SIN1_HUMAN
ID SIN1_HUMAN Reviewed; 522 AA.
AC Q9BPZ7; A8K1Z5; B1AMA4; B7Z309; Q00426; Q5JSV5; Q5JSV6; Q5JSV9; Q658R0;
AC Q699U1; Q699U2; Q699U3; Q699U4; Q6GVJ0; Q6GVJ1; Q6GVJ2;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Target of rapamycin complex 2 subunit MAPKAP1;
DE Short=TORC2 subunit MAPKAP1;
DE AltName: Full=Mitogen-activated protein kinase 2-associated protein 1;
DE AltName: Full=Stress-activated map kinase-interacting protein 1;
DE Short=SAPK-interacting protein 1;
DE Short=mSIN1;
GN Name=MAPKAP1; Synonyms=MIP1, SIN1;
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; 3 AND 5).
RX PubMed=15363842; DOI=10.1016/j.gene.2004.07.001;
RA Schroder W., Cloonan N., Bushell G., Sculley T.;
RT "Alternative polyadenylation and splicing of mRNAs transcribed from the
RT human Sin1 gene.";
RL Gene 339:17-23(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 6), TISSUE SPECIFICITY,
RP FUNCTION, AND INTERACTION WITH MAP3K2.
RX PubMed=15988011; DOI=10.1128/mcb.25.14.5955-5964.2005;
RA Cheng J., Zhang D., Kim K., Zhao Y., Zhao Y., Su B.;
RT "Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and
RT activation.";
RL Mol. Cell. Biol. 25:5955-5964(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Corpus callosum, and Substantia nigra;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 2-15 AND 257-267, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-502 (ISOFORM 1).
RC TISSUE=Glial cell;
RX PubMed=1849280; DOI=10.1073/pnas.88.7.2913;
RA Colicelli J., Nicolette C., Birchmeier C., Rodgers L., Riggs M., Wigler M.;
RT "Expression of three mammalian cDNAs that interfere with RAS function in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2913-2917(1991).
RN [10]
RP IDENTIFICATION IN THE TORC2 COMPLEX, FUNCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16962653; DOI=10.1016/j.cell.2006.08.033;
RA Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y., Huang Q.,
RA Qin J., Su B.;
RT "SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt
RT phosphorylation and substrate specificity.";
RL Cell 127:125-137(2006).
RN [11]
RP IDENTIFICATION IN THE TORC2 COMPLEX.
RX PubMed=16919458; DOI=10.1016/j.cub.2006.08.001;
RA Frias M.A., Thoreen C.C., Jaffe J.D., Schroder W., Sculley T., Carr S.A.,
RA Sabatini D.M.;
RT "mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define
RT three distinct mTORC2s.";
RL Curr. Biol. 16:1865-1870(2006).
RN [12]
RP INTERACTION WITH ATF2 AND MAPK8, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17054722; DOI=10.1111/j.1365-2443.2006.01016.x;
RA Makino C., Sano Y., Shinagawa T., Millar J.B., Ishii S.;
RT "Sin1 binds to both ATF-2 and p38 and enhances ATF-2-dependent
RT transcription in an SAPK signaling pathway.";
RL Genes Cells 11:1239-1251(2006).
RN [13]
RP FUNCTION.
RX PubMed=17043309; DOI=10.1101/gad.1461206;
RA Yang Q., Inoki K., Ikenoue T., Guan K.-L.;
RT "Identification of Sin1 as an essential TORC2 component required for
RT complex formation and kinase activity.";
RL Genes Dev. 20:2820-2832(2006).
RN [14]
RP INTERACTION WITH HRAS AND KRAS, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17303383; DOI=10.1016/j.cellsig.2007.01.013;
RA Schroder W.A., Buck M., Cloonan N., Hancock J.F., Suhrbier A., Sculley T.,
RA Bushell G.;
RT "Human Sin1 contains Ras-binding and pleckstrin homology domains and
RT suppresses Ras signalling.";
RL Cell. Signal. 19:1279-1289(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP INTERACTION WITH NBN.
RX PubMed=23762398; DOI=10.1371/journal.pone.0065586;
RA Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J.;
RT "Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific
RT domains.";
RL PLoS ONE 8:E65586-E65586(2013).
RN [18]
RP FUNCTION IN CILIOGENESIS, AND INTERACTION WITH CCDC28B.
RX PubMed=23727834; DOI=10.1093/hmg/ddt253;
RA Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N.,
RA Beales P.L., Badano J.L.;
RT "The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2
RT function and interacts with SIN1 to control cilia length independently of
RT the mTOR complex.";
RL Hum. Mol. Genet. 22:4031-4042(2013).
RN [19]
RP INTERACTION WITH RICTOR.
RX PubMed=33378666; DOI=10.1016/j.celrep.2020.108564;
RA Wrobel L., Siddiqi F.H., Hill S.M., Son S.M., Karabiyik C., Kim H.,
RA Rubinsztein D.C.;
RT "mTORC2 Assembly Is Regulated by USP9X-Mediated Deubiquitination of
RT RICTOR.";
RL Cell Rep. 33:108564-108564(2020).
CC -!- FUNCTION: Subunit of mTORC2, which regulates cell growth and survival
CC in response to hormonal signals. mTORC2 is activated by growth factors,
CC but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2
CC seems to function upstream of Rho GTPases to regulate the actin
CC cytoskeleton, probably by activating one or more Rho-type guanine
CC nucleotide exchange factors. mTORC2 promotes the serum-induced
CC formation of stress-fibers or F-actin. mTORC2 plays a critical role in
CC AKT1 'Ser-473' phosphorylation, which may facilitate the
CC phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1
CC which is a prerequisite for full activation. mTORC2 regulates the
CC phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the
CC phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is
CC required for complex formation and mTORC2 kinase activity. MAPKAP1
CC inhibits MAP3K2 by preventing its dimerization and autophosphorylation.
CC Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced
CC phosphorylation of ATF2 and ATF2-mediated transcription. Involved in
CC ciliogenesis, regulates cilia length through its interaction with
CC CCDC28B independently of mTORC2 complex. {ECO:0000269|PubMed:15988011,
CC ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:17043309,
CC ECO:0000269|PubMed:17054722, ECO:0000269|PubMed:17303383,
CC ECO:0000269|PubMed:23727834}.
CC -!- SUBUNIT: All isoforms except isoform 4 can be incorporated into the
CC mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR,
CC MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (PubMed:16962653,
CC PubMed:16919458, PubMed:33378666). Contrary to mTORC1, mTORC2 does not
CC bind to and is not sensitive to FKBP12-rapamycin. Interacts with ATF2,
CC MAP3K2 and MAPK8. Interacts with GTP-bound HRAS and KRAS. Interacts
CC with IFNAR2 and SGK1. Isoform 2 interacts with NBN. Isoform 1 interacts
CC with CCDC28B. {ECO:0000269|PubMed:15988011,
CC ECO:0000269|PubMed:16919458, ECO:0000269|PubMed:16962653,
CC ECO:0000269|PubMed:17054722, ECO:0000269|PubMed:17303383,
CC ECO:0000269|PubMed:23727834, ECO:0000269|PubMed:23762398,
CC ECO:0000269|PubMed:33378666}.
CC -!- INTERACTION:
CC Q9BPZ7; Q02156: PRKCE; NbExp=2; IntAct=EBI-749938, EBI-706254;
CC Q9BPZ7; P78527: PRKDC; NbExp=2; IntAct=EBI-749938, EBI-352053;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cytoplasmic vesicle. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=beta, gamma;
CC IsoId=Q9BPZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=alpha, beta;
CC IsoId=Q9BPZ7-2; Sequence=VSP_006098;
CC Name=3;
CC IsoId=Q9BPZ7-3; Sequence=VSP_033204;
CC Name=4;
CC IsoId=Q9BPZ7-4; Sequence=VSP_033202;
CC Name=5; Synonyms=alpha;
CC IsoId=Q9BPZ7-5; Sequence=VSP_033203, VSP_033207;
CC Name=6; Synonyms=gamma;
CC IsoId=Q9BPZ7-6; Sequence=VSP_033205, VSP_033206;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC heart and skeletal muscle. {ECO:0000269|PubMed:15988011}.
CC -!- MISCELLANEOUS: [Isoform 4]: Not involved in a TORC2 complex.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY524429; AAS90839.1; -; mRNA.
DR EMBL; AY524430; AAS90840.1; -; mRNA.
DR EMBL; AY524431; AAS90841.1; -; mRNA.
DR EMBL; AY524432; AAS90842.1; -; mRNA.
DR EMBL; AY633624; AAT46478.1; -; mRNA.
DR EMBL; AY633625; AAT46479.1; -; mRNA.
DR EMBL; AY633626; AAT46480.1; -; mRNA.
DR EMBL; AK290060; BAF82749.1; -; mRNA.
DR EMBL; AK295364; BAH12045.1; -; mRNA.
DR EMBL; AK316149; BAH14520.1; -; mRNA.
DR EMBL; AL833042; CAH56311.1; -; mRNA.
DR EMBL; AL162584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87630.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87631.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87632.1; -; Genomic_DNA.
DR EMBL; BC003044; AAH03044.1; -; mRNA.
DR EMBL; BC002326; AAH02326.1; -; mRNA.
DR EMBL; M37191; AAA36551.1; -; mRNA.
DR CCDS; CCDS35139.1; -. [Q9BPZ7-3]
DR CCDS; CCDS35140.1; -. [Q9BPZ7-1]
DR CCDS; CCDS35141.1; -. [Q9BPZ7-4]
DR CCDS; CCDS48020.1; -. [Q9BPZ7-5]
DR CCDS; CCDS6864.1; -. [Q9BPZ7-2]
DR PIR; C38637; C38637.
DR RefSeq; NP_001006618.1; NM_001006617.1. [Q9BPZ7-1]
DR RefSeq; NP_001006619.1; NM_001006618.1. [Q9BPZ7-5]
DR RefSeq; NP_001006620.1; NM_001006619.1. [Q9BPZ7-3]
DR RefSeq; NP_001006621.1; NM_001006620.1. [Q9BPZ7-4]
DR RefSeq; NP_001006622.1; NM_001006621.1. [Q9BPZ7-4]
DR RefSeq; NP_077022.1; NM_024117.3. [Q9BPZ7-2]
DR RefSeq; XP_011517312.1; XM_011519010.2.
DR RefSeq; XP_016870615.1; XM_017015126.1.
DR RefSeq; XP_016870616.1; XM_017015127.1.
DR PDB; 3VOQ; X-ray; 2.00 A; A/B=372-493.
DR PDB; 5ZCS; EM; 4.90 A; G/H=141-522.
DR PDB; 6ZWM; EM; 3.20 A; G/H=1-522.
DR PDB; 6ZWO; EM; 3.00 A; H=2-522.
DR PDB; 7LC1; X-ray; 2.35 A; B/D=275-510.
DR PDB; 7LC2; X-ray; 2.70 A; D/E=275-361.
DR PDB; 7PE7; EM; 3.41 A; G/H=1-522.
DR PDB; 7PE8; EM; 3.20 A; G=1-522.
DR PDB; 7PE9; EM; 3.70 A; G=1-522.
DR PDBsum; 3VOQ; -.
DR PDBsum; 5ZCS; -.
DR PDBsum; 6ZWM; -.
DR PDBsum; 6ZWO; -.
DR PDBsum; 7LC1; -.
DR PDBsum; 7LC2; -.
DR PDBsum; 7PE7; -.
DR PDBsum; 7PE8; -.
DR PDBsum; 7PE9; -.
DR AlphaFoldDB; Q9BPZ7; -.
DR SMR; Q9BPZ7; -.
DR BioGRID; 122551; 135.
DR ComplexPortal; CPX-4402; mTORC2 complex.
DR CORUM; Q9BPZ7; -.
DR DIP; DIP-39480N; -.
DR IntAct; Q9BPZ7; 37.
DR MINT; Q9BPZ7; -.
DR STRING; 9606.ENSP00000265960; -.
DR BindingDB; Q9BPZ7; -.
DR ChEMBL; CHEMBL4523999; -.
DR iPTMnet; Q9BPZ7; -.
DR PhosphoSitePlus; Q9BPZ7; -.
DR BioMuta; MAPKAP1; -.
DR DMDM; 15214282; -.
DR EPD; Q9BPZ7; -.
DR jPOST; Q9BPZ7; -.
DR MassIVE; Q9BPZ7; -.
DR MaxQB; Q9BPZ7; -.
DR PaxDb; Q9BPZ7; -.
DR PeptideAtlas; Q9BPZ7; -.
DR PRIDE; Q9BPZ7; -.
DR ProteomicsDB; 78599; -. [Q9BPZ7-1]
DR ProteomicsDB; 78600; -. [Q9BPZ7-2]
DR ProteomicsDB; 78601; -. [Q9BPZ7-3]
DR ProteomicsDB; 78602; -. [Q9BPZ7-4]
DR ProteomicsDB; 78603; -. [Q9BPZ7-5]
DR ProteomicsDB; 78604; -. [Q9BPZ7-6]
DR Antibodypedia; 30572; 326 antibodies from 39 providers.
DR DNASU; 79109; -.
DR Ensembl; ENST00000265960.8; ENSP00000265960.3; ENSG00000119487.17. [Q9BPZ7-1]
DR Ensembl; ENST00000350766.7; ENSP00000265961.5; ENSG00000119487.17. [Q9BPZ7-2]
DR Ensembl; ENST00000373498.5; ENSP00000362597.1; ENSG00000119487.17. [Q9BPZ7-1]
DR Ensembl; ENST00000373503.7; ENSP00000362602.3; ENSG00000119487.17. [Q9BPZ7-4]
DR Ensembl; ENST00000373511.6; ENSP00000362610.2; ENSG00000119487.17. [Q9BPZ7-3]
DR Ensembl; ENST00000394060.7; ENSP00000377624.3; ENSG00000119487.17. [Q9BPZ7-5]
DR Ensembl; ENST00000394063.5; ENSP00000377627.1; ENSG00000119487.17. [Q9BPZ7-4]
DR GeneID; 79109; -.
DR KEGG; hsa:79109; -.
DR MANE-Select; ENST00000265960.8; ENSP00000265960.3; NM_001006617.3; NP_001006618.1.
DR UCSC; uc004bpv.3; human. [Q9BPZ7-1]
DR CTD; 79109; -.
DR DisGeNET; 79109; -.
DR GeneCards; MAPKAP1; -.
DR HGNC; HGNC:18752; MAPKAP1.
DR HPA; ENSG00000119487; Low tissue specificity.
DR MIM; 610558; gene.
DR neXtProt; NX_Q9BPZ7; -.
DR OpenTargets; ENSG00000119487; -.
DR PharmGKB; PA38674; -.
DR VEuPathDB; HostDB:ENSG00000119487; -.
DR eggNOG; KOG3739; Eukaryota.
DR GeneTree; ENSGT00390000000642; -.
DR HOGENOM; CLU_514767_0_0_1; -.
DR InParanoid; Q9BPZ7; -.
DR OMA; NAKFWPQ; -.
DR OrthoDB; 1492466at2759; -.
DR PhylomeDB; Q9BPZ7; -.
DR TreeFam; TF315174; -.
DR PathwayCommons; Q9BPZ7; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR SignaLink; Q9BPZ7; -.
DR SIGNOR; Q9BPZ7; -.
DR BioGRID-ORCS; 79109; 157 hits in 1109 CRISPR screens.
DR ChiTaRS; MAPKAP1; human.
DR GeneWiki; MAPKAP1; -.
DR GenomeRNAi; 79109; -.
DR Pharos; Q9BPZ7; Tbio.
DR PRO; PR:Q9BPZ7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BPZ7; protein.
DR Bgee; ENSG00000119487; Expressed in hindlimb stylopod muscle and 195 other tissues.
DR ExpressionAtlas; Q9BPZ7; baseline and differential.
DR Genevisible; Q9BPZ7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031932; C:TORC2 complex; IPI:ComplexPortal.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; IC:ComplexPortal.
DR GO; GO:0007010; P:cytoskeleton organization; IC:ComplexPortal.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IDA:ComplexPortal.
DR GO; GO:0030307; P:positive regulation of cell growth; IC:ComplexPortal.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR DisProt; DP02693; -.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR031567; CRIM_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008828; Sin1/Avo1.
DR InterPro; IPR032679; Sin1_N.
DR InterPro; IPR031313; Sin1_PH_dom.
DR PANTHER; PTHR13335; PTHR13335; 1.
DR Pfam; PF16978; CRIM; 1.
DR Pfam; PF05422; SIN1; 1.
DR Pfam; PF16979; SIN1_PH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cytoplasmic vesicle; Direct protein sequencing; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..522
FT /note="Target of rapamycin complex 2 subunit MAPKAP1"
FT /id="PRO_0000218768"
FT REGION 2..267
FT /note="Interaction with NBN"
FT /evidence="ECO:0000269|PubMed:23762398"
FT REGION 2..184
FT /note="Interaction with MAP3K2"
FT /evidence="ECO:0000269|PubMed:15988011"
FT REGION 468..522
FT /note="Interaction with ATF2"
FT /evidence="ECO:0000269|PubMed:17054722"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..192
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_033202"
FT VAR_SEQ 321..438
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15363842"
FT /id="VSP_033203"
FT VAR_SEQ 321..356
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15363842, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15988011"
FT /id="VSP_006098"
FT VAR_SEQ 357..403
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15363842"
FT /id="VSP_033204"
FT VAR_SEQ 357..372
FT /note="SRADGVFEEDSQIDIA -> TLAASLHARFVRCKLA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15988011"
FT /id="VSP_033205"
FT VAR_SEQ 373..522
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15988011"
FT /id="VSP_033206"
FT VAR_SEQ 442..522
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15363842"
FT /id="VSP_033207"
FT CONFLICT 76..86
FT /note="WDFGIRRRSNT -> ADPARSVEAAS (in Ref. 9; AAA36551)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="D -> N (in Ref. 2; AAT46480/AAT46478/AAT46479)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="L -> F (in Ref. 3; BAF82749)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="I -> T (in Ref. 4; CAH56311)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="S -> N (in Ref. 2; AAT46478/AAT46479)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Q -> K (in Ref. 9; AAA36551)"
FT /evidence="ECO:0000305"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:7PE8"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:6ZWO"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:6ZWO"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:7LC1"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:7LC1"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:7LC1"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:7LC1"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:7LC1"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:7LC1"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:7LC1"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:7LC1"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:3VOQ"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:3VOQ"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:3VOQ"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 437..445
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:3VOQ"
FT STRAND 462..470
FT /evidence="ECO:0007829|PDB:3VOQ"
FT HELIX 472..487
FT /evidence="ECO:0007829|PDB:3VOQ"
FT HELIX 493..499
FT /evidence="ECO:0007829|PDB:7LC1"
SQ SEQUENCE 522 AA; 59123 MW; E3B808C6E58F7C48 CRC64;
MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE
TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL
KSLFEKKSLK EKPPISGKQS ILSVRLEQCP LQLNNPFNEY SKFDGKGHVG TTATKKIDVY
LPLHSSQDRL LPMTVVTMAS ARVQDLIGLI CWQYTSEGRE PKLNDNVSAY CLHIAEDDGE
VDTDFPPLDS NEPIHKFGFS TLALVEKYSS PGLTSKESLF VRINAAHGFS LIQVDNTKVT
MKEILLKAVK RRKGSQKVSG PQYRLEKQSE PNVAVDLDST LESQSAWEFC LVRENSSRAD
GVFEEDSQID IATVQDMLSS HHYKSFKVSM IHRLRFTTDV QLGISGDKVE IDPVTNQKAS
TKFWIKQKPI SIDSDLLCAC DLAEEKSPSH AIFKLTYLSN HDYKHLYFES DAATVNEIVL
KVNYILESRA STARADYFAQ KQRKLNRRTS FSFQKEKKSG QQ
