SRCN1_HUMAN
ID SRCN1_HUMAN Reviewed; 1183 AA.
AC Q9C0H9; Q75T46; Q8N4W8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=SRC kinase signaling inhibitor 1 {ECO:0000305};
DE AltName: Full=SNAP-25-interacting protein;
DE Short=SNIP {ECO:0000303|PubMed:19146815};
DE AltName: Full=p130Cas-associated protein;
DE AltName: Full=p140Cap;
GN Name=SRCIN1 {ECO:0000312|HGNC:HGNC:29506};
GN Synonyms=KIAA1684, P140 {ECO:0000303|PubMed:19146815},
GN SNIP {ECO:0000303|PubMed:19146815};
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 {ECO:0000312|EMBL:BAB21775.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Sugiyama A., Inoue H., Oka M.;
RT "Homo sapiens cDNA, SNIP homolog.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-1183 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 434-453; 620-647; 711-721; 739-745; 828-847; 969-995;
RP 1012-1023; 1085-1100; 1111-1128 AND 1134-1145 (ISOFORM 1), FUNCTION,
RP SUBCELLULAR LOCATION, INTERACTION WITH BCAR1, AND PHOSPHORYLATION.
RX PubMed=14657239; DOI=10.1091/mbc.e03-09-0689;
RA Di Stefano P., Cabodi S., Erba E.B., Margaria V., Bergatto E.,
RA Giuffrida M.G., Silengo L., Tarone G., Turco E., Defilippi P.;
RT "p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated
RT protein involved in cell spreading.";
RL Mol. Biol. Cell 15:787-800(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH CSK AND SRC.
RX PubMed=17525734; DOI=10.1038/sj.emboj.7601724;
RA Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L., Praduroux A.,
RA Piva R., Cavallo F., Forni G., Silengo L., Tarone G., Turco E.,
RA Defilippi P.;
RT "p140Cap protein suppresses tumour cell properties, regulating Csk and Src
RT kinase activity.";
RL EMBO J. 26:2843-2855(2007).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=18475297; DOI=10.1038/sj.bjc.6604365;
RA Kennedy S., Clynes M., Doolan P., Mehta J.P., Rani S., Crown J.,
RA O'Driscoll L.;
RT "SNIP/p140Cap mRNA expression is an unfavourable prognostic factor in
RT breast cancer and is not expressed in normal breast tissue.";
RL Br. J. Cancer 98:1641-1645(2008).
RN [9]
RP INTERACTION WITH SORBS3 AND SYP.
RX PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x;
RA Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R.,
RA Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.;
RT "Characterization of a multidomain adaptor protein, p140Cap, as part of a
RT pre-synaptic complex.";
RL J. Neurochem. 107:61-72(2008).
RN [10]
RP FUNCTION, INTERACTION WITH CTTN AND MAPRE3, AND SUBCELLULAR LOCATION.
RX PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT plasticity.";
RL Neuron 61:85-100(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-52; SER-53; SER-64;
RP SER-364; SER-857; SER-866 AND THR-884, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Acts as a negative regulator of SRC by activating CSK which
CC inhibits SRC activity and downstream signaling, leading to impaired
CC cell spreading and migration. Regulates dendritic spine morphology.
CC Involved in calcium-dependent exocytosis. May play a role in
CC neurotransmitter release or synapse maintenance.
CC {ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:17525734,
CC ECO:0000269|PubMed:19146815}.
CC -!- SUBUNIT: Interacts with the N-terminal coiled-coil region of SNAP25 (By
CC similarity). Interacts with BCAR1/p130Cas and SRC through its C-
CC terminal domain. Interacts with CSK, CTTN, SORBS3/vinexin, SYP and
CC MAPRE3/EB3. {ECO:0000250, ECO:0000269|PubMed:14657239,
CC ECO:0000269|PubMed:17525734, ECO:0000269|PubMed:18662323,
CC ECO:0000269|PubMed:19146815}.
CC -!- INTERACTION:
CC Q9C0H9; P56945: BCAR1; NbExp=3; IntAct=EBI-1393949, EBI-702093;
CC Q9C0H9; P12931: SRC; NbExp=3; IntAct=EBI-1393949, EBI-621482;
CC Q9C0H9-4; Q99732: LITAF; NbExp=3; IntAct=EBI-25907611, EBI-725647;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QXY2}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXY2}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q9QXY2}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q9QXY2}. Presynapse
CC {ECO:0000250|UniProtKB:Q9QXY2}. Postsynapse
CC {ECO:0000250|UniProtKB:Q9QXY2}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9QXY2}. Note=Localized to the perinuclear
CC region, lamellopodia, cortical actin and actin stress fibers but not to
CC focal adhesions. Strongly expressed in axons and dendrites of the CA1
CC and CA3 hippocampal regions and of the dentate gyrus. Detected in both
CC presynapses and postsynapses and enriched in postsynaptic density
CC fractions. {ECO:0000250|UniProtKB:Q9QXY2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C0H9-5; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q9C0H9-2; Sequence=VSP_059451, VSP_059454;
CC Name=3;
CC IsoId=Q9C0H9-4; Sequence=VSP_059450, VSP_059452, VSP_059453;
CC -!- TISSUE SPECIFICITY: Expressed in some primary breast carcinomas where
CC its presence is significantly associated with increased tumor size. Not
CC detected in normal breast tissue. {ECO:0000269|PubMed:18475297}.
CC -!- PTM: Tyrosine-phosphorylated in response to EGF and to cell adhesion to
CC integrin ligands. {ECO:0000269|PubMed:14657239}.
CC -!- SIMILARITY: Belongs to the SRCIN1 family. {ECO:0000305}.
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DR EMBL; AB127405; BAD03968.1; -; mRNA.
DR EMBL; AK126665; BAC86634.1; -; mRNA.
DR EMBL; AC006449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC244153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033233; AAH33233.1; -; mRNA.
DR EMBL; AB051471; BAB21775.1; -; mRNA.
DR CCDS; CCDS45660.1; -. [Q9C0H9-5]
DR RefSeq; NP_079524.2; NM_025248.2. [Q9C0H9-5]
DR AlphaFoldDB; Q9C0H9; -.
DR SMR; Q9C0H9; -.
DR BioGRID; 123275; 22.
DR ELM; Q9C0H9; -.
DR IntAct; Q9C0H9; 8.
DR MINT; Q9C0H9; -.
DR STRING; 9606.ENSP00000484715; -.
DR BindingDB; Q9C0H9; -.
DR ChEMBL; CHEMBL2150836; -.
DR GlyGen; Q9C0H9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9C0H9; -.
DR PhosphoSitePlus; Q9C0H9; -.
DR BioMuta; SRCIN1; -.
DR DMDM; 296452948; -.
DR EPD; Q9C0H9; -.
DR jPOST; Q9C0H9; -.
DR MassIVE; Q9C0H9; -.
DR MaxQB; Q9C0H9; -.
DR PaxDb; Q9C0H9; -.
DR PeptideAtlas; Q9C0H9; -.
DR PRIDE; Q9C0H9; -.
DR ProteomicsDB; 80047; -. [Q9C0H9-2]
DR ProteomicsDB; 80048; -. [Q9C0H9-4]
DR ProteomicsDB; 80049; -. [Q9C0H9-5]
DR Antibodypedia; 74250; 74 antibodies from 21 providers.
DR DNASU; 80725; -.
DR Ensembl; ENST00000615049.4; ENSP00000480869.1; ENSG00000273608.4. [Q9C0H9-5]
DR Ensembl; ENST00000617146.5; ENSP00000484715.1; ENSG00000277363.5. [Q9C0H9-5]
DR GeneID; 80725; -.
DR KEGG; hsa:80725; -.
DR MANE-Select; ENST00000617146.5; ENSP00000484715.1; NM_025248.3; NP_079524.2.
DR CTD; 80725; -.
DR DisGeNET; 80725; -.
DR GeneCards; SRCIN1; -.
DR HGNC; HGNC:29506; SRCIN1.
DR HPA; ENSG00000277363; Tissue enriched (brain).
DR MIM; 610786; gene.
DR neXtProt; NX_Q9C0H9; -.
DR OpenTargets; ENSG00000277363; -.
DR PharmGKB; PA165432823; -.
DR VEuPathDB; HostDB:ENSG00000277363; -.
DR eggNOG; ENOG502QPNH; Eukaryota.
DR GeneTree; ENSGT00940000157961; -.
DR InParanoid; Q9C0H9; -.
DR OMA; FRMAPSS; -.
DR OrthoDB; 65773at2759; -.
DR PhylomeDB; Q9C0H9; -.
DR TreeFam; TF332255; -.
DR PathwayCommons; Q9C0H9; -.
DR SignaLink; Q9C0H9; -.
DR SIGNOR; Q9C0H9; -.
DR BioGRID-ORCS; 80725; 19 hits in 1065 CRISPR screens.
DR ChiTaRS; SRCIN1; human.
DR GenomeRNAi; 80725; -.
DR Pharos; Q9C0H9; Tbio.
DR PRO; PR:Q9C0H9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9C0H9; protein.
DR Bgee; ENSG00000277363; Expressed in C1 segment of cervical spinal cord and 93 other tissues.
DR ExpressionAtlas; Q9C0H9; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR InterPro; IPR022782; AIP3-like_C.
DR InterPro; IPR026727; Srcin1.
DR PANTHER; PTHR22741:SF5; PTHR22741:SF5; 1.
DR Pfam; PF03915; AIP3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Exocytosis; Methylation;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1183
FT /note="SRC kinase signaling inhibitor 1"
FT /id="PRO_0000072011"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..697
FT /note="Interaction with SNAP25"
FT /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT REGION 861..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 654..674
FT /evidence="ECO:0000255"
FT COILED 726..746
FT /evidence="ECO:0000255"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 241
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 329
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 336
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 396
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 501
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 624
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 637
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 884
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT VAR_SEQ 1..694
FT /note="Missing (in isoform 3)"
FT /id="VSP_059450"
FT VAR_SEQ 1..180
FT /note="MGNAPSQDPERSSPPMLSADDAEYPREYRTLGGGGGGGSGGRRFSNVGLVHT
FT SERRHTVIAAQSLEALSGLQKADADRKRDAFMDHLKSKYPQHALALRGQQDRMREQPNY
FT WSFKTRSSRHTQGAQPGLADQAAKLSYASAESLETMSEAELPLGFSRMNRFRQSLPLSR
FT SASQTKLRSP -> MRGAWVHLHSGAASSLRPCRCGAGAAPKSSPRSPGGRRGDGSSDS
FT EGGVSFA (in isoform 2)"
FT /id="VSP_059451"
FT VAR_SEQ 910..951
FT /note="AAERDWEEKRAALTQYSAKDINRLLEETQAELLKAIPDLDCA -> VLGPGI
FT VGGAMSQVHTFLRPSFLEWGVPILWVFFLGGGGPVP (in isoform 3)"
FT /id="VSP_059452"
FT VAR_SEQ 952..1183
FT /note="Missing (in isoform 3)"
FT /id="VSP_059453"
FT VAR_SEQ 1141..1183
FT /note="Missing (in isoform 2)"
FT /id="VSP_059454"
FT CONFLICT 177
FT /note="L -> P (in Ref. 1; BAD03968)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="Missing (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="T -> I (in Ref. 2; BAC86634)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="L -> I (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="V -> M (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 841..842
FT /note="LS -> IN (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 971
FT /note="H -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="R -> K (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="Y -> R (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1086
FT /note="I -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1115
FT /note="Q -> P (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1122
FT /note="S -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="A -> V (in Ref. 2; BAC86634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1183 AA; 127105 MW; 52BF566E715EF6FF CRC64;
MGNAPSQDPE RSSPPMLSAD DAEYPREYRT LGGGGGGGSG GRRFSNVGLV HTSERRHTVI
AAQSLEALSG LQKADADRKR DAFMDHLKSK YPQHALALRG QQDRMREQPN YWSFKTRSSR
HTQGAQPGLA DQAAKLSYAS AESLETMSEA ELPLGFSRMN RFRQSLPLSR SASQTKLRSP
GVLFLQFGEE TRRVHITHEV SSLDTLHALI AHMFPQKLTM GMLKSPNTAI LIKDEARNVF
YELEDVRDIQ DRSIIKIYRK EPLYAAFPGS HLTNGDLRRE MVYASRESSP TRRLNNLSPA
PHLASGSPPP GLPSGLPSGL QSGSPSRSRL SYAGGRPPSY AGSPVHHAAE RLGGAPAAQG
VSPSPSAILE RRDVKPDEDL ASKAGGMVLV KGEGLYADPY GLLHEGRLSL AAAAGDPFAY
PGAGGLYKRG SVRSLSTYSA AALQSDLEDS LYKAAGGGGP LYGDGYGFRL PPSSPQKLAD
VAAPPGGPPP PHSPYSGPPS RGSPVRQSFR KDSGSSSVFA ESPGGKTRSA GSASTAGAPP
SELFPGPGER SLVGFGPPVP AKDTETRERM EAMEKQIASL TGLVQSALLR GSEPETPSEK
IEGSNGAATP SAPCGSGGRS SGATPVSGPP PPSASSTPAG QPTAVSRLQM QLHLRGLQNS
ASDLRGQLQQ LRKLQLQNQE SVRALLKRTE AELSMRVSEA ARRQEDPLQR QRTLVEEERL
RYLNDEELIT QQLNDLEKSV EKIQRDVSHN HRLVPGPELE EKALVLKQLG ETLTELKAHF
PGLQSKMRVV LRVEVEAVKF LKEEPQRLDG LLKRCRGVTD TLAQIRRQVD EGVWPPPNNL
LSQSPKKVTA ETDFNKSVDF EMPPPSPPLN LHELSGPAEG ASLTPKGGNP TKGLDTPGKR
SVDKAVSVEA AERDWEEKRA ALTQYSAKDI NRLLEETQAE LLKAIPDLDC ASKAHPGPAP
TPDHKPPKAP HGQKAAPRTE PSGRRGSDEL TVPRYRTEKP SKSPPPPPPR RSFPSSHGLT
TTRTGEVVVT SKKDSAFIKK AESEELEVQK PQVKLRRAVS EVARPASTPP IMASAIKDED
DEDRIIAELE SGGGSVPPMK VVTPGASRLK AAQGQAGSPD KSKHGKQRAE YMRIQAQQQA
TKPSKEMSGS NETSSPVSEK PSASRTSIPV LTSFGARNSS ISF
