ITPI2_HUMAN
ID ITPI2_HUMAN Reviewed; 1259 AA.
AC P28290; A8K6T0; Q68DA6; Q7Z7L2; Q8N1L3; Q8N263; Q8N7H2; Q8NEN5; Q96E36;
AC Q96PW1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein ITPRID2 {ECO:0000305};
DE AltName: Full=Cleavage signal-1 protein {ECO:0000303|PubMed:1555770};
DE Short=CS-1 {ECO:0000303|PubMed:1555770};
DE AltName: Full=ITPR-interacting domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Ki-ras-induced actin-interacting protein {ECO:0000303|PubMed:14673706};
DE AltName: Full=Sperm-specific antigen 2;
GN Name=ITPRID2 {ECO:0000312|HGNC:HGNC:11319};
GN Synonyms=CS1 {ECO:0000303|PubMed:1555770}, KIAA1927,
GN KRAP {ECO:0000303|PubMed:14673706}, SSFA2 {ECO:0000312|HGNC:HGNC:11319};
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), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INDUCTION BY KRAS.
RX PubMed=14673706; DOI=10.1007/s10038-003-0106-3;
RA Inokuchi J., Komiya M., Baba I., Naito S., Sasazuki T., Shirasawa S.;
RT "Deregulated expression of KRAP, a novel gene encoding actin-interacting
RT protein, in human colon cancer cells.";
RL J. Hum. Genet. 49:46-52(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-836.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP TRP-833 AND LEU-836.
RC TISSUE=Mammary gland, Placenta, and Tongue;
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 MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Pancreas, Prostate, and 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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 991-1259 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=1555770; DOI=10.1016/0378-1119(92)90377-2;
RA Javed A.A., Naz R.K.;
RT "Human cleavage signal-1 protein; cDNA cloning, transcription and
RT immunological analysis.";
RL Gene 112:205-211(1992).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87; SER-92; SER-668; SER-737;
RP SER-739; SER-746 AND SER-1134, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-270; SER-737; SER-746
RP AND SER-759, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-209; SER-330;
RP SER-668; SER-737; SER-739; SER-746; SER-759; SER-767; SER-803; THR-1156 AND
RP SER-1161, AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87; SER-92; SER-270; SER-466;
RP SER-644; SER-737; SER-739; SER-746; SER-902; SER-1063; SER-1118; SER-1134;
RP SER-1161 AND THR-1168, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-808, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-360 AND LYS-808, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- INTERACTION:
CC P28290-2; P06396: GSN; NbExp=3; IntAct=EBI-25863618, EBI-351506;
CC P28290-2; P01112: HRAS; NbExp=3; IntAct=EBI-25863618, EBI-350145;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14673706}.
CC Note=Located near the plasma membrane. Associated with actin filaments.
CC May also exist as a membrane-bound form with extracellular regions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P28290-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28290-2; Sequence=VSP_023865;
CC Name=3;
CC IsoId=P28290-3; Sequence=VSP_023866, VSP_023867;
CC -!- TISSUE SPECIFICITY: Strongly expressed in pancreas and testis. Present
CC in colon cancer cells (at protein level).
CC {ECO:0000269|PubMed:14673706}.
CC -!- INDUCTION: Up-regulated by activated KRAS.
CC {ECO:0000269|PubMed:14673706}.
CC -!- PTM: A 33 kDa peptide corresponding to the C-terminus of this protein
CC is found in the testis and seems to be cleaved into 2 peptides of 14
CC kDa and 18 kDa found on the surface of mature sperm cells. This sperm
CC surface antigen may be involved in some step of early cleavage of the
CC fertilized oocyte.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB00773.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH12947.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB67820.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC05308.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB116937; BAC81767.1; -; mRNA.
DR EMBL; AB067514; BAB67820.2; ALT_INIT; mRNA.
DR EMBL; AK091197; BAC03607.1; -; mRNA.
DR EMBL; AK097375; BAC05027.1; -; mRNA.
DR EMBL; AK098455; BAC05308.1; ALT_INIT; mRNA.
DR EMBL; AK291745; BAF84434.1; -; mRNA.
DR EMBL; CR749488; CAH18314.1; -; mRNA.
DR EMBL; AC009962; AAY14913.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10980.1; -; Genomic_DNA.
DR EMBL; BC012947; AAH12947.1; ALT_INIT; mRNA.
DR EMBL; BC028706; AAH28706.1; -; mRNA.
DR EMBL; BC052581; AAH52581.1; -; mRNA.
DR EMBL; BC064499; AAH64499.1; -; mRNA.
DR EMBL; M61199; AAB00773.1; ALT_INIT; mRNA.
DR CCDS; CCDS2284.1; -. [P28290-3]
DR CCDS; CCDS46467.1; -. [P28290-1]
DR RefSeq; NP_001123917.1; NM_001130445.2. [P28290-1]
DR RefSeq; NP_001274432.1; NM_001287503.1.
DR RefSeq; NP_001274433.1; NM_001287504.1.
DR RefSeq; NP_006742.2; NM_006751.6. [P28290-3]
DR AlphaFoldDB; P28290; -.
DR BioGRID; 112622; 114.
DR DIP; DIP-47271N; -.
DR IntAct; P28290; 79.
DR MINT; P28290; -.
DR STRING; 9606.ENSP00000388731; -.
DR GlyGen; P28290; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P28290; -.
DR PhosphoSitePlus; P28290; -.
DR BioMuta; SSFA2; -.
DR DMDM; 134047924; -.
DR EPD; P28290; -.
DR jPOST; P28290; -.
DR MassIVE; P28290; -.
DR MaxQB; P28290; -.
DR PaxDb; P28290; -.
DR PeptideAtlas; P28290; -.
DR PRIDE; P28290; -.
DR ProteomicsDB; 54458; -. [P28290-1]
DR ProteomicsDB; 54459; -. [P28290-2]
DR ProteomicsDB; 54460; -. [P28290-3]
DR Antibodypedia; 33982; 113 antibodies from 20 providers.
DR DNASU; 6744; -.
DR Ensembl; ENST00000320370.11; ENSP00000314669.7; ENSG00000138434.17. [P28290-3]
DR Ensembl; ENST00000431877.7; ENSP00000388731.2; ENSG00000138434.17. [P28290-1]
DR GeneID; 6744; -.
DR KEGG; hsa:6744; -.
DR MANE-Select; ENST00000431877.7; ENSP00000388731.2; NM_001130445.3; NP_001123917.1.
DR UCSC; uc002uoh.5; human. [P28290-1]
DR CTD; 6744; -.
DR DisGeNET; 6744; -.
DR GeneCards; ITPRID2; -.
DR HGNC; HGNC:11319; ITPRID2.
DR HPA; ENSG00000138434; Tissue enhanced (pancreas).
DR MIM; 118990; gene.
DR neXtProt; NX_P28290; -.
DR OpenTargets; ENSG00000138434; -.
DR PharmGKB; PA36143; -.
DR VEuPathDB; HostDB:ENSG00000138434; -.
DR eggNOG; ENOG502QSG8; Eukaryota.
DR GeneTree; ENSGT00940000158532; -.
DR HOGENOM; CLU_007016_0_0_1; -.
DR InParanoid; P28290; -.
DR OMA; QHSNPDF; -.
DR OrthoDB; 94956at2759; -.
DR PhylomeDB; P28290; -.
DR TreeFam; TF331566; -.
DR PathwayCommons; P28290; -.
DR SignaLink; P28290; -.
DR BioGRID-ORCS; 6744; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; SSFA2; human.
DR GeneWiki; SSFA2; -.
DR GenomeRNAi; 6744; -.
DR Pharos; P28290; Tbio.
DR PRO; PR:P28290; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P28290; protein.
DR Bgee; ENSG00000138434; Expressed in body of pancreas and 210 other tissues.
DR ExpressionAtlas; P28290; baseline and differential.
DR Genevisible; P28290; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051015; F:actin filament binding; IDA:CACAO.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR InterPro; IPR029325; ITPR-bd.
DR InterPro; IPR026648; ITPRID2.
DR InterPro; IPR029326; SSFA2_C.
DR InterPro; IPR043444; TESPA1-like.
DR PANTHER; PTHR17469; PTHR17469; 1.
DR PANTHER; PTHR17469:SF11; PTHR17469:SF11; 1.
DR Pfam; PF14722; KRAP_IP3R_bind; 1.
DR Pfam; PF14723; SSFA2_C; 1.
DR SMART; SM01257; KRAP_IP3R_bind; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1259
FT /note="Protein ITPRID2"
FT /id="PRO_0000072211"
FT REGION 31..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 959..1037
FT /evidence="ECO:0000255"
FT COMPBIAS 44..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1156
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1168
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 808
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_023865"
FT VAR_SEQ 1226..1251
FT /note="IKESIVGEIRREIVSGLLAAVSSSKA -> VGMDPISCVILELSMICTGGGV
FT ICALEDTCC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023866"
FT VAR_SEQ 1252..1259
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023867"
FT VARIANT 817
FT /note="A -> V (in dbSNP:rs16867510)"
FT /id="VAR_056998"
FT VARIANT 833
FT /note="R -> W (in dbSNP:rs13419020)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031186"
FT VARIANT 836
FT /note="P -> L (in dbSNP:rs17647806)"
FT /evidence="ECO:0000269|PubMed:11572484,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_031187"
FT VARIANT 1258
FT /note="Y -> N (in dbSNP:rs2303554)"
FT /id="VAR_059724"
FT CONFLICT 292
FT /note="A -> V (in Ref. 4; CAH18314)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="S -> P (in Ref. 3; BAC05027)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="K -> E (in Ref. 3; BAC05027)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="E -> G (in Ref. 4; CAH18314)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="M -> L (in Ref. 8; AAB00773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="A -> T (in Ref. 8; AAB00773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1108..1110
FT /note="QAT -> KQR (in Ref. 8; AAB00773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1116
FT /note="V -> I (in Ref. 8; AAB00773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193
FT /note="E -> ESE (in Ref. 8; AAB00773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1259 AA; 138386 MW; D5843D9D6D5414D7 CRC64;
MDRPLSSSAE AEEELEWQVA SRRRKAWAKC RSSWQASETE DLSTEATTQD EEEDEEEDLP
GAQLPAAGGR GNVPNEKIAI WLKDCRTPLG ASLDEQSSST LKGVLVRNGG SFEDDLSLGA
EANHLHESDA QIENCNNILA KERRLQFHQK GRSMNSTGSG KSSGTVSSVS ELLELYEEDP
EEILYNLGFG RDEPDIASKI PSRFFNSSSF AKGIDIKVFL SAQMQRMEVE NPNYALTSRF
RQIEVLTTVA NAFSSLYSQV SGTPLQRIGS MSSVTSNKET DPPPPLTRSN TANRLMKTLS
KLNLCVDKTE KGESSSPSPS AEKGKILNVS VIEESGNKND QKSQKIMKKK ESSSMLATVK
EEVSGSSAAV TENADSDRIS DEANSNFNQG TENEQSKETQ SHESKLGEES GIVESKLDSD
FNISSHSELE NSSELKSVHI STPEKEPCAP LTIPSIRNIM TQQKDSFEME EVQSTEGEAP
HVPATYQLGL TKSKRDHLLR TASQHSDSSG FAEDSTDCLS LNHLQVQESL QAMGSSADSC
DSETTVTSLG EDLATPTAQD QPYFNESEEE SLVPLQKGLE KAAAVADKRK SGSQDFPQCN
TIENTGTKQS TCSPGDHIIE ITEVEEDLFP AETVELLREA SAESDVGKSS ESEFTQYTTH
HILKSLASIE AKCSDMSSEN TTGPPSSMDR VNTALQRAQM KVCSLSNQRM GRSLLKSKDL
LKQRYLFAKA GYPLRRSQSL PTTLLSPVRV VSSVNVRLSP GKETRCSPPS FTYKYTPEEE
QELEKRVMEH DGQSLVKSTI FISPSSVKKE EAPQSEAPRV EECHHGRTPT CSRLAPPPMS
QSTCSLHSIH SEWQERPLCE HTRTLSTHSV PNISGATCSA FASPFGCPYS HRHATYPYRV
CSVNPPSAIE MQLRRVLHDI RNSLQNLSQY PMMRGPDPAA APYSTQKSSV LPLYENTFQE
LQVMRRSLNL FRTQMMDLEL AMLRQQTMVY HHMTEEERFE VDQLQGLRNS VRMELQDLEL
QLEERLLGLE EQLRAVRMPS PFRSSALMGM CGSRSADNLS CPSPLNVMEP VTELMQEQSY
LKSELGLGLG EMGFEIPPGE SSESVFSQAT SESSSVCSGP SHANRRTGVP STASVGKSKT
PLVARKKVFR ASVALTPTAP SRTGSVQTPP DLESSEEVDA AEGAPEVVGP KSEVEEGHGK
LPSMPAAEEM HKNVEQDELQ QVIREIKESI VGEIRREIVS GLLAAVSSSK ASNSKQDYH
