CDV3_HUMAN
ID CDV3_HUMAN Reviewed; 258 AA.
AC Q9UKY7; B3KUC2; Q96IP9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein CDV3 homolog;
GN Name=CDV3; Synonyms=H41;
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), AND TISSUE SPECIFICITY.
RX PubMed=10497265; DOI=10.1093/nar/27.20.4008;
RA Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
RT "Identification of differentially expressed genes associated with HER-2/neu
RT overexpression in human breast cancer cells.";
RL Nucleic Acids Res. 27:4008-4017(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, 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 [7]
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=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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND THR-182, AND
RP IDENTIFICATION BY 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-8; SER-106; SER-107
RP AND THR-182, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UKY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKY7-2; Sequence=VSP_027760, VSP_027761;
CC Name=3;
CC IsoId=Q9UKY7-3; Sequence=VSP_041357, VSP_041358, VSP_041359;
CC -!- TISSUE SPECIFICITY: Expression levels correlate with those of HER-2/neu
CC in breast cancer cells. {ECO:0000269|PubMed:10497265}.
CC -!- SIMILARITY: Belongs to the CDV3 family. {ECO:0000305}.
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DR EMBL; AF103803; AAF02423.1; -; mRNA.
DR EMBL; AK096865; BAG53384.1; -; mRNA.
DR EMBL; AC016255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007338; AAH07338.1; -; mRNA.
DR CCDS; CCDS3079.1; -. [Q9UKY7-1]
DR CCDS; CCDS46917.1; -. [Q9UKY7-2]
DR CCDS; CCDS46918.1; -. [Q9UKY7-3]
DR RefSeq; NP_001127894.1; NM_001134422.1. [Q9UKY7-2]
DR RefSeq; NP_001127895.1; NM_001134423.2. [Q9UKY7-3]
DR RefSeq; NP_001269691.1; NM_001282762.1.
DR RefSeq; NP_001269692.1; NM_001282763.1.
DR RefSeq; NP_001269693.1; NM_001282764.1.
DR RefSeq; NP_001269694.1; NM_001282765.1.
DR RefSeq; NP_060018.1; NM_017548.4. [Q9UKY7-1]
DR AlphaFoldDB; Q9UKY7; -.
DR BioGRID; 120726; 57.
DR IntAct; Q9UKY7; 2.
DR STRING; 9606.ENSP00000264993; -.
DR GlyGen; Q9UKY7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKY7; -.
DR MetOSite; Q9UKY7; -.
DR PhosphoSitePlus; Q9UKY7; -.
DR BioMuta; CDV3; -.
DR DMDM; 74721018; -.
DR EPD; Q9UKY7; -.
DR jPOST; Q9UKY7; -.
DR MassIVE; Q9UKY7; -.
DR MaxQB; Q9UKY7; -.
DR PaxDb; Q9UKY7; -.
DR PeptideAtlas; Q9UKY7; -.
DR PRIDE; Q9UKY7; -.
DR ProteomicsDB; 84914; -. [Q9UKY7-1]
DR ProteomicsDB; 84915; -. [Q9UKY7-2]
DR ProteomicsDB; 84916; -. [Q9UKY7-3]
DR TopDownProteomics; Q9UKY7-1; -. [Q9UKY7-1]
DR TopDownProteomics; Q9UKY7-2; -. [Q9UKY7-2]
DR TopDownProteomics; Q9UKY7-3; -. [Q9UKY7-3]
DR Antibodypedia; 33371; 89 antibodies from 17 providers.
DR DNASU; 55573; -.
DR Ensembl; ENST00000264993.8; ENSP00000264993.3; ENSG00000091527.17. [Q9UKY7-1]
DR Ensembl; ENST00000420115.6; ENSP00000413272.2; ENSG00000091527.17. [Q9UKY7-3]
DR Ensembl; ENST00000431519.6; ENSP00000391955.2; ENSG00000091527.17. [Q9UKY7-2]
DR GeneID; 55573; -.
DR KEGG; hsa:55573; -.
DR MANE-Select; ENST00000264993.8; ENSP00000264993.3; NM_017548.5; NP_060018.1.
DR UCSC; uc003epp.5; human. [Q9UKY7-1]
DR CTD; 55573; -.
DR DisGeNET; 55573; -.
DR GeneCards; CDV3; -.
DR HGNC; HGNC:26928; CDV3.
DR HPA; ENSG00000091527; Low tissue specificity.
DR MIM; 618789; gene.
DR neXtProt; NX_Q9UKY7; -.
DR OpenTargets; ENSG00000091527; -.
DR PharmGKB; PA142672138; -.
DR VEuPathDB; HostDB:ENSG00000091527; -.
DR eggNOG; ENOG502QRFT; Eukaryota.
DR GeneTree; ENSGT00390000000805; -.
DR HOGENOM; CLU_089760_1_0_1; -.
DR InParanoid; Q9UKY7; -.
DR OMA; KNENQDP; -.
DR OrthoDB; 1568537at2759; -.
DR PhylomeDB; Q9UKY7; -.
DR TreeFam; TF315891; -.
DR PathwayCommons; Q9UKY7; -.
DR SignaLink; Q9UKY7; -.
DR BioGRID-ORCS; 55573; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; CDV3; human.
DR GenomeRNAi; 55573; -.
DR Pharos; Q9UKY7; Tbio.
DR PRO; PR:Q9UKY7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UKY7; protein.
DR Bgee; ENSG00000091527; Expressed in parietal pleura and 206 other tissues.
DR ExpressionAtlas; Q9UKY7; baseline and differential.
DR Genevisible; Q9UKY7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR InterPro; IPR026806; CDV3.
DR PANTHER; PTHR16284; PTHR16284; 1.
DR Pfam; PF15359; CDV3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..258
FT /note="Protein CDV3 homolog"
FT /id="PRO_0000299560"
FT REGION 1..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q4VAA2"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q4VAA2"
FT MOD_RES 244
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041357"
FT VAR_SEQ 209..213
FT /note="KDKEM -> NRYLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027760"
FT VAR_SEQ 210..212
FT /note="DKE -> YLK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041358"
FT VAR_SEQ 213..258
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041359"
FT VAR_SEQ 214..258
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027761"
SQ SEQUENCE 258 AA; 27335 MW; 4BE95D0C217EE346 CRC64;
MAETEERSLD NFFAKRDKKK KKERSNRAAS AAGAAGSAGG SSGAAGAAGG GAGAGTRPGD
GGTASAGAAG PGAATKAVTK DEDEWKELEQ KEVDYSGLRV QAMQISSEKE EDDNEKRQDP
GDNWEEGGGG GGGMEKSSGP WNKTAPVQAP PAPVIVTETP EPAMTSGVYR PPGARLTTTR
KTPQGPPEIY SDTQFPSLQS TAKHVESRKD KEMEKSFEVV RHKNRGRDEV SKNQALKLQL
DNQYAVLENQ KSSHSQYN
