ASPC1_HUMAN
ID ASPC1_HUMAN Reviewed; 553 AA.
AC Q9BZE9; A8K3K9; Q7Z6N7; Q8WV59; Q96LS5; Q96M40;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Tether containing UBX domain for GLUT4;
DE AltName: Full=Alveolar soft part sarcoma chromosomal region candidate gene 1 protein;
DE AltName: Full=Alveolar soft part sarcoma locus;
DE AltName: Full=Renal papillary cell carcinoma protein 17;
DE AltName: Full=UBX domain-containing protein 9;
GN Name=ASPSCR1; Synonyms=ASPL, RCC17, TUG, UBXD9, UBXN9;
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), CHROMOSOMAL TRANSLOCATION WITH
RP TFE3, TISSUE SPECIFICITY, AND INVOLVEMENT IN ASPS.
RX PubMed=11244503; DOI=10.1038/sj.onc.1204074;
RA Ladanyi M., Lui M.Y., Antonescu C.R., Krause-Boehm A., Meindl A.,
RA Argani P., Healey J.H., Ueda T., Yoshikawa H., Meloni-Ehrig A.,
RA Sorensen P.H.B., Mertens F., Mandahl N., van den Berghe H., Sciot R.,
RA Dal Cin P., Bridge J.;
RT "The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses the
RT TFE3 transcription factor gene to ASPL, a novel gene at 17q25.";
RL Oncogene 20:48-57(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP GLN-252.
RC TISSUE=Brain, Heart, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP GLN-252.
RC TISSUE=Eye, and Skin;
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 [4]
RP CHROMOSOMAL TRANSLOCATION WITH TFE3, AND TISSUE SPECIFICITY.
RX PubMed=11358836;
RA Heimann P., El Housni H., Ogur G., Weterman M.A.J., Petty E.M., Vassart G.;
RT "Fusion of a novel gene, RCC17, to the TFE3 gene in t(X;17)(p11.2;q25.3)-
RT bearing papillary renal cell carcinomas.";
RL Cancer Res. 61:4130-4135(2001).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VCP.
RX PubMed=22207755; DOI=10.1074/jbc.m111.284232;
RA Orme C.M., Bogan J.S.;
RT "The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates
RT the p97 ATPase and resides at the endoplasmic reticulum-golgi intermediate
RT compartment.";
RL J. Biol. Chem. 287:6679-6692(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-500 AND SER-502, AND
RP IDENTIFICATION BY 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 [12]
RP FUNCTION IN VCP METHYLATION, INTERACTION WITH VCPKMT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-500 AND SER-502, 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).
CC -!- FUNCTION: Tethering protein that sequesters GLUT4-containing vesicles
CC in the cytoplasm in the absence of insulin. Modulates the amount of
CC GLUT4 that is available at the cell surface (By similarity). Enhances
CC VCP methylation catalyzed by VCPKMT. {ECO:0000250,
CC ECO:0000269|PubMed:23349634}.
CC -!- SUBUNIT: Interacts with GLUT4 (By similarity). Interacts with VCPKMT.
CC Interacts with VCP. {ECO:0000250, ECO:0000269|PubMed:22207755,
CC ECO:0000269|PubMed:23349634}.
CC -!- INTERACTION:
CC Q9BZE9; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1993677, EBI-10173507;
CC Q9BZE9; P49760: CLK2; NbExp=3; IntAct=EBI-1993677, EBI-750020;
CC Q9BZE9; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-1993677, EBI-10175326;
CC Q9BZE9; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1993677, EBI-6509505;
CC Q9BZE9; Q15323: KRT31; NbExp=3; IntAct=EBI-1993677, EBI-948001;
CC Q9BZE9; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1993677, EBI-11959885;
CC Q9BZE9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1993677, EBI-10171774;
CC Q9BZE9; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-1993677, EBI-945833;
CC Q9BZE9; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-1993677, EBI-2554984;
CC Q9BZE9; P15884: TCF4; NbExp=3; IntAct=EBI-1993677, EBI-533224;
CC Q9BZE9; P55072: VCP; NbExp=28; IntAct=EBI-1993677, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000269|PubMed:22207755};
CC Peripheral membrane protein. Cytoplasm {ECO:0000269|PubMed:23349634}.
CC Nucleus {ECO:0000269|PubMed:23349634}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BZE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZE9-2; Sequence=VSP_020578;
CC Name=3;
CC IsoId=Q9BZE9-3; Sequence=VSP_020574, VSP_020577;
CC Name=4;
CC IsoId=Q9BZE9-4; Sequence=VSP_020574, VSP_020575, VSP_020576;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis, heart,
CC skeletal muscle and pancreas. {ECO:0000269|PubMed:11244503,
CC ECO:0000269|PubMed:11358836}.
CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 is found in
CC patients with alveolar soft part sarcoma. Translocation
CC t(X;17)(p11;q25) with TFE3 forms a ASPSCR1-TFE3 fusion protein.
CC {ECO:0000269|PubMed:11244503}.
CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 has been found
CC in two patients with of papillary renal cell carcinoma. Translocation
CC t(X;17)(p11.2;q25). {ECO:0000269|PubMed:11358836}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ASPSCR1ID358.html";
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DR EMBL; AF324219; AAK08959.2; -; mRNA.
DR EMBL; AK057403; BAB71472.1; -; mRNA.
DR EMBL; AK057851; BAB71595.1; -; mRNA.
DR EMBL; AK290624; BAF83313.1; -; mRNA.
DR EMBL; BC006152; AAH06152.1; -; mRNA.
DR EMBL; BC018722; AAH18722.1; -; mRNA.
DR CCDS; CCDS11796.1; -. [Q9BZE9-1]
DR CCDS; CCDS58611.1; -. [Q9BZE9-2]
DR CCDS; CCDS82222.1; -. [Q9BZE9-3]
DR RefSeq; NP_001238817.1; NM_001251888.1. [Q9BZE9-2]
DR RefSeq; NP_001317457.1; NM_001330528.1. [Q9BZE9-3]
DR RefSeq; NP_076988.1; NM_024083.3. [Q9BZE9-1]
DR PDB; 5IFS; X-ray; 2.46 A; A/C=317-553.
DR PDB; 5IFW; X-ray; 3.40 A; A=317-504.
DR PDBsum; 5IFS; -.
DR PDBsum; 5IFW; -.
DR AlphaFoldDB; Q9BZE9; -.
DR SMR; Q9BZE9; -.
DR BioGRID; 122516; 67.
DR IntAct; Q9BZE9; 35.
DR MINT; Q9BZE9; -.
DR GlyGen; Q9BZE9; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9BZE9; -.
DR PhosphoSitePlus; Q9BZE9; -.
DR BioMuta; ASPSCR1; -.
DR DMDM; 74717746; -.
DR EPD; Q9BZE9; -.
DR jPOST; Q9BZE9; -.
DR MassIVE; Q9BZE9; -.
DR MaxQB; Q9BZE9; -.
DR PaxDb; Q9BZE9; -.
DR PeptideAtlas; Q9BZE9; -.
DR PRIDE; Q9BZE9; -.
DR ProteomicsDB; 79824; -. [Q9BZE9-1]
DR ProteomicsDB; 79825; -. [Q9BZE9-2]
DR ProteomicsDB; 79826; -. [Q9BZE9-3]
DR ProteomicsDB; 79827; -. [Q9BZE9-4]
DR Antibodypedia; 19857; 300 antibodies from 30 providers.
DR DNASU; 79058; -.
DR Ensembl; ENST00000306729.11; ENSP00000306625.7; ENSG00000169696.16. [Q9BZE9-2]
DR Ensembl; ENST00000306739.9; ENSP00000302176.4; ENSG00000169696.16. [Q9BZE9-1]
DR Ensembl; ENST00000580534.5; ENSP00000462329.1; ENSG00000169696.16. [Q9BZE9-3]
DR GeneID; 79058; -.
DR KEGG; hsa:79058; -.
DR MANE-Select; ENST00000306739.9; ENSP00000302176.4; NM_024083.4; NP_076988.1.
DR UCSC; uc002kcx.3; human. [Q9BZE9-1]
DR CTD; 79058; -.
DR DisGeNET; 79058; -.
DR GeneCards; ASPSCR1; -.
DR HGNC; HGNC:13825; ASPSCR1.
DR HPA; ENSG00000169696; Low tissue specificity.
DR MalaCards; ASPSCR1; -.
DR MIM; 606236; gene.
DR neXtProt; NX_Q9BZE9; -.
DR OpenTargets; ENSG00000169696; -.
DR Orphanet; 163699; Alveolar soft tissue sarcoma.
DR Orphanet; 319308; MiT family translocation renal cell carcinoma.
DR PharmGKB; PA25058; -.
DR VEuPathDB; HostDB:ENSG00000169696; -.
DR eggNOG; KOG2699; Eukaryota.
DR GeneTree; ENSGT00940000156853; -.
DR HOGENOM; CLU_025227_0_0_1; -.
DR InParanoid; Q9BZE9; -.
DR OMA; EEGAHYA; -.
DR OrthoDB; 1104599at2759; -.
DR PhylomeDB; Q9BZE9; -.
DR TreeFam; TF320363; -.
DR PathwayCommons; Q9BZE9; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR SignaLink; Q9BZE9; -.
DR SIGNOR; Q9BZE9; -.
DR BioGRID-ORCS; 79058; 18 hits in 1076 CRISPR screens.
DR ChiTaRS; ASPSCR1; human.
DR GeneWiki; ASPSCR1; -.
DR GenomeRNAi; 79058; -.
DR Pharos; Q9BZE9; Tbio.
DR PRO; PR:Q9BZE9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BZE9; protein.
DR Bgee; ENSG00000169696; Expressed in right lobe of liver and 141 other tissues.
DR ExpressionAtlas; Q9BZE9; baseline and differential.
DR Genevisible; Q9BZE9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0012506; C:vesicle membrane; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0031401; P:positive regulation of protein modification process; IMP:UniProtKB.
DR GO; GO:0046324; P:regulation of glucose import; IEA:Ensembl.
DR InterPro; IPR021569; TUG-UBL1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF11470; TUG-UBL1; 1.
DR Pfam; PF00789; UBX; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Cytoplasm; Membrane; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..553
FT /note="Tether containing UBX domain for GLUT4"
FT /id="PRO_0000249885"
FT DOMAIN 386..462
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 182..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..380
FT /note="Interaction with GLUT4"
FT /evidence="ECO:0000250"
FT REGION 499..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 311..312
FT /note="Breakpoint for translocation to form ASPSCR1-TFE3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBT9"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020574"
FT VAR_SEQ 390..425
FT /note="KVALRVLFPDRYVLQGFFRPSETVGDLRDFVRSHLG -> RRSLSLSPRLES
FT VVPSQLTASSASRVQVVLLPQPPK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020575"
FT VAR_SEQ 426..553
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020576"
FT VAR_SEQ 434
FT /note="F -> CLSSFGRMDGRGPRCFLTRRCLLSSV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020577"
FT VAR_SEQ 451
FT /note="Q -> QPQLGDRVAPFTLGPSLKRCLGPEQRTRLPVVGDGGDVDSGRLLFWG
FT PSRGRASPSTGQPPCHPVCRPSSPPSPRPSSGDPSRVKAGHKHVGTGR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020578"
FT VARIANT 252
FT /note="L -> Q (in dbSNP:rs8074498)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027503"
FT VARIANT 318
FT /note="V -> M (in dbSNP:rs34085048)"
FT /id="VAR_034745"
FT VARIANT 487
FT /note="D -> E (in dbSNP:rs13087)"
FT /id="VAR_027504"
FT CONFLICT 257
FT /note="G -> E (in Ref. 2; BAB71595)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="D -> G (in Ref. 2; BAB71595)"
FT /evidence="ECO:0000305"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 349..368
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 374..387
FT /evidence="ECO:0007829|PDB:5IFS"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:5IFS"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:5IFS"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:5IFS"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5IFS"
FT TURN 436..439
FT /evidence="ECO:0007829|PDB:5IFS"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:5IFW"
FT TURN 449..453
FT /evidence="ECO:0007829|PDB:5IFS"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:5IFW"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 483..494
FT /evidence="ECO:0007829|PDB:5IFS"
SQ SEQUENCE 553 AA; 60183 MW; B013FDF9A48D2E5E CRC64;
MAAPAGGGGS AVSVLAPNGR RHTVKVTPST VLLQVLEDTC RRQDFNPCEY DLKFQRSVLD
LSLQWRFANL PNNAKLEMVP ASRSREGPEN MVRIALQLDD GSRLQDSFCS GQTLWELLSH
FPQIRECLQH PGGATPVCVY TRDEVTGEAA LRGTTLQSLG LTGGSATIRF VMKCYDPVGK
TPGSLGSSAS AGQAAASAPL PLESGELSRG DLSRPEDADT SGPCCEHTQE KQSTRAPAAA
PFVPFSGGGQ RLGGPPGPTR PLTSSSAKLP KSLSSPGGPS KPKKSKSGQD PQQEQEQERE
RDPQQEQERE RPVDREPVDR EPVVCHPDLE ERLQAWPAEL PDEFFELTVD DVRRRLAQLK
SERKRLEEAP LVTKAFREAQ IKEKLERYPK VALRVLFPDR YVLQGFFRPS ETVGDLRDFV
RSHLGNPELS FYLFITPPKT VLDDHTQTLF QANLFPAALV HLGAEEPAGV YLEPGLLEHA
ISPSAADVLV ARYMSRAAGS PSPLPAPDPA PKSEPAAEEG ALVPPEPIPG TAQPVKRSLG
KVPKWLKLPA SKR
