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Kinase D-interacting substrate of 220 kDa (Ankyrin repeat-rich membrane-spanning protein)

 KDIS_HUMAN              Reviewed;        1771 AA.
Q9ULH0; A1L4N4; Q4VC08; Q6MZU2; Q9H889; Q9H9E4; Q9NT37; Q9UF42;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 3.
25-OCT-2017, entry version 130.
RecName: Full=Kinase D-interacting substrate of 220 kDa;
AltName: Full=Ankyrin repeat-rich membrane-spanning protein;
Name=KIDINS220; Synonyms=ARMS, KIAA1250;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1636-1771 (ISOFORM 1), AND VARIANT
HIS-1608.
TISSUE=Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1089-1771 (ISOFORM 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1526-1771 (ISOFORM 1), AND VARIANT
HIS-1608.
TISSUE=Esophageal carcinoma, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1478-1771, AND VARIANT HIS-1608.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18089783; DOI=10.1158/0008-5472.CAN-07-1930;
Liao Y.-H., Hsu S.-M., Huang P.-H.;
"ARMS depletion facilitates UV irradiation induced apoptotic cell
death in melanoma.";
Cancer Res. 67:11547-11556(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918; SER-1365 AND
SER-1521, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555 AND SER-1633, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-885; THR-914;
SER-918; SER-1163; SER-1296; SER-1352; SER-1359; SER-1361; SER-1362;
SER-1365; SER-1521; SER-1526; SER-1555; SER-1574; SER-1623; SER-1633;
THR-1679; SER-1681 AND THR-1684, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
INVOLVEMENT IN SINO, VARIANTS SINO 1350-TRP--LEU-1771 DEL AND
1366-GLN--LEU-1771 DEL, AND CHARACTERIZATION OF VARIANT SINO
1350-TRP--LEU-1771 DEL AND 1366-GLN--LEU-1771 DEL.
PubMed=27005418; DOI=10.1093/hmg/ddw082;
DDD Study;
Josifova D.J., Monroe G.R., Tessadori F., de Graaff E.,
van der Zwaag B., Mehta S.G., Harakalova M., Duran K.J.,
Savelberg S.M., Nijman I.J., Jungbluth H., Hoogenraad C.C.,
Bakkers J., Knoers N.V., Firth H.V., Beales P.L., van Haaften G.,
van Haelst M.M.;
"Heterozygous KIDINS220/ARMS nonsense variants cause spastic
paraplegia, intellectual disability, nystagmus, and obesity.";
Hum. Mol. Genet. 25:2158-2167(2016).
-!- FUNCTION: Promotes a prolonged MAP-kinase signaling by
neurotrophins through activation of a Rap1-dependent mechanism.
Provides a docking site for the CRKL-C3G complex, resulting in
Rap1-dependent sustained ERK activation. May play an important
role in regulating postsynaptic signal transduction through the
syntrophin-mediated localization of receptor tyrosine kinases such
as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced
JAK/STAT activation. Plays a role in nerve growth factor (NGF)-
induced recruitment of RAPGEF2 to late endosomes and neurite
outgrowth. May play a role in neurotrophin- and ephrin-mediated
neuronal outgrowth and in axon guidance during neural development
and in neuronal regeneration (By similarity). Modulates stress-
induced apoptosis of melanoma cells via regulation of the MEK/ERK
signaling pathway. {ECO:0000250, ECO:0000269|PubMed:18089783}.
-!- SUBUNIT: Interacts with NTRK1, NTRK2, NTRK3, ERKL and NGFR. Can
form a ternary complex with NGFR and NTRK1 and this complex is
affected by the expression levels of KIDINS220/ARMS. An increase
in KIDINS220/ARMS expression leads to a decreased association of
NGFR and NTRK1. Interacts with SNTA1 and SNTB2 and binds to their
PDZ domains. Interacts with EPHA4 and PRKD1 (By similarity). Found
in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and
RAPGEF2; the complex is mainly formed at late endosomes in a nerve
growth factor (NGF)-dependent manner (By similarity). Interacts
with RAPGEF2; the interaction is strengthened after NGF
stimulation (By similarity). Interacts (via C-terminal domain)
with MAGI2 (via PDZ domain) (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q13643:FHL3; NbExp=4; IntAct=EBI-11046235, EBI-741101;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Late endosome {ECO:0000250}. Note=Localized
at late endosome before or after nerve growth factor (NGF)
stimulation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9ULH0-1; Sequence=Displayed;
Name=2;
IsoId=Q9ULH0-2; Sequence=VSP_031862, VSP_031866;
Name=3;
IsoId=Q9ULH0-3; Sequence=VSP_031863, VSP_031864, VSP_031865;
Name=4;
IsoId=Q9ULH0-4; Sequence=VSP_031867;
Name=5;
IsoId=Q9ULH0-5; Sequence=VSP_031861;
-!- TISSUE SPECIFICITY: Abundant in developing and adult neural
tissues as well as neuroendocrine cells and dendritic cells.
Overexpressed in melanoma and melanoma cell lines.
{ECO:0000269|PubMed:18089783}.
-!- DOMAIN: The transmembrane domain mediates interaction with NTRK1.
{ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by NTRK1, NTRK2, EPHB2 and EPHA4.
Phosphorylation at Ser-918 is induced by phorbol ester treatment.
Phosphorylation by NTRK2 is induced by brain-derived neurotrophic
factor (BDNF) and neurotrophin-4/5. Phosphorylation by NTRK1 is
induced by nerve growth factor (NGF) (By similarity).
{ECO:0000250}.
-!- DISEASE: Spastic paraplegia, intellectual disability, nystagmus,
and obesity (SINO) [MIM:617296]: An autosomal dominant syndrome
characterized by rapid growth in infancy, obesity, global
developmental delay, intellectual disability, spastic paraplegia,
ocular defects, and dysmorphic facial features.
{ECO:0000269|PubMed:27005418}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA86564.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB14728.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB033076; BAA86564.2; ALT_INIT; mRNA.
EMBL; AK022873; BAB14285.1; -; mRNA.
EMBL; AK023926; BAB14728.1; ALT_INIT; mRNA.
EMBL; AL133620; CAB63746.1; -; mRNA.
EMBL; AL137553; CAB70807.1; -; mRNA.
EMBL; BX640878; CAE45935.1; -; mRNA.
EMBL; BC094714; AAH94714.1; -; mRNA.
EMBL; BC130610; AAI30611.1; -; mRNA.
CCDS; CCDS42650.1; -. [Q9ULH0-1]
PIR; T43458; T43458.
RefSeq; NP_065789.1; NM_020738.2. [Q9ULH0-1]
UniGene; Hs.467627; -.
UniGene; Hs.593330; -.
UniGene; Hs.9873; -.
ProteinModelPortal; Q9ULH0; -.
SMR; Q9ULH0; -.
BioGrid; 121565; 63.
IntAct; Q9ULH0; 40.
MINT; MINT-1390552; -.
STRING; 9606.ENSP00000256707; -.
iPTMnet; Q9ULH0; -.
PhosphoSitePlus; Q9ULH0; -.
SwissPalm; Q9ULH0; -.
BioMuta; KIDINS220; -.
DMDM; 172044825; -.
EPD; Q9ULH0; -.
PaxDb; Q9ULH0; -.
PeptideAtlas; Q9ULH0; -.
PRIDE; Q9ULH0; -.
Ensembl; ENST00000256707; ENSP00000256707; ENSG00000134313. [Q9ULH0-1]
Ensembl; ENST00000319688; ENSP00000319947; ENSG00000134313. [Q9ULH0-3]
Ensembl; ENST00000473731; ENSP00000418974; ENSG00000134313. [Q9ULH0-4]
GeneID; 57498; -.
KEGG; hsa:57498; -.
UCSC; uc002qzc.2; human. [Q9ULH0-1]
CTD; 57498; -.
DisGeNET; 57498; -.
EuPathDB; HostDB:ENSG00000134313.14; -.
GeneCards; KIDINS220; -.
HGNC; HGNC:29508; KIDINS220.
HPA; HPA014790; -.
MIM; 615759; gene.
MIM; 617296; phenotype.
neXtProt; NX_Q9ULH0; -.
OpenTargets; ENSG00000134313; -.
PharmGKB; PA164721911; -.
eggNOG; KOG0502; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00900000140807; -.
InParanoid; Q9ULH0; -.
KO; K12460; -.
OMA; TQGKKKW; -.
OrthoDB; EOG091G01EB; -.
PhylomeDB; Q9ULH0; -.
TreeFam; TF344032; -.
Reactome; R-HSA-170984; ARMS-mediated activation.
SignaLink; Q9ULH0; -.
SIGNOR; Q9ULH0; -.
ChiTaRS; KIDINS220; human.
GeneWiki; KIDINS220; -.
GenomeRNAi; 57498; -.
PRO; PR:Q9ULH0; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000134313; -.
ExpressionAtlas; Q9ULH0; baseline and differential.
Genevisible; Q9ULH0; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; IBA:GO_Central.
CDD; cd00204; ANK; 3.
Gene3D; 1.25.40.20; -; 4.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011646; KAP_P-loop.
InterPro; IPR013761; SAM/pointed.
Pfam; PF12796; Ank_2; 4.
Pfam; PF07693; KAP_NTPase; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 11.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 10.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Complete proteome; Disease mutation;
Endosome; Hereditary spastic paraplegia; Membrane; Mental retardation;
Neurodegeneration; Neurogenesis; Obesity; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transmembrane;
Transmembrane helix.
CHAIN 1 1771 Kinase D-interacting substrate of 220
kDa.
/FTId=PRO_0000322119.
TOPO_DOM 1 499 Cytoplasmic. {ECO:0000255}.
TRANSMEM 500 520 Helical. {ECO:0000255}.
TOPO_DOM 521 524 Extracellular. {ECO:0000255}.
TRANSMEM 525 545 Helical. {ECO:0000255}.
TOPO_DOM 546 659 Cytoplasmic. {ECO:0000255}.
TRANSMEM 660 680 Helical. {ECO:0000255}.
TOPO_DOM 681 685 Extracellular. {ECO:0000255}.
TRANSMEM 686 706 Helical. {ECO:0000255}.
TOPO_DOM 707 1771 Cytoplasmic. {ECO:0000255}.
REPEAT 4 33 ANK 1.
REPEAT 37 66 ANK 2.
REPEAT 70 99 ANK 3.
REPEAT 103 132 ANK 4.
REPEAT 136 165 ANK 5.
REPEAT 169 198 ANK 6.
REPEAT 202 231 ANK 7.
REPEAT 235 264 ANK 8.
REPEAT 268 297 ANK 9.
REPEAT 301 330 ANK 10.
REPEAT 334 363 ANK 11.
REPEAT 367 396 ANK 12.
DOMAIN 440 953 KAP NTPase.
REGION 1089 1092 Mediates interaction with CRKL.
{ECO:0000250}.
REGION 1767 1771 Mediates interaction with SNTA1.
{ECO:0000250}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 885 885 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 914 914 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 918 918 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1163 1163 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1296 1296 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1352 1352 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1359 1359 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1361 1361 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1362 1362 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1365 1365 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1521 1521 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1526 1526 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1555 1555 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1574 1574 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1623 1623 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1633 1633 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1679 1679 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1681 1681 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1684 1684 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1228 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_031861.
VAR_SEQ 1 42 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031862.
VAR_SEQ 135 135 L -> LQ (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_031863.
VAR_SEQ 1005 1030 ISKNIPTTKDVEPLLEIDGDIRNFEV -> CCGADSCDRDR
IGISKSVLVAMLMES (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_031864.
VAR_SEQ 1031 1771 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_031865.
VAR_SEQ 1138 1194 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031866.
VAR_SEQ 1177 1195 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_031867.
VARIANT 538 538 I -> T (in dbSNP:rs2289229).
/FTId=VAR_048285.
VARIANT 1307 1307 R -> H (in dbSNP:rs2304591).
/FTId=VAR_039399.
VARIANT 1350 1771 Missing (in SINO; no effect on protein
abundance).
{ECO:0000269|PubMed:27005418}.
/FTId=VAR_077995.
VARIANT 1366 1771 Missing (in SINO; no effect on protein
abundance; no effect on subcellular
localization).
{ECO:0000269|PubMed:27005418}.
/FTId=VAR_077996.
VARIANT 1608 1608 Q -> H (in dbSNP:rs1044280).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_039400.
CONFLICT 1335 1335 T -> P (in Ref. 4; CAE45935).
{ECO:0000305}.
CONFLICT 1613 1613 N -> D (in Ref. 3; BAB14285).
{ECO:0000305}.
SEQUENCE 1771 AA; 196542 MW; FD1F99DB88B6996D CRC64;
MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMIAAEQGN LEIVKELIKN
GANCNLEDLD NWTALISASK EGHVHIVEEL LKCGVNLEHR DMGGWTALMW ACYKGRTDVV
ELLLSHGANP SVTGLYSVYP IIWAAGRGHA DIVHLLLQNG AKVNCSDKYG TTPLVWAARK
GHLECVKHLL AMGADVDQEG ANSMTALIVA VKGGYTQSVK EILKRNPNVN LTDKDGNTAL
MIASKEGHTE IVQDLLDAGT YVNIPDRSGD TVLIGAVRGG HVEIVRALLQ KYADIDIRGQ
DNKTALYWAV EKGNATMVRD ILQCNPDTEI CTKDGETPLI KATKMRNIEV VELLLDKGAK
VSAVDKKGDT PLHIAIRGRS RKLAELLLRN PKDGRLLYRP NKAGETPYNI DCSHQKSILT
QIFGARHLSP TETDGDMLGY DLYSSALADI LSEPTMQPPI CVGLYAQWGS GKSFLLKKLE
DEMKTFAGQQ IEPLFQFSWL IVFLTLLLCG GLGLLFAFTV HPNLGIAVSL SFLALLYIFF
IVIYFGGRRE GESWNWAWVL STRLARHIGY LELLLKLMFV NPPELPEQTT KALPVRFLFT
DYNRLSSVGG ETSLAEMIAT LSDACEREFG FLATRLFRVF KTEDTQGKKK WKKTCCLPSF
VIFLFIIGCI ISGITLLAIF RVDPKHLTVN AVLISIASVV GLAFVLNCRT WWQVLDSLLN
SQRKRLHNAA SKLHKLKSEG FMKVLKCEVE LMARMAKTID SFTQNQTRLV VIIDGLDACE
QDKVLQMLDT VRVLFSKGPF IAIFASDPHI IIKAINQNLN SVLRDSNING HDYMRNIVHL
PVFLNSRGLS NARKFLVTSA TNGDVPCSDT TGIQEDADRR VSQNSLGEMT KLGSKTALNR
RDTYRRRQMQ RTITRQMSFD LTKLLVTEDW FSDISPQTMR RLLNIVSVTG RLLRANQISF
NWDRLASWIN LTEQWPYRTS WLILYLEETE GIPDQMTLKT IYERISKNIP TTKDVEPLLE
IDGDIRNFEV FLSSRTPVLV ARDVKVFLPC TVNLDPKLRE IIADVRAARE QISIGGLAYP
PLPLHEGPPR APSGYSQPPS VCSSTSFNGP FAGGVVSPQP HSSYYSGMTG PQHPFYNRPF
FAPYLYTPRY YPGGSQHLIS RPSVKTSLPR DQNNGLEVIK EDAAEGLSSP TDSSRGSGPA
PGPVVLLNSL NVDAVCEKLK QIEGLDQSML PQYCTTIKKA NINGRVLAQC NIDELKKEMN
MNFGDWHLFR STVLEMRNAE SHVVPEDPRF LSESSSGPAP HGEPARRASH NELPHTELSS
QTPYTLNFSF EELNTLGLDE GAPRHSNLSW QSQTRRTPSL SSLNSQDSSI EISKLTDKVQ
AEYRDAYREY IAQMSQLEGG PGSTTISGRS SPHSTYYMGQ SSSGGSIHSN LEQEKGKDSE
PKPDDGRKSF LMKRGDVIDY SSSGVSTNDA SPLDPITEED EKSDQSGSKL LPGKKSSERS
SLFQTDLKLK GSGLRYQKLP SDEDESGTEE SDNTPLLKDD KDRKAEGKVE RVPKSPEHSA
EPIRTFIKAK EYLSDALLDK KDSSDSGVRS SESSPNHSLH NEVADDSQLE KANLIELEDD
SHSGKRGIPH SLSGLQDPII ARMSICSEDK KSPSECSLIA SSPEENWPAC QKAYNLNRTP
STVTLNNNSA PANRANQNFD EMEGIRETSQ VILRPSSSPN PTTIQNENLK SMTHKRSQRS
SYTRLSKDPP ELHAAASSES TGFGEERESI L


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