ID   SRPK3_HUMAN             Reviewed;         567 AA.
AC   Q9UPE1; Q13583; Q4F970; Q562F5; Q9UM62;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   25-MAY-2022, entry version 177.
DE   RecName: Full=SRSF protein kinase 3;
DE            EC=2.7.11.1;
DE   AltName: Full=Muscle-specific serine kinase 1;
DE            Short=MSSK-1;
DE   AltName: Full=Serine/arginine-rich protein-specific kinase 3;
DE            Short=SR-protein-specific kinase 3;
DE   AltName: Full=Serine/threonine-protein kinase 23;
GN   Name=SRPK3; Synonyms=MSSK1, STK23;
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 2 AND 3).
RC   TISSUE=Skeletal muscle;
RA   Brenner V., Rosenthal A., Platzer M.;
RT   "Cloning and sequencing of a new human serine kinase gene located in human
RT   Xq28.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA   Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA   Wen S., Lin L., Yang S.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
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   TISSUE SPECIFICITY.
RX   PubMed=11063724; DOI=10.1093/hmg/9.18.2651;
RA   Grunau C., Hindermann W., Rosenthal A.;
RT   "Large-scale methylation analysis of human genomic DNA reveals tissue-
RT   specific differences between the methylation profiles of genes and
RT   pseudogenes.";
RL   Hum. Mol. Genet. 9:2651-2663(2000).
RN   [7]
RP   REVIEW ON FUNCTION.
RX   PubMed=21205200; DOI=10.1111/j.1742-4658.2010.07987.x;
RA   Giannakouros T., Nikolakaki E., Mylonis I., Georgatsou E.;
RT   "Serine-arginine protein kinases: a small protein kinase family with a
RT   large cellular presence.";
RL   FEBS J. 278:570-586(2011).
RN   [8]
RP   VARIANTS [LARGE SCALE ANALYSIS] CYS-101; GLU-114 AND LYS-233.
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: Serine/arginine-rich protein-specific kinase which
CC       specifically phosphorylates its substrates at serine residues located
CC       in regions rich in arginine/serine dipeptides, known as RS domains.
CC       Phosphorylates the SR splicing factor SRSF1 and the lamin-B receptor
CC       (LBR) in vitro. Required for normal muscle development (By similarity).
CC       {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=2.7.11.1;
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=2.7.11.1;
CC   -!- INTERACTION:
CC       Q9UPE1; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-6381269, EBI-539478;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9UPE1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UPE1-2; Sequence=VSP_040939, VSP_040940, VSP_040941;
CC       Name=3;
CC         IsoId=Q9UPE1-3; Sequence=VSP_040940, VSP_040941;
CC       Name=4;
CC         IsoId=Q9UPE1-4; Sequence=VSP_040940;
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in skeletal and heart muscle.
CC       {ECO:0000269|PubMed:11063724}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase 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; AF027406; AAD01848.1; -; mRNA.
DR   EMBL; U82808; AAD00539.1; -; mRNA.
DR   EMBL; DQ099381; AAZ13757.1; -; mRNA.
DR   EMBL; AK301749; BAG63211.1; -; mRNA.
DR   EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC092416; AAH92416.1; -; mRNA.
DR   EMBL; BC117124; AAI17125.1; -; mRNA.
DR   CCDS; CCDS35441.1; -. [Q9UPE1-1]
DR   CCDS; CCDS55537.1; -. [Q9UPE1-3]
DR   CCDS; CCDS55538.1; -. [Q9UPE1-4]
DR   RefSeq; NP_001164231.1; NM_001170760.1. [Q9UPE1-4]
DR   RefSeq; NP_001164232.1; NM_001170761.1. [Q9UPE1-3]
DR   RefSeq; NP_055185.2; NM_014370.3. [Q9UPE1-1]
DR   AlphaFoldDB; Q9UPE1; -.
DR   SMR; Q9UPE1; -.
DR   BioGRID; 117745; 144.
DR   IntAct; Q9UPE1; 138.
DR   STRING; 9606.ENSP00000359119; -.
DR   BindingDB; Q9UPE1; -.
DR   ChEMBL; CHEMBL5415; -.
DR   DrugCentral; Q9UPE1; -.
DR   GuidetoPHARMACOLOGY; 2210; -.
DR   iPTMnet; Q9UPE1; -.
DR   PhosphoSitePlus; Q9UPE1; -.
DR   BioMuta; SRPK3; -.
DR   DMDM; 332278151; -.
DR   EPD; Q9UPE1; -.
DR   jPOST; Q9UPE1; -.
DR   MassIVE; Q9UPE1; -.
DR   MaxQB; Q9UPE1; -.
DR   PaxDb; Q9UPE1; -.
DR   PeptideAtlas; Q9UPE1; -.
DR   PRIDE; Q9UPE1; -.
DR   ProteomicsDB; 85367; -. [Q9UPE1-1]
DR   ProteomicsDB; 85368; -. [Q9UPE1-2]
DR   ProteomicsDB; 85369; -. [Q9UPE1-3]
DR   ProteomicsDB; 85370; -. [Q9UPE1-4]
DR   Antibodypedia; 30953; 170 antibodies from 26 providers.
DR   DNASU; 26576; -.
DR   Ensembl; ENST00000370101.8; ENSP00000359119.3; ENSG00000184343.11.
DR   Ensembl; ENST00000370104.5; ENSP00000359122.1; ENSG00000184343.11. [Q9UPE1-4]
DR   Ensembl; ENST00000393786.7; ENSP00000377376.3; ENSG00000184343.11. [Q9UPE1-3]
DR   GeneID; 26576; -.
DR   KEGG; hsa:26576; -.
DR   MANE-Select; ENST00000370101.8; ENSP00000359119.3; NM_014370.4; NP_055185.2.
DR   UCSC; uc004fil.4; human. [Q9UPE1-1]
DR   CTD; 26576; -.
DR   DisGeNET; 26576; -.
DR   GeneCards; SRPK3; -.
DR   HGNC; HGNC:11402; SRPK3.
DR   HPA; ENSG00000184343; Tissue enhanced (skeletal muscle, tongue).
DR   MIM; 301002; gene.
DR   neXtProt; NX_Q9UPE1; -.
DR   OpenTargets; ENSG00000184343; -.
DR   PharmGKB; PA162404805; -.
DR   VEuPathDB; HostDB:ENSG00000184343; -.
DR   eggNOG; KOG1290; Eukaryota.
DR   GeneTree; ENSGT00940000157877; -.
DR   InParanoid; Q9UPE1; -.
DR   OMA; IEKYEWP; -.
DR   OrthoDB; 866496at2759; -.
DR   TreeFam; TF105334; -.
DR   BRENDA; 2.7.11.1; 2681.
DR   PathwayCommons; Q9UPE1; -.
DR   SignaLink; Q9UPE1; -.
DR   BioGRID-ORCS; 26576; 8 hits in 725 CRISPR screens.
DR   ChiTaRS; SRPK3; human.
DR   GenomeRNAi; 26576; -.
DR   Pharos; Q9UPE1; Tchem.
DR   PRO; PR:Q9UPE1; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9UPE1; protein.
DR   Bgee; ENSG00000184343; Expressed in muscle of leg and 167 other tissues.
DR   ExpressionAtlas; Q9UPE1; baseline and differential.
DR   Genevisible; Q9UPE1; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0060537; P:muscle tissue development; ISS:UniProtKB.
DR   GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
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; 2.
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   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Developmental protein; Differentiation;
KW   Kinase; Myogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..567
FT                   /note="SRSF protein kinase 3"
FT                   /id="PRO_0000086709"
FT   DOMAIN          79..565
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         85..93
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..280
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        212
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         108
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z0G2"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z0G2"
FT   VAR_SEQ         1..42
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_040939"
FT   VAR_SEQ         259
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT                   ECO:0000303|Ref.2"
FT                   /id="VSP_040940"
FT   VAR_SEQ         318..350
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_040941"
FT   VARIANT         101
FT                   /note="R -> C (in dbSNP:rs55910507)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041119"
FT   VARIANT         114
FT                   /note="G -> E (in dbSNP:rs35865042)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041120"
FT   VARIANT         233
FT                   /note="E -> K (in dbSNP:rs34497419)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041121"
SQ   SEQUENCE   567 AA;  62014 MW;  754A9F3759ADEE82 CRC64;
     MSASTGGGGD SGGSGGSSSS SQASCGPESS GSELALATPV PQMLQGLLGS DDEEQEDPKD
     YCKGGYHPVK IGDVFNGRYH VVRKLGWGHF STVWLCWDIQ RKRFVALKVV KSAGHYTETA
     VDEIKLLKCV RDSDPSDPKR ETIVQLIDDF RISGVNGVHV CMVLEVLGHQ LLKWIIKSNY
     QGLPVPCVKS IVRQVLHGLD YLHTKCKIIH TDIKPENILL CVGDAYIRRL AAEATEWQQA
     GAPPPSRSIV STAPQEVLQT GKLSKNKRKK MRRKRKQQKR LLEERLRDLQ RLEAMEAATQ
     AEDSGLRLDG GSGSTSSSGC HPGGARAGPS PASSSPAPGG GRSLSAGSQT SGFSGSLFSP
     ASCSILSGSS NQRETGGLLS PSTPFGASNL LVNPLEPQNA DKIKIKIADL GNACWVHKHF
     TEDIQTRQYR AVEVLIGAEY GPPADIWSTA CMAFELATGD YLFEPHSGED YSRDEDHIAH
     IVELLGDIPP AFALSGRYSR EFFNRRGELR HIHNLKHWGL YEVLMEKYEW PLEQATQFSA
     FLLPMMEYIP EKRASAADCL QHPWLNP
//