KCC1B_HUMAN
ID KCC1B_HUMAN Reviewed; 343 AA.
AC Q6P2M8; B4DJR8; B4E1A6; B7WPG0; D3DWU7; Q8N4R0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1B;
DE EC=2.7.11.17;
DE AltName: Full=CaM kinase I beta;
DE Short=CaM kinase IB;
DE Short=CaM-KI beta;
DE Short=CaMKI-beta;
DE AltName: Full=Pregnancy up-regulated non-ubiquitously-expressed CaM kinase;
GN Name=PNCK;
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 [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Liver, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [6]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-262.
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).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a
CC proposed calcium-triggered signaling cascade. In vitro phosphorylates
CC CREB1 and SYN1/synapsin I. Phosphorylates and activates CAMK1 (By
CC similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6P2M8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2M8-2; Sequence=VSP_012635;
CC Name=3;
CC IsoId=Q6P2M8-3; Sequence=VSP_012634;
CC Name=4;
CC IsoId=Q6P2M8-5; Sequence=VSP_039091;
CC Name=5;
CC IsoId=Q6P2M8-6; Sequence=VSP_043373;
CC -!- PTM: Phosphorylated by CAMKK1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AK296203; BAG58930.1; -; mRNA.
DR EMBL; AK303746; BAG64718.1; -; mRNA.
DR EMBL; CR611192; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72838.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72839.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72841.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72842.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72843.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72845.1; -; Genomic_DNA.
DR EMBL; BC064422; AAH64422.1; -; mRNA.
DR CCDS; CCDS35503.2; -. [Q6P2M8-5]
DR CCDS; CCDS48189.1; -. [Q6P2M8-6]
DR RefSeq; NP_001034671.3; NM_001039582.3. [Q6P2M8-5]
DR RefSeq; NP_001129212.1; NM_001135740.1. [Q6P2M8-6]
DR RefSeq; XP_005274708.1; XM_005274651.2.
DR RefSeq; XP_006724872.1; XM_006724809.3. [Q6P2M8-1]
DR RefSeq; XP_011529409.2; XM_011531107.2. [Q6P2M8-1]
DR RefSeq; XP_011529412.1; XM_011531110.2.
DR RefSeq; XP_011529413.1; XM_011531111.2. [Q6P2M8-1]
DR RefSeq; XP_011529414.1; XM_011531112.2. [Q6P2M8-1]
DR RefSeq; XP_016884766.1; XM_017029277.1.
DR RefSeq; XP_016884767.1; XM_017029278.1.
DR RefSeq; XP_016884768.1; XM_017029279.1. [Q6P2M8-1]
DR AlphaFoldDB; Q6P2M8; -.
DR SMR; Q6P2M8; -.
DR BioGRID; 126582; 1.
DR IntAct; Q6P2M8; 2.
DR STRING; 9606.ENSP00000405950; -.
DR BindingDB; Q6P2M8; -.
DR ChEMBL; CHEMBL3627592; -.
DR iPTMnet; Q6P2M8; -.
DR PhosphoSitePlus; Q6P2M8; -.
DR BioMuta; PNCK; -.
DR DMDM; 67466915; -.
DR jPOST; Q6P2M8; -.
DR MassIVE; Q6P2M8; -.
DR PaxDb; Q6P2M8; -.
DR PeptideAtlas; Q6P2M8; -.
DR PRIDE; Q6P2M8; -.
DR ProteomicsDB; 66908; -. [Q6P2M8-1]
DR ProteomicsDB; 66909; -. [Q6P2M8-2]
DR ProteomicsDB; 66910; -. [Q6P2M8-3]
DR ProteomicsDB; 66911; -. [Q6P2M8-5]
DR ProteomicsDB; 66912; -. [Q6P2M8-6]
DR Antibodypedia; 2076; 216 antibodies from 26 providers.
DR DNASU; 139728; -.
DR Ensembl; ENST00000340888.8; ENSP00000340586.4; ENSG00000130822.16. [Q6P2M8-1]
DR Ensembl; ENST00000370142.5; ENSP00000359161.1; ENSG00000130822.16. [Q6P2M8-2]
DR Ensembl; ENST00000370145.8; ENSP00000359164.4; ENSG00000130822.16. [Q6P2M8-6]
DR Ensembl; ENST00000370150.5; ENSP00000359169.1; ENSG00000130822.16. [Q6P2M8-1]
DR Ensembl; ENST00000447676.6; ENSP00000405950.2; ENSG00000130822.16. [Q6P2M8-5]
DR GeneID; 139728; -.
DR KEGG; hsa:139728; -.
DR MANE-Select; ENST00000340888.8; ENSP00000340586.4; NM_001366977.1; NP_001353906.1.
DR UCSC; uc011myt.3; human. [Q6P2M8-1]
DR CTD; 139728; -.
DR DisGeNET; 139728; -.
DR GeneCards; PNCK; -.
DR HGNC; HGNC:13415; PNCK.
DR HPA; ENSG00000130822; Tissue enhanced (brain, intestine, seminal vesicle).
DR MIM; 300680; gene.
DR neXtProt; NX_Q6P2M8; -.
DR OpenTargets; ENSG00000130822; -.
DR PharmGKB; PA134988711; -.
DR VEuPathDB; HostDB:ENSG00000130822; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000162187; -.
DR InParanoid; Q6P2M8; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q6P2M8; -.
DR TreeFam; TF314166; -.
DR PathwayCommons; Q6P2M8; -.
DR SignaLink; Q6P2M8; -.
DR SIGNOR; Q6P2M8; -.
DR BioGRID-ORCS; 139728; 18 hits in 737 CRISPR screens.
DR ChiTaRS; PNCK; human.
DR GenomeRNAi; 139728; -.
DR Pharos; Q6P2M8; Tchem.
DR PRO; PR:Q6P2M8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q6P2M8; protein.
DR Bgee; ENSG00000130822; Expressed in right frontal lobe and 120 other tissues.
DR ExpressionAtlas; Q6P2M8; baseline and differential.
DR Genevisible; Q6P2M8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd14169; STKc_CaMKI_beta; 1.
DR InterPro; IPR042696; CaMKI_beta_STKc.
DR InterPro; IPR011009; Kinase-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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Calmodulin-binding; Cytoplasm;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..343
FT /note="Calcium/calmodulin-dependent protein kinase type 1B"
FT /id="PRO_0000086079"
FT DOMAIN 15..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 290..311
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 319..343
FT /note="Disordered"
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 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012634"
FT VAR_SEQ 1
FT /note="M -> MEAAFGQVAGSACPRRGGEGRDWKAESLADLWPKSSPGDSHRWCKGP
FT GAGPAGPQLREAARASSGLGGGGRHPSRIPAIALQDM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039091"
FT VAR_SEQ 1
FT /note="M -> MWRRVCGGLAGRRPSGDM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043373"
FT VAR_SEQ 179
FT /note="V -> AEPVTLSGMAACVPVRASVCLWPP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012635"
FT VARIANT 262
FT /note="Q -> H (in dbSNP:rs56060609)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040598"
FT CONFLICT 127
FT /note="L -> P (in Ref. 1; BAG58930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38500 MW; E954AEE89DE608C9 CRC64;
MLLLKKHTED ISSVYEIRER LGSGAFSEVV LAQERGSAHL VALKCIPKKA LRGKEALVEN
EIAVLRRISH PNIVALEDVH ESPSHLYLAM ELVTGGELFD RIMERGSYTE KDASHLVGQV
LGAVSYLHSL GIVHRDLKPE NLLYATPFED SKIMVSDFGL SKIQAGNMLG TACGTPGYVA
PELLEQKPYG KAVDVWALGV ISYILLCGYP PFYDESDPEL FSQILRASYE FDSPFWDDIS
ESAKDFIRHL LERDPQKRFT CQQALRHLWI SGDTAFDRDI LGSVSEQIRK NFARTHWKRA
FNATSFLRHI RKLGQIPEGE GASEQGMARH SHSGLRAGQP PKW
