OCAD1_HUMAN
ID OCAD1_HUMAN Reviewed; 245 AA.
AC Q9NX40; C9K030; G8JLN7; Q9BZE8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=OCIA domain-containing protein 1;
DE AltName: Full=Ovarian cancer immunoreactive antigen domain containing 1 {ECO:0000303|PubMed:20515946};
DE AltName: Full=Ovarian carcinoma immunoreactive antigen;
GN Name=OCIAD1 {ECO:0000312|HGNC:HGNC:16074};
GN Synonyms=ASRIJ {ECO:0000250|UniProtKB:Q9CRD0}, OCIA;
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 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Ovarian carcinoma;
RX PubMed=11162530; DOI=10.1006/bbrc.2000.4126;
RA Luo L.Y., Soosaipillai A., Diamandis E.P.;
RT "Molecular cloning of a novel human gene on chromosome 4p11 by
RT immunoscreening of an ovarian carcinoma cDNA library.";
RL Biochem. Biophys. Res. Commun. 280:401-406(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary tumor;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-191, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP FUNCTION.
RX PubMed=20515946; DOI=10.1158/1535-7163.mct-09-1024;
RA Wang C., Michener C.M., Belinson J.L., Vaziri S., Ganapathi R.,
RA Sengupta S.;
RT "Role of the 18:1 lysophosphatidic acid-ovarian cancer immunoreactive
RT antigen domain containing 1 (OCIAD1)-integrin axis in generating late-stage
RT ovarian cancer.";
RL Mol. Cancer Ther. 9:1709-1718(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-123 AND SER-191, AND
RP IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-116 AND SER-123, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-191, 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Maintains stem cell potency (By similarity). Increases STAT3
CC phosphorylation and controls ERK phosphorylation (By similarity). May
CC act as a scaffold, increasing STAT3 recruitment onto endosomes (By
CC similarity). Involved in integrin-mediated cancer cell adhesion and
CC colony formation in ovarian cancer (PubMed:20515946).
CC {ECO:0000250|UniProtKB:Q9CRD0, ECO:0000269|PubMed:20515946}.
CC -!- SUBUNIT: Interacts with STAT3. {ECO:0000250|UniProtKB:Q9CRD0}.
CC -!- INTERACTION:
CC Q9NX40; Q12797-6: ASPH; NbExp=3; IntAct=EBI-2683029, EBI-12092171;
CC Q9NX40; P17544: ATF7; NbExp=2; IntAct=EBI-2683029, EBI-765623;
CC Q9NX40; P49069: CAMLG; NbExp=3; IntAct=EBI-2683029, EBI-1748958;
CC Q9NX40; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-2683029, EBI-3918971;
CC Q9NX40; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-2683029, EBI-713304;
CC Q9NX40; Q15546: MMD; NbExp=3; IntAct=EBI-2683029, EBI-17873222;
CC Q9NX40; Q99726: SLC30A3; NbExp=3; IntAct=EBI-2683029, EBI-10294651;
CC Q9NX40; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-2683029, EBI-11528917;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q9CRD0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q9NX40-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9NX40-2; Sequence=VSP_027621, VSP_027622;
CC Name=3;
CC IsoId=Q9NX40-3; Sequence=VSP_027622;
CC Name=4;
CC IsoId=Q9NX40-4; Sequence=VSP_046212;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in many tissues,
CC including testis, brain, placenta, ovary, prostate and mammary gland.
CC Isoform 2 expression is restricted to the central nervous system
CC including brain, cerebellum and spinal cord.
CC {ECO:0000269|PubMed:11162530}.
CC -!- DOMAIN: The OCIA domain is necessary and sufficient for endosomal
CC localization. {ECO:0000250|UniProtKB:Q9CRD0}.
CC -!- MISCELLANEOUS: 'Asrij' stands for 'blood' in Sanskrit as this protein
CC is strongly expressed in blood vessels.
CC -!- SIMILARITY: Belongs to the OCIAD1 family. {ECO:0000305}.
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DR EMBL; AF323665; AAG45220.1; -; mRNA.
DR EMBL; AF324350; AAK12121.1; -; mRNA.
DR EMBL; AF251296; AAG44596.1; -; mRNA.
DR EMBL; AL539411; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK000462; BAA91181.1; -; mRNA.
DR EMBL; AC079927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW93070.1; -; Genomic_DNA.
DR EMBL; BC003409; AAH03409.1; -; mRNA.
DR EMBL; BC088361; AAH88361.1; -; mRNA.
DR CCDS; CCDS3484.1; -. [Q9NX40-1]
DR CCDS; CCDS43228.1; -. [Q9NX40-2]
DR CCDS; CCDS47052.1; -. [Q9NX40-4]
DR PIR; JC7586; JC7586.
DR RefSeq; NP_001073308.1; NM_001079839.2. [Q9NX40-1]
DR RefSeq; NP_001073309.1; NM_001079840.2. [Q9NX40-4]
DR RefSeq; NP_001073310.1; NM_001079841.2. [Q9NX40-2]
DR RefSeq; NP_001073311.2; NM_001079842.2. [Q9NX40-4]
DR RefSeq; NP_060300.1; NM_017830.3. [Q9NX40-1]
DR RefSeq; XP_016863818.1; XM_017008329.1. [Q9NX40-2]
DR AlphaFoldDB; Q9NX40; -.
DR BioGRID; 120280; 422.
DR IntAct; Q9NX40; 114.
DR MINT; Q9NX40; -.
DR STRING; 9606.ENSP00000370882; -.
DR GlyGen; Q9NX40; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX40; -.
DR PhosphoSitePlus; Q9NX40; -.
DR SwissPalm; Q9NX40; -.
DR BioMuta; OCIAD1; -.
DR DMDM; 74734685; -.
DR EPD; Q9NX40; -.
DR jPOST; Q9NX40; -.
DR MassIVE; Q9NX40; -.
DR MaxQB; Q9NX40; -.
DR PaxDb; Q9NX40; -.
DR PeptideAtlas; Q9NX40; -.
DR PRIDE; Q9NX40; -.
DR ProteomicsDB; 34288; -.
DR ProteomicsDB; 83031; -. [Q9NX40-1]
DR ProteomicsDB; 83032; -. [Q9NX40-2]
DR ProteomicsDB; 83033; -. [Q9NX40-3]
DR TopDownProteomics; Q9NX40-1; -. [Q9NX40-1]
DR TopDownProteomics; Q9NX40-2; -. [Q9NX40-2]
DR TopDownProteomics; Q9NX40-3; -. [Q9NX40-3]
DR Antibodypedia; 23858; 234 antibodies from 32 providers.
DR DNASU; 54940; -.
DR Ensembl; ENST00000264312.12; ENSP00000264312.7; ENSG00000109180.15. [Q9NX40-1]
DR Ensembl; ENST00000381473.7; ENSP00000370882.3; ENSG00000109180.15. [Q9NX40-1]
DR Ensembl; ENST00000396448.6; ENSP00000379725.2; ENSG00000109180.15. [Q9NX40-2]
DR Ensembl; ENST00000425583.6; ENSP00000416943.2; ENSG00000109180.15. [Q9NX40-4]
DR Ensembl; ENST00000444354.6; ENSP00000399656.2; ENSG00000109180.15. [Q9NX40-4]
DR Ensembl; ENST00000508293.5; ENSP00000423002.1; ENSG00000109180.15. [Q9NX40-1]
DR Ensembl; ENST00000513391.2; ENSP00000423909.2; ENSG00000109180.15. [Q9NX40-1]
DR GeneID; 54940; -.
DR KEGG; hsa:54940; -.
DR MANE-Select; ENST00000264312.12; ENSP00000264312.7; NM_017830.4; NP_060300.1.
DR UCSC; uc003gyo.4; human. [Q9NX40-1]
DR CTD; 54940; -.
DR DisGeNET; 54940; -.
DR GeneCards; OCIAD1; -.
DR HGNC; HGNC:16074; OCIAD1.
DR HPA; ENSG00000109180; Low tissue specificity.
DR MIM; 619596; gene.
DR neXtProt; NX_Q9NX40; -.
DR OpenTargets; ENSG00000109180; -.
DR PharmGKB; PA134898158; -.
DR VEuPathDB; HostDB:ENSG00000109180; -.
DR eggNOG; ENOG502RXQR; Eukaryota.
DR GeneTree; ENSGT00530000063690; -.
DR HOGENOM; CLU_083038_0_0_1; -.
DR InParanoid; Q9NX40; -.
DR OMA; AGKMSYM; -.
DR OrthoDB; 1322104at2759; -.
DR PhylomeDB; Q9NX40; -.
DR TreeFam; TF327106; -.
DR PathwayCommons; Q9NX40; -.
DR SignaLink; Q9NX40; -.
DR BioGRID-ORCS; 54940; 39 hits in 1079 CRISPR screens.
DR ChiTaRS; OCIAD1; human.
DR GenomeRNAi; 54940; -.
DR Pharos; Q9NX40; Tbio.
DR PRO; PR:Q9NX40; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NX40; protein.
DR Bgee; ENSG00000109180; Expressed in pancreatic ductal cell and 191 other tissues.
DR ExpressionAtlas; Q9NX40; baseline and differential.
DR Genevisible; Q9NX40; HS.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:FlyBase.
DR GO; GO:0005764; C:lysosome; ISS:FlyBase.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:FlyBase.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISS:FlyBase.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISS:FlyBase.
DR GO; GO:2000736; P:regulation of stem cell differentiation; ISS:UniProtKB.
DR InterPro; IPR040187; OCAD1/2.
DR InterPro; IPR009764; OCIA_dom.
DR PANTHER; PTHR13336; PTHR13336; 1.
DR Pfam; PF07051; OCIA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Phosphoprotein; Reference proteome.
FT CHAIN 1..245
FT /note="OCIA domain-containing protein 1"
FT /id="PRO_0000299382"
FT DOMAIN 1..112
FT /note="OCIA"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 183..233
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_046212"
FT VAR_SEQ 184..187
FT /note="PDPN -> RNFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11162530"
FT /id="VSP_027621"
FT VAR_SEQ 188..245
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11162530"
FT /id="VSP_027622"
SQ SEQUENCE 245 AA; 27626 MW; B4CD4F4B5483884D CRC64;
MNGRADFREP NAEVPRPIPH IGPDYIPTEE ERRVFAECND ESFWFRSVPL AATSMLITQG
LISKGILSSH PKYGSIPKLI LACIMGYFAG KLSYVKTCQE KFKKLENSPL GEALRSGQAR
RSSPPGHYYQ KSKYDSSVSG QSSFVTSPAA DNIEMLPHYE PIPFSSSMNE SAPTGITDHI
VQGPDPNLEE SPKRKNITYE ELRNKNRESY EVSLTQKTDP SVRPMHERVP KKEVKVNKYG
DTWDE
