticity by binding
CC       and bundling actin filaments in a kinase-independent manner. This
CC       structural function is required for correct targeting of CaMK2A, which
CC       acts downstream of NMDAR to promote dendritic spine and synapse
CC       formation and maintain synaptic plasticity which enables long-term
CC       potentiation (LTP) and hippocampus-dependent learning. In developing
CC       hippocampal neurons, promotes arborization of the dendritic tree and in
CC       mature neurons, promotes dendritic remodeling. Also regulates the
CC       migration of developing neurons (PubMed:29100089). Participates in the
CC       modulation of skeletal muscle function in response to exercise. In
CC       slow-twitch muscles, is involved in regulation of sarcoplasmic
CC       reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates
CC       in the control of Ca(2+) release from the SR through phosphorylation of
CC       triadin, a ryanodine receptor-coupling factor, and phospholamban
CC       (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2.
CC       {ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:29100089}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.17;
CC   -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin results in conformational change that relieves intrasteric
CC       autoinhibition and allows autophosphorylation of Thr-287 which turns
CC       the kinase in a constitutively active form and confers to the kinase a
CC       Ca(2+)-independent activity. {ECO:0000269|PubMed:14722083}.
CC   -!- SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta
CC       (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms
CC       assemble into homo- or heteromultimeric holoenzymes composed of 12
CC       subunits with two hexameric rings stacked one on top of the other
CC       (PubMed:14722083, Ref.19). Interacts with SYNGAP1 and CAMK2N2 (By
CC       similarity). Interacts with MPDZ (PubMed:15312654). Interacts with
CC       FOXO3 (By similarity). Interacts (when in a kinase inactive state not
CC       associated with calmodulin) with ARC; leading to target ARC to inactive
CC       synapses (By similarity). Interacts with CAMK2N1; this interaction
CC       requires CAMK2B activation by Ca(2+) (By similarity).
CC       {ECO:0000250|UniProtKB:P08413, ECO:0000250|UniProtKB:P28652,
CC       ECO:0000269|PubMed:14722083, ECO:0000269|PubMed:15312654,
CC       ECO:0000269|Ref.19}.
CC   -!- INTERACTION:
CC       Q13554; O00154: ACOT7; NbExp=3; IntAct=EBI-1058722, EBI-948905;
CC       Q13554; Q2VPB7: AP5B1; NbExp=3; IntAct=EBI-1058722, EBI-5917279;
CC       Q13554; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-1058722, EBI-1383687;
CC       Q13554; Q13554: CAMK2B; NbExp=2; IntAct=EBI-1058722, EBI-1058722;
CC       Q13554; Q13557: CAMK2D; NbExp=4; IntAct=EBI-1058722, EBI-351018;
CC       Q13554; Q8N0U1: FAM171A2; NbExp=3; IntAct=EBI-1058722, EBI-10264767;
CC       Q13554; P60412: KRTAP10-11; NbExp=3; IntAct=EBI-1058722, EBI-10217483;
CC       Q13554; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-1058722, EBI-1048945;
CC       Q13554; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-1058722, EBI-10241353;
CC       Q13554; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-1058722, EBI-77889;
CC       Q13554; Q9BUE0: MED18; NbExp=3; IntAct=EBI-1058722, EBI-394640;
CC       Q13554; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-1058722, EBI-399246;
CC       Q13554; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-1058722, EBI-10288852;
CC       Q13554; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-1058722, EBI-5453723;
CC       Q13554; Q93100: PHKB; NbExp=3; IntAct=EBI-1058722, EBI-740559;
CC       Q13554; Q969H6: POP5; NbExp=3; IntAct=EBI-1058722, EBI-366525;
CC       Q13554; P61225: RAP2B; NbExp=3; IntAct=EBI-1058722, EBI-750871;
CC       Q13554; O43251: RBFOX2; NbExp=3; IntAct=EBI-1058722, EBI-746056;
CC       Q13554; Q93062: RBPMS; NbExp=3; IntAct=EBI-1058722, EBI-740322;
CC       Q13554; P62913: RPL11; NbExp=3; IntAct=EBI-1058722, EBI-354380;
CC       Q13554; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-1058722, EBI-9089805;
CC       Q13554; Q5W111: SPRYD7; NbExp=3; IntAct=EBI-1058722, EBI-10248098;
CC       Q13554; Q8N0Z6: TTC5; NbExp=3; IntAct=EBI-1058722, EBI-9526213;
CC       Q13554; B3KWQ7; NbExp=3; IntAct=EBI-1058722, EBI-10175974;
CC       Q13554-3; O00154-4: ACOT7; NbExp=3; IntAct=EBI-11523526, EBI-12007918;
CC       Q13554-3; P15289: ARSA; NbExp=3; IntAct=EBI-11523526, EBI-2117357;
CC       Q13554-3; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-11523526, EBI-1383687;
CC       Q13554-3; Q13557-8: CAMK2D; NbExp=4; IntAct=EBI-11523526, EBI-11534483;
CC       Q13554-3; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-11523526, EBI-12020154;
CC       Q13554-3; Q9NUG4: CCM2L; NbExp=3; IntAct=EBI-11523526, EBI-350645;
CC       Q13554-3; Q16543: CDC37; NbExp=3; IntAct=EBI-11523526, EBI-295634;
CC       Q13554-3; Q6P1R4: DUS1L; NbExp=3; IntAct=EBI-11523526, EBI-6660325;
CC       Q13554-3; O43790: KRT86; NbExp=3; IntAct=EBI-11523526, EBI-9996498;
CC       Q13554-3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11523526, EBI-11959885;
CC       Q13554-3; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-11523526, EBI-12020132;
CC       Q13554-3; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11523526, EBI-11962084;
CC       Q13554-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11523526, EBI-16439278;
CC       Q13554-3; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-11523526, EBI-10288852;
CC       Q13554-3; Q15014: MORF4L2; NbExp=3; IntAct=EBI-11523526, EBI-399257;
CC       Q13554-3; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-11523526, EBI-5453723;
CC       Q13554-3; Q96T60: PNKP; NbExp=3; IntAct=EBI-11523526, EBI-1045072;
CC       Q13554-3; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-11523526, EBI-5452779;
CC       Q13554-3; P61225: RAP2B; NbExp=3; IntAct=EBI-11523526, EBI-750871;
CC       Q13554-3; P78317: RNF4; NbExp=3; IntAct=EBI-11523526, EBI-2340927;
CC       Q13554-3; O14787-2: TNPO2; NbExp=3; IntAct=EBI-11523526, EBI-12076664;
CC       Q13554-3; Q9Y5L0: TNPO3; NbExp=3; IntAct=EBI-11523526, EBI-1042571;
CC       Q13554-3; Q8N0Z6: TTC5; NbExp=3; IntAct=EBI-11523526, EBI-9526213;
CC       Q13554-3; P26640: VARS1; NbExp=3; IntAct=EBI-11523526, EBI-355765;
CC       Q13554-3; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-11523526, EBI-10188476;
CC       Q13554-3; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-11523526, EBI-17634549;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:21529938}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250}. Sarcoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:21529938}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21529938}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21529938}. Synapse {ECO:0000250|UniProtKB:P08413}.
CC       Note=In slow-twitch muscle, evenly distributed between longitudinal SR
CC       and junctional SR.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC         Comment=The variable region of the CAMK2B protein is encoded by at
CC         least 7 exons (V1 to V7). Alternative splicing within this region
CC         gives rise to CAMK2B isoforms.;
CC       Name=4;
CC         IsoId=Q13554-1; Sequence=Displayed;
CC       Name=1; Synonyms=Beta;
CC         IsoId=Q13554-2; Sequence=VSP_004776;
CC       Name=2; Synonyms=Beta1, Beta'E;
CC         IsoId=Q13554-3; Sequence=VSP_004770, VSP_004771, VSP_004775,
CC                                  VSP_004776;
CC       Name=3; Synonyms=Beta2;
CC         IsoId=Q13554-4; Sequence=VSP_004770, VSP_004771, VSP_004774,
CC                                  VSP_004776;
CC       Name=5; Synonyms=Beta4, BetaE;
CC         IsoId=Q13554-5; Sequence=VSP_004770, VSP_004771, VSP_004776;
CC       Name=6; Synonyms=Beta6;
CC         IsoId=Q13554-6; Sequence=VSP_004773, VSP_004776, VSP_004777;
CC       Name=7; Synonyms=Beta7;
CC         IsoId=Q13554-7; Sequence=VSP_004770, VSP_004772;
CC       Name=8;
CC         IsoId=Q13554-8; Sequence=VSP_041219, VSP_004776;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal
CC       brain. Expression is slightly lower in fetal brain. Expressed in
CC       skeletal muscle. {ECO:0000269|PubMed:16690701}.
CC   -!- INDUCTION: Activity is induced in skeletal muscle during exercise.
CC       {ECO:0000269|PubMed:16690701}.
CC   -!- DOMAIN: The CAMK2 protein kinases contain a unique C-terminal subunit
CC       association domain responsible for oligomerization.
CC   -!- PTM: Autophosphorylation of Thr-287 following activation by
CC       Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an
CC       activated state. {ECO:0000269|PubMed:14722083,
CC       ECO:0000269|PubMed:16690701}.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal dominant 54
CC       (MRD54) [MIM:617799]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period.
CC       {ECO:0000269|PubMed:29100089, ECO:0000269|PubMed:29560374}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC99802.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF078803; AAD42035.1; -; mRNA.
DR   EMBL; AF081572; AAD42036.1; -; mRNA.
DR   EMBL; AF081924; AAD42037.1; -; mRNA.
DR   EMBL; AF083419; AAD42038.1; -; mRNA.
DR   EMBL; AF140350; AAD42070.1; -; mRNA.
DR   EMBL; U23460; AAC99802.1; ALT_FRAME; mRNA.
DR   EMBL; AF112472; AAD03744.1; -; mRNA.
DR   EMBL; AF112471; AAD03743.1; -; mRNA.
DR   EMBL; AJ252236; CAB65120.1; -; mRNA.
DR   EMBL; AJ252237; CAB65121.1; -; mRNA.
DR   EMBL; AJ252238; CAB65122.1; -; mRNA.
DR   EMBL; AK290148; BAF82837.1; -; mRNA.
DR   EMBL; AK315663; BAG38029.1; -; mRNA.
DR   EMBL; CH236960; EAL23756.1; -; Genomic_DNA.
DR   EMBL; CH236960; EAL23757.1; -; Genomic_DNA.
DR   EMBL; CH236960; EAL23758.1; -; Genomic_DNA.
DR   EMBL; CH236960; EAL23759.1; -; Genomic_DNA.
DR   EMBL; CH236960; EAL23760.1; -; Genomic_DNA.
DR   EMBL; CH236960; EAL23761.1; -; Genomic_DNA.
DR   EMBL; CH236960; EAL23762.1; -; Genomic_DNA.
DR   EMBL; BC019070; AAH19070.1; -; mRNA.
DR   EMBL; U50358; AAB16863.1; -; mRNA.
DR   CCDS; CCDS43573.1; -. [Q13554-8]
DR   CCDS; CCDS5483.1; -. [Q13554-1]
DR   CCDS; CCDS5484.1; -. [Q13554-2]
DR   CCDS; CCDS5485.1; -. [Q13554-5]
DR   CCDS; CCDS5486.1; -. [Q13554-3]
DR   CCDS; CCDS5487.1; -. [Q13554-6]
DR   CCDS; CCDS5488.1; -. [Q13554-4]
DR   CCDS; CCDS5489.1; -. [Q13554-7]
DR   RefSeq; NP_001211.3; NM_001220.4. [Q13554-1]
DR   RefSeq; NP_001280099.1; NM_001293170.1. [Q13554-2]
DR   RefSeq; NP_742075.1; NM_172078.2. [Q13554-2]
DR   RefSeq; NP_742076.1; NM_172079.2. [Q13554-5]
DR   RefSeq; NP_742077.1; NM_172080.2. [Q13554-8]
DR   RefSeq; NP_742078.1; NM_172081.2. [Q13554-3]
DR   RefSeq; NP_742079.1; NM_172082.2. [Q13554-6]
DR   RefSeq; NP_742080.1; NM_172083.2. [Q13554-4]
DR   RefSeq; NP_742081.1; NM_172084.2. [Q13554-7]
DR   PDB; 3BHH; X-ray; 2.40 A; A/B/C/D=11-303.
DR   PDBsum; 3BHH; -.
DR   AlphaFoldDB; Q13554; -.
DR   SMR; Q13554; -.
DR   BioGRID; 107266; 149.
DR   DIP; DIP-39770N; -.
DR   IntAct; Q13554; 80.
DR   MINT; Q13554; -.
DR   STRING; 9606.ENSP00000379098; -.
DR   BindingDB; Q13554; -.
DR   ChEMBL; CHEMBL4121; -.
DR   DrugBank; DB07168; [4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]-6-(methylamino)pyrimidin-2-yl}amino)phenyl]acetonitrile.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; Q13554; -.
DR   GuidetoPHARMACOLOGY; 1556; -.
DR   GlyGen; Q13554; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q13554; -.
DR   PhosphoSitePlus; Q13554; -.
DR   BioMuta; CAMK2B; -.
DR   DMDM; 334302890; -.
DR   EPD; Q13554; -.
DR   jPOST; Q13554; -.
DR   MassIVE; Q13554; -.
DR   MaxQB; Q13554; -.
DR   PaxDb; Q13554; -.
DR   PeptideAtlas; Q13554; -.
DR   PRIDE; Q13554; -.
DR   ProteomicsDB; 59530; -. [Q13554-1]
DR   ProteomicsDB; 59531; -. [Q13554-2]
DR   ProteomicsDB; 59532; -. [Q13554-3]
DR   ProteomicsDB; 59533; -. [Q13554-4]
DR   ProteomicsDB; 59534; -. [Q13554-5]
DR   ProteomicsDB; 59535; -. [Q13554-6]
DR   ProteomicsDB; 59536; -. [Q13554-7]
DR   ProteomicsDB; 59537; -. [Q13554-8]
DR   Antibodypedia; 3482; 557 antibodies from 38 providers.
DR   DNASU; 816; -.
DR   Ensembl; ENST00000258682.10; ENSP00000258682.6; ENSG00000058404.20. [Q13554-8]
DR   Ensembl; ENST00000346990.8; ENSP00000326518.5; ENSG00000058404.20. [Q13554-7]
DR   Ensembl; ENST00000347193.8; ENSP00000326544.6; ENSG00000058404.20. [Q13554-6]
DR   Ensembl; ENST00000350811.7; ENSP00000326375.5; ENSG00000058404.20. [Q13554-2]
DR   Ensembl; ENST00000353625.8; ENSP00000326427.5; ENSG00000058404.20. [Q13554-4]
DR   Ensembl; ENST00000358707.7; ENSP00000351542.3; ENSG00000058404.20. [Q13554-3]
DR   Ensembl; ENST00000395747.6; ENSP00000379096.2; ENSG00000058404.20. [Q13554-5]
DR   Ensembl; ENST00000395749.7; ENSP00000379098.2; ENSG00000058404.20. [Q13554-1]
DR   Ensembl; ENST00000440254.6; ENSP00000397937.2; ENSG00000058404.20. [Q13554-2]
DR   Ensembl; ENST00000457475.5; ENSP00000390292.1; ENSG00000058404.20. [Q13554-5]
DR   GeneID; 816; -.
DR   KEGG; hsa:816; -.
DR   MANE-Select; ENST00000395749.7; ENSP00000379098.2; NM_001220.5; NP_001211.3.
DR   UCSC; uc003tkp.3; human. [Q13554-1]
DR   CTD; 816; -.
DR   DisGeNET; 816; -.
DR   GeneCards; CAMK2B; -.
DR   HGNC; HGNC:1461; CAMK2B.
DR   HPA; ENSG00000058404; Tissue enhanced (brain, skeletal muscle).
DR   MalaCards; CAMK2B; -.
DR   MIM; 607707; gene.
DR   MIM; 617799; phenotype.
DR   neXtProt; NX_Q13554; -.
DR   OpenTargets; ENSG00000058404; -.
DR   Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR   PharmGKB; PA91; -.
DR   VEuPathDB; HostDB:ENSG00000058404; -.
DR   eggNOG; KOG0033; Eukaryota.
DR   GeneTree; ENSGT00940000158973; -.
DR   HOGENOM; CLU_000288_71_0_1; -.
DR   InParanoid; Q13554; -.
DR   OMA; CIAYTRL; -.
DR   OrthoDB; 330091at2759; -.
DR   PhylomeDB; Q13554; -.
DR   TreeFam; TF315229; -.
DR   BRENDA; 2.7.11.17; 2681.
DR   PathwayCommons; Q13554; -.
DR   Reactome; R-HSA-111932; CaMK IV-mediated phosphorylation of CREB.
DR   Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR   Reactome; R-HSA-399719; Trafficking of AMPA receptors.
DR   Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-HSA-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR   Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
DR   Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-HSA-5578775; Ion homeostasis.
DR   Reactome; R-HSA-5673000; RAF activation.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR   Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR   Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR   Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR   Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR   Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
DR   Reactome; R-HSA-9620244; Long-term potentiation.
DR   Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR   Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR   SignaLink; Q13554; -.
DR   SIGNOR; Q13554; -.
DR   BioGRID-ORCS; 816; 16 hits in 1103 CRISPR screens.
DR   ChiTaRS; CAMK2B; human.
DR   EvolutionaryTrace; Q13554; -.
DR   GeneWiki; CAMK2B; -.
DR   GenomeRNAi; 816; -.
DR   Pharos; Q13554; Tchem.
DR   PRO; PR:Q13554; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q13554; protein.
DR   Bgee; ENSG00000058404; Expressed in cerebellar cortex and 170 other tissues.
DR   ExpressionAtlas; Q13554; baseline and differential.
DR   Genevisible; Q13554; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR   GO; GO:0051924; P:regulation of calcium ion transport; TAS:UniProtKB.
DR   GO; GO:0060998; P:regulation of dendritic spine development; TAS:UniProtKB.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; TAS:UniProtKB.
DR   GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB.
DR   GO; GO:0014733; P:regulation of skeletal muscle adaptation; TAS:UniProtKB.
DR   GO; GO:0051823; P:regulation of synapse structural plasticity; TAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW   Calmodulin-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Differentiation; Intellectual disability; Kinase; Membrane; Neurogenesis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Sarcoplasmic reticulum; Serine/threonine-protein kinase; Synapse;
KW   Transferase.
FT   CHAIN           1..666
FT                   /note="Calcium/calmodulin-dependent protein kinase type II
FT                   subunit beta"
FT                   /id="PRO_0000086096"
FT   DOMAIN          14..272
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          283..292
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000250"
FT   REGION          291..301
FT                   /note="Calmodulin-binding"
FT   REGION          349..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..446
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..530
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         20..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         17
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P28652"
FT   MOD_RES         287
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:16690701"
FT   MOD_RES         306
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         307
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08413"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28652"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08413"
FT   MOD_RES         400
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P28652"
FT   MOD_RES         401
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         316..340
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041219"
FT   VAR_SEQ         316
FT                   /note="V -> A (in isoform 2, isoform 3, isoform 5 and
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:10819240,
FT                   ECO:0000303|PubMed:10858498, ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9060999,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_004770"
FT   VAR_SEQ         317..533
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:10858498"
FT                   /id="VSP_004772"
FT   VAR_SEQ         317..340
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10819240,
FT                   ECO:0000303|PubMed:10858498, ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9060999,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_004771"
FT   VAR_SEQ         354..392
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10819240"
FT                   /id="VSP_004774"
FT   VAR_SEQ         354..377
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10858498"
FT                   /id="VSP_004773"
FT   VAR_SEQ         379..393
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10819240,
FT                   ECO:0000303|PubMed:10858498, ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9060999"
FT                   /id="VSP_004775"
FT   VAR_SEQ         410..533
FT                   /note="Missing (in isoform 1, isoform 2, isoform 3, isoform
FT                   5, isoform 6 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10819240,
FT                   ECO:0000303|PubMed:10858498, ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9060999,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_004776"
FT   VAR_SEQ         559..584
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10858498"
FT                   /id="VSP_004777"
FT   VARIANT         29..666
FT                   /note="Missing (in MRD54)"
FT                   /evidence="ECO:0000269|PubMed:29100089"
FT                   /id="VAR_080588"
FT   VARIANT         110
FT                   /note="E -> K (in MRD54; decreased protein abundance;
FT                   increased autophosphorylation; decreased neuronal
FT                   migration; dbSNP:rs1554402092)"
FT                   /evidence="ECO:0000269|PubMed:29100089"
FT                   /id="VAR_080589"
FT   VARIANT         139
FT                   /note="P -> L (in MRD54; decreased protein abundance;
FT                   increased autophosphorylation; decreased neuronal
FT                   migration; dbSNP:rs1554389088)"
FT                   /evidence="ECO:0000269|PubMed:29100089"
FT                   /id="VAR_080590"
FT   VARIANT         213
FT                   /note="P -> L (in MRD54; dbSNP:rs1554387293)"
FT                   /evidence="ECO:0000269|PubMed:29560374"
FT                   /id="VAR_081162"
FT   VARIANT         237
FT                   /note="E -> K (in MRD54; no effect on protein abundance;
FT                   increased autophosphorylation; decreased neuronal
FT                   migration; dbSNP:rs1554386687)"
FT                   /evidence="ECO:0000269|PubMed:29100089"
FT                   /id="VAR_080591"
FT   VARIANT         284
FT                   /note="R -> S (in MRD54; dbSNP:rs1554385203)"
FT                   /evidence="ECO:0000269|PubMed:29560374"
FT                   /id="VAR_081163"
FT   VARIANT         301
FT                   /note="K -> E (in MRD54; no effect on protein abundance;
FT                   loss of autophosphorylation; changed function in neuronal
FT                   migration; dbSNP:rs1554385111)"
FT                   /evidence="ECO:0000269|PubMed:29100089"
FT                   /id="VAR_080592"
FT   VARIANT         489
FT                   /note="P -> L (in a colorectal adenocarcinoma sample;
FT                   somatic mutation; dbSNP:rs555460132)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045581"
FT   VARIANT         510
FT                   /note="E -> K (in dbSNP:rs35452727)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045582"
FT   CONFLICT        68
FT                   /note="L -> V (in Ref. 3; AAD03744/AAD03743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="K -> N (in Ref. 8; AAB16863)"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..19
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   TURN            34..36
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           52..67
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          83..91
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           98..102
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           110..129
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           183..186
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           194..209
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           219..228
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   TURN            235..238
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           243..252
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   TURN            257..259
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           263..266
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           270..273
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           275..278
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   HELIX           285..298
FT                   /evidence="ECO:0007829|PDB:3BHH"
FT   CONFLICT        Q13554-3:316
FT                   /note="A -> V (in Ref. 1; AAD42036)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   666 AA;  72678 MW;  8CACFC3E392C3857 CRC64;
     MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL SARDHQKLER
     EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
     LEAVLHCHQM GVVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY
     LSPEVLRKEA YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
     VTPEAKNLIN QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL
     KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD GVKPQTNSTK
     NSAAATSPKG TLPPAALEPQ TTVIHNPVDG IKESSDSANT TIEDEDAKAP RVPDILSSVR
     RGSGAPEAEG PLPCPSPAPF SPLPAPSPRI SDILNSVRRG SGTPEAEGPL SAGPPPCLSP
     ALLGPLSSPS PRISDILNSV RRGSGTPEAE GPSPVGPPPC PSPTIPGPLP TPSRKQEIIK
     TTEQLIEAVN NGDFEAYAKI CDPGLTSFEP EALGNLVEGM DFHRFYFENL LAKNSKPIHT
     TILNPHVHVI GEDAACIAYI RLTQYIDGQG RPRTSQSEET RVWHRRDGKW QNVHFHCSGA
     PVAPLQ
 
 
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