DEN2B_HUMAN
ID DEN2B_HUMAN Reviewed; 1137 AA.
AC P78524; B2R6X7; B3KXQ6; P78523; Q16492; Q7KYY2; Q7KZ12; Q8NE12; Q9BQQ6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=DENN domain-containing protein 2B;
DE AltName: Full=HeLa tumor suppression 1;
DE AltName: Full=Suppression of tumorigenicity 5 protein;
GN Name=DENND2B {ECO:0000312|HGNC:HGNC:11350};
GN Synonyms=HTS1, ST5 {ECO:0000303|PubMed:10229203,
GN ECO:0000303|PubMed:8972856};
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 1; 2 AND 3), AND VARIANT GLU-399.
RX PubMed=8972856; DOI=10.1093/nar/24.23.4700;
RA Lichy J.H., Majidi M., Elbaum J., Tsai M.M.;
RT "Differential expression of the human ST5 gene in HeLa-fibroblast hybrid
RT cell lines mediated by YY1: evidence that YY1 plays a part in tumor
RT suppression.";
RL Nucleic Acids Res. 24:4700-4708(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-399.
RX PubMed=11528127; DOI=10.1159/000056999;
RA Amid C., Bahr A., Mujica A., Sampson N., Bikar S.E., Winterpacht A.,
RA Zabel B., Hankeln T., Schmidt E.R.;
RT "Comparative genomic sequencing reveals a strikingly similar architecture
RT of a conserved syntenic region on human chromosome 11p15.3 (including gene
RT ST5) and mouse chromosome 7.";
RL Cytogenet. Cell Genet. 93:284-290(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Spleen;
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(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 1), AND VARIANTS ASN-316;
RP THR-620 AND GLY-774.
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 493-1137.
RX PubMed=1390339;
RA Lichy J.H., Modi W.S., Seuanez H.N., Howley P.M.;
RT "Identification of a human chromosome 11 gene which is differentially
RT regulated in tumorigenic and nontumorigenic somatic cell hybrids of HeLa
RT cells.";
RL Cell Growth Differ. 3:541-548(1992).
RN [8]
RP FUNCTION (ISOFORMS 1 AND 3), AND INTERACTION WITH ABL1.
RX PubMed=9632734; DOI=10.1074/jbc.273.26.16608;
RA Majidi M., Hubbs A.E., Lichy J.H.;
RT "Activation of extracellular signal-regulated kinase 2 by a novel Abl-
RT binding protein, ST5.";
RL J. Biol. Chem. 273:16608-16614(1998).
RN [9]
RP FUNCTION (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=10229203; DOI=10.1038/sj.onc.1202554;
RA Hubbs A.E., Majidi M., Lichy J.H.;
RT "Expression of an isoform of the novel signal transduction protein ST5 is
RT linked to cell morphology.";
RL Oncogene 18:2519-2525(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, 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 [11]
RP FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR (ISOFORM 2).
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 THR-364 AND SER-368, 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 FUNCTION (ISOFORM 1), INTERACTION WITH ITSN1 AND GRB2, SUBCELLULAR LOCATION
RP (ISOFORM 1), PHOSPHORYLATION AT SER-30, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29030480; DOI=10.15252/embr.201744034;
RA Ioannou M.S., Kulasekaran G., Fotouhi M., Morein J.J., Han C., Tse S.,
RA Nossova N., Han T., Mannard E., McPherson P.S.;
RT "Intersectin-s interaction with DENND2B facilitates recycling of epidermal
RT growth factor receptor.";
RL EMBO Rep. 18:2119-2130(2017).
CC -!- FUNCTION: [Isoform 1]: May be involved in cytoskeletal organization and
CC tumorogenicity. Seems to be involved in a signaling transduction
CC pathway leading to activation of MAPK1/ERK2. Plays a role in EGFR
CC trafficking from recycling endosomes back to the cell membrane
CC (PubMed:29030480). {ECO:0000269|PubMed:29030480,
CC ECO:0000269|PubMed:9632734}.
CC -!- FUNCTION: [Isoform 2]: Guanine nucleotide exchange factor (GEF) which
CC may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP,
CC converting inactive GDP-bound Rab proteins into their active GTP-bound
CC form. {ECO:0000269|PubMed:20937701}.
CC -!- FUNCTION: [Isoform 3]: May block ERK2 activation stimulated by ABL1
CC (Probable). May alter cell morphology and cell growth (Probable).
CC {ECO:0000305|PubMed:10229203, ECO:0000305|PubMed:9632734}.
CC -!- SUBUNIT: Interacts with ITSN1 and GRB2 (PubMed:29030480). Isoform 1
CC interacts with the SH3 domain of ABL1. {ECO:0000269|PubMed:29030480,
CC ECO:0000269|PubMed:9632734}.
CC -!- INTERACTION:
CC P78524; P42858: HTT; NbExp=3; IntAct=EBI-962633, EBI-466029;
CC P78524; O76024: WFS1; NbExp=3; IntAct=EBI-962633, EBI-720609;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:29030480}. Cell membrane
CC {ECO:0000269|PubMed:29030480}. Recycling endosome
CC {ECO:0000269|PubMed:29030480}. Note=Colocalizes with RAB13 and ITSN1 at
CC cytoplasmic vesicles that are most likely recycling endosomes.
CC Colocalizes with the cortical actin cytoskeleton.
CC {ECO:0000269|PubMed:29030480}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=p126;
CC IsoId=P78524-1; Sequence=Displayed;
CC Name=2; Synonyms=p82;
CC IsoId=P78524-2; Sequence=VSP_019988;
CC Name=3; Synonyms=p70;
CC IsoId=P78524-3; Sequence=VSP_019987;
CC -!- TISSUE SPECIFICITY: Widely expressed with the exception of peripheral
CC blood lymphocytes. Isoform 1 is expressed in several epithelial and
CC fibroblast (including tumorigenic) but absent in lymphoid cell lines
CC (at protein level). Isoform 3 is expressed in primary cell or weakly
CC tumorigenic but not in tumorigenic cell lines (at protein level).
CC {ECO:0000269|PubMed:10229203}.
CC -!- PTM: Phosphorylated. Phosphorylation decreases ITSN1 binding.
CC {ECO:0000269|PubMed:29030480}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50925.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U15131; AAC50925.1; ALT_FRAME; mRNA.
DR EMBL; U15779; AAB97097.1; -; mRNA.
DR EMBL; U15780; AAC50926.1; -; mRNA.
DR EMBL; AJ400879; CAC35387.1; -; Genomic_DNA.
DR EMBL; AK127763; BAG54568.1; -; mRNA.
DR EMBL; AK312758; BAG35624.1; -; mRNA.
DR EMBL; AC026894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68618.1; -; Genomic_DNA.
DR EMBL; BC036655; AAH36655.1; -; mRNA.
DR EMBL; S45936; AAB23647.1; -; mRNA.
DR CCDS; CCDS7791.1; -. [P78524-1]
DR CCDS; CCDS7792.1; -. [P78524-2]
DR PIR; A49013; A49013.
DR RefSeq; NP_005409.3; NM_005418.3. [P78524-1]
DR RefSeq; NP_631896.1; NM_139157.2. [P78524-2]
DR RefSeq; NP_998783.1; NM_213618.1. [P78524-1]
DR RefSeq; XP_005253140.1; XM_005253083.2.
DR RefSeq; XP_011518620.1; XM_011520318.1.
DR RefSeq; XP_011518631.1; XM_011520329.1. [P78524-2]
DR AlphaFoldDB; P78524; -.
DR SMR; P78524; -.
DR BioGRID; 112642; 21.
DR IntAct; P78524; 24.
DR MINT; P78524; -.
DR STRING; 9606.ENSP00000433528; -.
DR iPTMnet; P78524; -.
DR PhosphoSitePlus; P78524; -.
DR BioMuta; ST5; -.
DR DMDM; 317373507; -.
DR EPD; P78524; -.
DR jPOST; P78524; -.
DR MassIVE; P78524; -.
DR MaxQB; P78524; -.
DR PaxDb; P78524; -.
DR PeptideAtlas; P78524; -.
DR PRIDE; P78524; -.
DR ProteomicsDB; 57631; -. [P78524-1]
DR ProteomicsDB; 57632; -. [P78524-2]
DR ProteomicsDB; 57633; -. [P78524-3]
DR Antibodypedia; 24131; 217 antibodies from 30 providers.
DR DNASU; 6764; -.
DR Ensembl; ENST00000313726.11; ENSP00000319678.6; ENSG00000166444.19. [P78524-1]
DR Ensembl; ENST00000526757.5; ENSP00000435097.1; ENSG00000166444.19. [P78524-2]
DR Ensembl; ENST00000530438.5; ENSP00000436802.1; ENSG00000166444.19. [P78524-2]
DR Ensembl; ENST00000530991.5; ENSP00000432887.1; ENSG00000166444.19. [P78524-3]
DR Ensembl; ENST00000534127.5; ENSP00000433528.1; ENSG00000166444.19. [P78524-1]
DR GeneID; 6764; -.
DR KEGG; hsa:6764; -.
DR MANE-Select; ENST00000313726.11; ENSP00000319678.6; NM_213618.2; NP_998783.1.
DR UCSC; uc001mgt.4; human. [P78524-1]
DR CTD; 6764; -.
DR DisGeNET; 6764; -.
DR GeneCards; DENND2B; -.
DR HGNC; HGNC:11350; DENND2B.
DR HPA; ENSG00000166444; Low tissue specificity.
DR MIM; 140750; gene.
DR neXtProt; NX_P78524; -.
DR OpenTargets; ENSG00000166444; -.
DR VEuPathDB; HostDB:ENSG00000166444; -.
DR eggNOG; KOG3569; Eukaryota.
DR GeneTree; ENSGT00950000182931; -.
DR HOGENOM; CLU_008960_0_0_1; -.
DR InParanoid; P78524; -.
DR OMA; SHVRKES; -.
DR OrthoDB; 138384at2759; -.
DR PhylomeDB; P78524; -.
DR TreeFam; TF320336; -.
DR PathwayCommons; P78524; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P78524; -.
DR BioGRID-ORCS; 6764; 6 hits in 1064 CRISPR screens.
DR ChiTaRS; ST5; human.
DR GeneWiki; ST5_(gene); -.
DR GenomeRNAi; 6764; -.
DR Pharos; P78524; Tbio.
DR PRO; PR:P78524; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P78524; protein.
DR Bgee; ENSG00000166444; Expressed in body of uterus and 186 other tissues.
DR ExpressionAtlas; P78524; baseline and differential.
DR Genevisible; P78524; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR PROSITE; PS50211; DENN; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Cell membrane; Cytoplasm;
KW Endosome; Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1137
FT /note="DENN domain-containing protein 2B"
FT /id="PRO_0000247448"
FT DOMAIN 698..846
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 868..1001
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 1003..1096
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..447
FT /note="Interaction with ABL1"
FT /evidence="ECO:0000269|PubMed:9632734"
FT REGION 641..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29030480"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924W7"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q924W7"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924W7"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q924W7"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924W7"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924W7"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..528
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8972856"
FT /id="VSP_019987"
FT VAR_SEQ 28..447
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8972856"
FT /id="VSP_019988"
FT VARIANT 316
FT /note="K -> N (in dbSNP:rs3794153)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027101"
FT VARIANT 399
FT /note="D -> E (in dbSNP:rs3812762)"
FT /evidence="ECO:0000269|PubMed:11528127,
FT ECO:0000269|PubMed:8972856"
FT /id="VAR_027102"
FT VARIANT 620
FT /note="I -> T (in dbSNP:rs17853683)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027103"
FT VARIANT 657
FT /note="S -> F (in dbSNP:rs11042047)"
FT /id="VAR_030642"
FT VARIANT 774
FT /note="S -> G (in dbSNP:rs17853682)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027104"
FT CONFLICT 113
FT /note="A -> T (in Ref. 1; AAC50925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1137 AA; 126485 MW; 96ACD16E0602479E CRC64;
MTMTANKNSS ITHGAGGTKA PRGTLSRSQS VSPPPVLSPP RSPIYPLSDS ETSACRYPSH
SSSRVLLKDR HPPAPSPQNP QDPSPDTSPP TCPFKTASFG YLDRSPSACK RDAQKESVQG
AAQDVAGVAA CLPLAQSTPF PGPAAGPRGV LLTRTGTRAH SLGIREKISA WEGRREASPR
MSMCGEKREG SGSEWAASEG CPSLGCPSVV PSPCSSEKTF DFKGLRRMSR TFSECSYPET
EEEGEALPVR DSFYRLEKRL GRSEPSAFLR GHGSRKESSA VLSRIQKIEQ VLKEQPGRGL
PQLPSSCYSV DRGKRKTGTL GSLEEPAGGA SVSAGSRAVG VAGVAGEAGP PPEREGSGST
KPGTPGNSPS SQRLPSKSSL DPAVNPVPKP KRTFEYEADK NPKSKPSNGL PPSPTPAAPP
PLPSTPAPPV TRRPKKDMRG HRKSQSRKSF EFEDASSLQS LYPSSPTENG TENQPKFGSK
STLEENAYED IVGDLPKENP YEDVDLKSRR AGRKSQQLSE NSLDSLHRMW SPQDRKYNSP
PTQLSLKPNS QSLRSGNWSE RKSHRLPRLP KRHSHDDMLL LAQLSLPSSP SSLNEDSLST
TSELLSSRRA RRIPKLVQRI NSIYNAKRGK KRLKKLSMSS IETASLRDEN SESESDSDDR
FKAHTQRLVH IQSMLKRAPS YRTLELELLE WQERELFEYF VVVSLKKKPS RNTYLPEVSY
QFPKLDRPTK QMREAEERLK AIPQFCFPDA KDWLPVSEYS SETFSFMLTG EDGSRRFGYC
RRLLPSGKGP RLPEVYCVIS RLGCFGLFSK VLDEVERRRG ISAALVYPFM RSLMESPFPA
PGKTIKVKTF LPGAGNEVLE LRRPMDSRLE HVDFECLFTC LSVRQLIRIF ASLLLERRVI
FVADKLSTLS SCSHAVVALL YPFSWQHTFI PVLPASMIDI VCCPTPFLVG LLSSSLPKLK
ELPVEEALMV NLGSDRFIRQ MDDEDTLLPR KLQAALEQAL ERKNELISQD SDSDSDDECN
TLNGLVSEVF IRFFVETVGH YSLFLTQSEK GERAFQREAF RKSVASKSIR RFLEVFMESQ
MFAGFIQDRE LRKCRAKGLF EQRVEQYLEE LPDTEQSGMN KFLRGLGNKM KFLHKKN
