TM1L1_HUMAN
ID TM1L1_HUMAN Reviewed; 476 AA.
AC O75674; B7Z9E2; Q53G06; Q8N749;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=TOM1-like protein 1;
DE AltName: Full=Src-activating and signaling molecule protein;
DE AltName: Full=Target of Myb-like protein 1;
GN Name=TOM1L1; Synonyms=SRCASM;
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] (ISOFORM 1).
RX PubMed=10329004; DOI=10.1006/geno.1998.5739;
RA Seroussi E., Kedra D., Kost-Alimova M., Sandberg-Nordqvist A.-C.,
RA Fransson I., Jacobs J.F.M., Fu Y., Pan H.-Q., Roe B.A., Imreh S.,
RA Dumanski J.P.;
RT "TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and
RT encode proteins similar to the endosomal proteins HGS and STAM.";
RL Genomics 57:380-388(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Adrenal gland, and Trachea;
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 MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-323, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-323, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-323, AND
RP IDENTIFICATION BY MASS 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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 9-150.
RG Northeast structural genomics consortium (NESG);
RT "X-ray crystal structure of the VHS domain of human TOM1-like protein,
RT Northeast structural genomics consortium target HR3050E.";
RL Submitted (JUN-2011) to the PDB data bank.
CC -!- FUNCTION: Probable adapter protein involved in signaling pathways.
CC Interacts with the SH2 and SH3 domains of various signaling proteins
CC when it is phosphorylated. May promote FYN activation, possibly by
CC disrupting intramolecular SH3-dependent interactions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FYN, GRB2 and PIK3R1 when phosphorylated.
CC Interacts with LYN. {ECO:0000250}.
CC -!- INTERACTION:
CC O75674; Q00610: CLTC; NbExp=4; IntAct=EBI-712991, EBI-354967;
CC O75674; P00533: EGFR; NbExp=6; IntAct=EBI-712991, EBI-297353;
CC O75674; P62993: GRB2; NbExp=2; IntAct=EBI-712991, EBI-401755;
CC O75674; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-712991, EBI-74615;
CC O75674; O60784: TOM1; NbExp=2; IntAct=EBI-712991, EBI-74634;
CC O75674; P52735: VAV2; NbExp=2; IntAct=EBI-712991, EBI-297549;
CC O75674-2; P59910: DNAJB13; NbExp=3; IntAct=EBI-12011552, EBI-11514233;
CC O75674-2; Q9H0E2: TOLLIP; NbExp=5; IntAct=EBI-12011552, EBI-74615;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endosome membrane
CC {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=A small proportion is membrane-associated.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75674-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75674-2; Sequence=VSP_056852, VSP_056853;
CC Name=3;
CC IsoId=O75674-3; Sequence=VSP_057424;
CC -!- PTM: Phosphorylated on tyrosines by FYN and LYN. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
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DR EMBL; AJ010071; CAA08993.1; -; mRNA.
DR EMBL; AK315039; BAG37522.1; -; mRNA.
DR EMBL; AK315907; BAH14278.1; -; mRNA.
DR EMBL; AK223125; BAD96845.1; -; mRNA.
DR EMBL; AC007485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94551.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94553.1; -; Genomic_DNA.
DR EMBL; BC029396; AAH29396.1; -; mRNA.
DR CCDS; CCDS11582.1; -. [O75674-1]
DR CCDS; CCDS82160.1; -. [O75674-2]
DR CCDS; CCDS82161.1; -. [O75674-3]
DR RefSeq; NP_001308102.1; NM_001321173.1. [O75674-2]
DR RefSeq; NP_001308103.1; NM_001321174.1. [O75674-3]
DR RefSeq; NP_001308104.1; NM_001321175.1. [O75674-3]
DR RefSeq; NP_001308105.1; NM_001321176.1. [O75674-3]
DR RefSeq; NP_005477.2; NM_005486.2. [O75674-1]
DR RefSeq; XP_016879491.1; XM_017024002.1. [O75674-3]
DR PDB; 3RRU; X-ray; 3.00 A; A/B=9-150.
DR PDBsum; 3RRU; -.
DR AlphaFoldDB; O75674; -.
DR SMR; O75674; -.
DR BioGRID; 115352; 80.
DR ELM; O75674; -.
DR IntAct; O75674; 44.
DR MINT; O75674; -.
DR STRING; 9606.ENSP00000460823; -.
DR MoonDB; O75674; Predicted.
DR iPTMnet; O75674; -.
DR PhosphoSitePlus; O75674; -.
DR BioMuta; TOM1L1; -.
DR CPTAC; CPTAC-284; -.
DR CPTAC; CPTAC-285; -.
DR EPD; O75674; -.
DR jPOST; O75674; -.
DR MassIVE; O75674; -.
DR MaxQB; O75674; -.
DR PaxDb; O75674; -.
DR PeptideAtlas; O75674; -.
DR PRIDE; O75674; -.
DR ProteomicsDB; 50148; -. [O75674-1]
DR ProteomicsDB; 7027; -.
DR ProteomicsDB; 72262; -.
DR Antibodypedia; 18249; 256 antibodies from 34 providers.
DR DNASU; 10040; -.
DR Ensembl; ENST00000348161.8; ENSP00000343901.4; ENSG00000141198.16. [O75674-3]
DR Ensembl; ENST00000536554.5; ENSP00000443099.1; ENSG00000141198.16. [O75674-3]
DR Ensembl; ENST00000570371.5; ENSP00000458553.1; ENSG00000141198.16. [O75674-2]
DR Ensembl; ENST00000575333.5; ENSP00000458918.1; ENSG00000141198.16. [O75674-2]
DR Ensembl; ENST00000575882.6; ENSP00000460823.1; ENSG00000141198.16. [O75674-1]
DR GeneID; 10040; -.
DR KEGG; hsa:10040; -.
DR MANE-Select; ENST00000575882.6; ENSP00000460823.1; NM_005486.3; NP_005477.2.
DR UCSC; uc002iuc.4; human. [O75674-1]
DR UCSC; uc010dbz.3; human.
DR CTD; 10040; -.
DR DisGeNET; 10040; -.
DR GeneCards; TOM1L1; -.
DR HGNC; HGNC:11983; TOM1L1.
DR HPA; ENSG00000141198; Low tissue specificity.
DR MIM; 604701; gene.
DR neXtProt; NX_O75674; -.
DR OpenTargets; ENSG00000141198; -.
DR PharmGKB; PA36667; -.
DR VEuPathDB; HostDB:ENSG00000141198; -.
DR eggNOG; KOG1087; Eukaryota.
DR GeneTree; ENSGT00940000160240; -.
DR HOGENOM; CLU_043812_0_0_1; -.
DR InParanoid; O75674; -.
DR OMA; HHHKGAQ; -.
DR OrthoDB; 594067at2759; -.
DR PhylomeDB; O75674; -.
DR TreeFam; TF314105; -.
DR PathwayCommons; O75674; -.
DR SignaLink; O75674; -.
DR SIGNOR; O75674; -.
DR BioGRID-ORCS; 10040; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; TOM1L1; human.
DR GeneWiki; TOM1L1; -.
DR GenomeRNAi; 10040; -.
DR Pharos; O75674; Tbio.
DR PRO; PR:O75674; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75674; protein.
DR Bgee; ENSG00000141198; Expressed in jejunal mucosa and 163 other tissues.
DR ExpressionAtlas; O75674; baseline and differential.
DR Genevisible; O75674; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; TAS:HGNC-UCL.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IDA:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; NAS:HGNC-UCL.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR014645; TOM1.
DR InterPro; IPR027428; TOM1L1.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR13856:SF28; PTHR13856:SF28; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR PIRSF; PIRSF036948; TOM1; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endosome; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW SH3-binding; Transport.
FT CHAIN 1..476
FT /note="TOM1-like protein 1"
FT /id="PRO_0000072566"
FT DOMAIN 22..154
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 200..288
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 155..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..395
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="Interaction with PIK3R1"
FT /evidence="ECO:0000250"
FT MOTIF 421..425
FT /note="SH3-binding"
FT /evidence="ECO:0000250"
FT MOTIF 460..463
FT /note="SH2-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 162..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923U0"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 460
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q923U0"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057424"
FT VAR_SEQ 345..346
FT /note="NF -> SK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056852"
FT VAR_SEQ 347..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056853"
FT VARIANT 108
FT /note="R -> S (in dbSNP:rs16955377)"
FT /id="VAR_047469"
FT CONFLICT 48
FT /note="G -> A (in Ref. 1; CAA08993)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:3RRU"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:3RRU"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3RRU"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:3RRU"
SQ SEQUENCE 476 AA; 52989 MW; 47ED5FA1F40144C0 CRC64;
MAFGKSHRDP YATSVGHLIE KATFAGVQTE DWGQFMHICD IINTTQDGPK DAVKALKKRI
SKNYNHKEIQ LTLSLIDMCV QNCGPSFQSL IVKKEFVKEN LVKLLNPRYN LPLDIQNRIL
NFIKTWSQGF PGGVDVSEVK EVYLDLVKKG VQFPPSEAEA ETARQETAQI SSNPPTSVPT
APALSSVIAP KNSTVTLVPE QIGKLHSELD MVKMNVRVMS AILMENTPGS ENHEDIELLQ
KLYKTGREMQ ERIMDLLVVV ENEDVTVELI QVNEDLNNAI LGYERFTRNQ QRILEQNKNQ
KEATNTTSEP SAPSQDLLDL SPSPRMPRAT LGELNTMNNQ LSGLNFSLPS SDVTNNLKPS
LHPQMNLLAL ENTEIPPFAQ RTSQNLTSSH AYDNFLEHSN SVFLQPVSLQ TIAAAPSNQS
LPPLPSNHPA MTKSDLQPPN YYEVMEFDPL APAVTTEAIY EEIDAHQHKG AQNDGD
