DEP1A_HUMAN
ID DEP1A_HUMAN Reviewed; 811 AA.
AC Q5TB30; A8QXE0; A8QXE1; Q05DU3; Q5TB28; Q9H9I3; Q9NX21; Q9NXZ0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=DEP domain-containing protein 1A;
GN Name=DEPDC1; Synonyms=DEPDC1A;
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 2).
RC TISSUE=Rhabdomyosarcoma;
RA Martelange V.;
RL Thesis (2000), Universite Catholique de Louvain / Bruxelles, Belgium.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Urinary bladder carcinoma;
RX PubMed=17452976; DOI=10.1038/sj.onc.1210466;
RA Kanehira M., Harada Y., Takata R., Shuin T., Miki T., Fujioka T.,
RA Nakamura Y., Katagiri T.;
RT "Involvement of upregulation of DEPDC1 (DEP domain containing 1) in bladder
RT carcinogenesis.";
RL Oncogene 26:6448-6455(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-354 (ISOFORM 1).
RC TISSUE=Placenta, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-811 (ISOFORM 1).
RC TISSUE=Signet-ring cell carcinoma, and Teratocarcinoma;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZNF224.
RX PubMed=20587513; DOI=10.1158/0008-5472.can-10-0255;
RA Harada Y., Kanehira M., Fujisawa Y., Takata R., Shuin T., Miki T.,
RA Fujioka T., Nakamura Y., Katagiri T.;
RT "Cell-permeable peptide DEPDC1-ZNF224 interferes with transcriptional
RT repression and oncogenicity in bladder cancer cells.";
RL Cancer Res. 70:5829-5839(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP STRUCTURE BY NMR OF 11-108.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the dep domain from human dep domain-containing
RT protein 1.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation as a
CC transcriptional corepressor. The DEPDC1A-ZNF224 complex may play a
CC critical role in bladder carcinogenesis by repressing the transcription
CC of the A20 gene, leading to transport of NF-KB protein into the
CC nucleus, resulting in suppression of apoptosis of bladder cancer cells.
CC {ECO:0000269|PubMed:20587513}.
CC -!- SUBUNIT: Isoform 2 and isoform 5 can form homodimers and heterodimers.
CC Interacts with ZNF224. {ECO:0000269|PubMed:17452976,
CC ECO:0000269|PubMed:20587513}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17452976,
CC ECO:0000269|PubMed:20587513}. Note=Colocalizes with ZNF224 at the
CC nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=DEPDC1-V1;
CC IsoId=Q5TB30-5; Sequence=Displayed;
CC Name=2; Synonyms=DEPDC1-V2;
CC IsoId=Q5TB30-2; Sequence=VSP_024652, VSP_024653;
CC -!- TISSUE SPECIFICITY: Expressed in testis. Up-regulated in bladder cancer
CC cells (at protein level). {ECO:0000269|PubMed:17452976}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03511.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91201.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14246.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14246.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ278112; CAB92444.1; -; mRNA.
DR EMBL; AB281187; BAF91373.1; -; mRNA.
DR EMBL; AB281274; BAF91374.1; -; mRNA.
DR EMBL; AL138789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06475.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06476.1; -; Genomic_DNA.
DR EMBL; BC003511; AAH03511.1; ALT_SEQ; mRNA.
DR EMBL; BC065304; AAH65304.1; -; mRNA.
DR EMBL; AK000490; BAA91201.1; ALT_INIT; mRNA.
DR EMBL; AK022792; BAB14246.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44159.1; -. [Q5TB30-5]
DR CCDS; CCDS644.1; -. [Q5TB30-2]
DR RefSeq; NP_001107592.1; NM_001114120.2. [Q5TB30-5]
DR RefSeq; NP_060249.2; NM_017779.5. [Q5TB30-2]
DR PDB; 2YSR; NMR; -; A=11-108.
DR PDBsum; 2YSR; -.
DR AlphaFoldDB; Q5TB30; -.
DR SMR; Q5TB30; -.
DR BioGRID; 120774; 117.
DR IntAct; Q5TB30; 22.
DR MINT; Q5TB30; -.
DR STRING; 9606.ENSP00000412292; -.
DR iPTMnet; Q5TB30; -.
DR PhosphoSitePlus; Q5TB30; -.
DR BioMuta; DEPDC1; -.
DR DMDM; 300669641; -.
DR EPD; Q5TB30; -.
DR jPOST; Q5TB30; -.
DR MassIVE; Q5TB30; -.
DR MaxQB; Q5TB30; -.
DR PaxDb; Q5TB30; -.
DR PeptideAtlas; Q5TB30; -.
DR PRIDE; Q5TB30; -.
DR ProteomicsDB; 64887; -. [Q5TB30-5]
DR ProteomicsDB; 64888; -. [Q5TB30-2]
DR Antibodypedia; 33419; 151 antibodies from 20 providers.
DR DNASU; 55635; -.
DR Ensembl; ENST00000370966.9; ENSP00000360005.5; ENSG00000024526.17. [Q5TB30-2]
DR Ensembl; ENST00000456315.7; ENSP00000412292.2; ENSG00000024526.17. [Q5TB30-5]
DR GeneID; 55635; -.
DR KEGG; hsa:55635; -.
DR MANE-Select; ENST00000456315.7; ENSP00000412292.2; NM_001114120.3; NP_001107592.1.
DR UCSC; uc001del.5; human. [Q5TB30-5]
DR CTD; 55635; -.
DR DisGeNET; 55635; -.
DR GeneCards; DEPDC1; -.
DR HGNC; HGNC:22949; DEPDC1.
DR HPA; ENSG00000024526; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 612002; gene.
DR neXtProt; NX_Q5TB30; -.
DR OpenTargets; ENSG00000024526; -.
DR PharmGKB; PA134974825; -.
DR VEuPathDB; HostDB:ENSG00000024526; -.
DR eggNOG; ENOG502QR00; Eukaryota.
DR GeneTree; ENSGT00950000182976; -.
DR HOGENOM; CLU_019607_0_0_1; -.
DR InParanoid; Q5TB30; -.
DR OMA; VPQYVMY; -.
DR OrthoDB; 413007at2759; -.
DR PhylomeDB; Q5TB30; -.
DR TreeFam; TF328365; -.
DR PathwayCommons; Q5TB30; -.
DR SignaLink; Q5TB30; -.
DR BioGRID-ORCS; 55635; 27 hits in 1077 CRISPR screens.
DR EvolutionaryTrace; Q5TB30; -.
DR GenomeRNAi; 55635; -.
DR Pharos; Q5TB30; Tbio.
DR PRO; PR:Q5TB30; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TB30; protein.
DR Bgee; ENSG00000024526; Expressed in ventricular zone and 118 other tissues.
DR ExpressionAtlas; Q5TB30; baseline and differential.
DR Genevisible; Q5TB30; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR SMART; SM00049; DEP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50186; DEP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTPase activation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..811
FT /note="DEP domain-containing protein 1A"
FT /id="PRO_0000284786"
FT DOMAIN 24..108
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 281..321
FT /note="Rho-GAP"
FT REGION 598..653
FT /note="Interaction with ZNF224"
FT /evidence="ECO:0000269|PubMed:20587513"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 304
FT /note="V -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17452976, ECO:0000303|Ref.1"
FT /id="VSP_024652"
FT VAR_SEQ 305..588
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17452976, ECO:0000303|Ref.1"
FT /id="VSP_024653"
FT VARIANT 404
FT /note="I -> R (in dbSNP:rs3790479)"
FT /id="VAR_059798"
FT CONFLICT 720
FT /note="S -> P (in Ref. 6; BAA91201)"
FT /evidence="ECO:0000305"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:2YSR"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2YSR"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:2YSR"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2YSR"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2YSR"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:2YSR"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2YSR"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2YSR"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2YSR"
SQ SEQUENCE 811 AA; 92960 MW; F694E10FB79AF3B0 CRC64;
MESQGVPPGP YRATKLWNEV TTSFRAGMPL RKHRQHFKKY GNCFTAGEAV DWLYDLLRNN
SNFGPEVTRQ QTIQLLRKFL KNHVIEDIKG RWGSENVDDN NQLFRFPATS PLKTLPRRYP
ELRKNNIENF SKDKDSIFKL RNLSRRTPKR HGLHLSQENG EKIKHEIINE DQENAIDNRE
LSQEDVEEVW RYVILIYLQT ILGVPSLEEV INPKQVIPQY IMYNMANTSK RGVVILQNKS
DDLPHWVLSA MKCLANWPRS NDMNNPTYVG FERDVFRTIA DYFLDLPEPL LTFEYYELFV
NILVVCGYIT VSDRSSGIHK IQDDPQSSKF LHLNNLNSFK STECLLLSLL HREKNKEESD
STERLQISNP GFQERCAKKM QLVNLRNRRV SANDIMGGSC HNLIGLSNMH DLSSNSKPRC
CSLEGIVDVP GNSSKEASSV FHQSFPNIEG QNNKLFLESK PKQEFLLNLH SEENIQKPFS
AGFKRTSTLT VQDQEELCNG KCKSKQLCRS QSLLLRSSTR RNSYINTPVA EIIMKPNVGQ
GSTSVQTAME SELGESSATI NKRLCKSTIE LSENSLLPAS SMLTGTQSLL QPHLERVAID
ALQLCCLLLP PPNRRKLQLL MRMISRMSQN VDMPKLHDAM GTRSLMIHTF SRCVLCCAEE
VDLDELLAGR LVSFLMDHHQ EILQVPSYLQ TAVEKHLDYL KKGHIENPGD GLFAPLPTYS
YCKQISAQEF DEQKVSTSQA AIAELLENII KNRSLPLKEK RKKLKQFQKE YPLIYQKRFP
TTESEAALFG DKPTIKQPML ILRKPKFRSL R
