DLGP5_HUMAN
ID DLGP5_HUMAN Reviewed; 846 AA.
AC Q15398; A8MTM6; B4DRM8; Q86T11; Q8NG58;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Disks large-associated protein 5;
DE Short=DAP-5;
DE AltName: Full=Discs large homolog 7;
DE AltName: Full=Disks large-associated protein DLG7;
DE AltName: Full=Hepatoma up-regulated protein;
DE Short=HURP;
GN Name=DLGAP5; Synonyms=DLG7, KIAA0008;
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), VARIANT GLU-69, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12527899; DOI=10.1038/sj.onc.1206129;
RA Tsou A.-P., Yang C.-W., Huang C.-Y.F., Yu R.C.-T., Lee Y.-C.G.,
RA Chang C.-W., Chen B.-R., Chung Y.-F., Fann M.-J., Chi C.-W., Chiu J.-H.,
RA Chou C.-K.;
RT "Identification of a novel cell cycle regulated gene, HURP, overexpressed
RT in human hepatocellular carcinoma.";
RL Oncogene 22:298-307(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [3]
RP SEQUENCE REVISION TO 253.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=T-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Lung;
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 [10]
RP FUNCTION, INTERACTION WITH CDH1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=14699157; DOI=10.1074/jbc.m309843200;
RA Laprise P., Viel A., Rivard N.;
RT "Human homolog of disc-large is required for adherens junction assembly and
RT differentiation of human intestinal epithelial cells.";
RL J. Biol. Chem. 279:10157-10166(2004).
RN [11]
RP FUNCTION, INTERACTION WITH CDK1; FBXO7 AND SCF COMPLEX, UBIQUITINATION, AND
RP PHOSPHORYLATION AT SER-67; THR-329; THR-401; THR-402; SER-618; THR-639;
RP SER-642; THR-759 AND SER-839.
RX PubMed=15145941; DOI=10.1074/jbc.m404950200;
RA Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.;
RT "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated
RT hepatoma up-regulated protein (HURP) proteolysis by a proline-rich
RT region.";
RL J. Biol. Chem. 279:32592-32602(2004).
RN [12]
RP PHOSPHORYLATION AT SER-627; SER-725; SER-757 AND SER-830.
RX PubMed=15987997; DOI=10.1128/mcb.25.14.5789-5800.2005;
RA Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.;
RT "Phosphorylation and stabilization of HURP by Aurora-A: implication of HURP
RT as a transforming target of Aurora-A.";
RL Mol. Cell. Biol. 25:5789-5800(2005).
RN [13]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15561729; DOI=10.1074/mcp.m400158-mcp200;
RA Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W.;
RT "Proteome analysis of the human mitotic spindle.";
RL Mol. Cell. Proteomics 4:35-43(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-806 AND SER-812, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326; THR-329; THR-338;
RP SER-618; SER-662; SER-725; THR-784; SER-806 AND SER-812, AND IDENTIFICATION
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-725; SER-777;
RP SER-830 AND SER-839, 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-777, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-202; SER-618;
RP SER-627; SER-629; SER-634; SER-662; SER-725; SER-774; SER-777 AND SER-806,
RP 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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-347, AND IDENTIFICATION BY MASS
RP 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 -!- FUNCTION: Potential cell cycle regulator that may play a role in
CC carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the
CC ubiquitin-proteasome pathway. Key regulator of adherens junction
CC integrity and differentiation that may be involved in CDH1-mediated
CC adhesion and signaling in epithelial cells.
CC {ECO:0000269|PubMed:12527899, ECO:0000269|PubMed:14699157,
CC ECO:0000269|PubMed:15145941}.
CC -!- SUBUNIT: Interacts with CDK1. Interacts with the C-terminal proline-
CC rich region of FBXO7. Recruited by FBXO7 to a SCF (SKP1-CUL1-F-box)
CC protein complex in a CDK1/Cyclin B-phosphorylation dependent manner.
CC Interacts with CDH1. {ECO:0000269|PubMed:14699157,
CC ECO:0000269|PubMed:15145941}.
CC -!- INTERACTION:
CC Q15398; Q08379: GOLGA2; NbExp=3; IntAct=EBI-748280, EBI-618309;
CC Q15398; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-748280, EBI-742948;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
CC spindle. Note=Localizes to the spindle in mitotic cells. Colocalizes
CC with CDH1 at sites of cell-cell contact in intestinal epithelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15398-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15398-1; Sequence=VSP_015550;
CC Name=3;
CC IsoId=Q15398-3; Sequence=VSP_045341;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in fetal liver. Expressed at
CC lower levels in bone marrow, testis, colon, and placenta.
CC {ECO:0000269|PubMed:12527899}.
CC -!- DEVELOPMENTAL STAGE: Elevated levels of expression detected in the G2/M
CC phase of synchronized cultures of HeLa cells.
CC {ECO:0000269|PubMed:12527899}.
CC -!- PTM: Ubiquitinated, leading to its degradation.
CC {ECO:0000269|PubMed:15145941}.
CC -!- PTM: Decreased phosphorylation levels are associated with the
CC differentiation of intestinal epithelial cells.
CC {ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15145941,
CC ECO:0000269|PubMed:15987997}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
CC -!- CAUTION: It was localized to the spindle and the spindle pole
CC (PubMed:12527899) but was later found to be localized to the spindle
CC and to be excluded from the spindle pole (PubMed:15561729).
CC {ECO:0000305|PubMed:12527899, ECO:0000305|PubMed:15561729}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02797.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD62583.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB076695; BAB97376.1; -; mRNA.
DR EMBL; D13633; BAA02797.3; ALT_INIT; mRNA.
DR EMBL; BX248255; CAD62583.1; ALT_INIT; mRNA.
DR EMBL; BT007344; AAP36008.1; -; mRNA.
DR EMBL; AK299338; BAG61340.1; -; mRNA.
DR EMBL; AL139316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80664.1; -; Genomic_DNA.
DR EMBL; BC010658; AAH10658.2; -; mRNA.
DR EMBL; BC016276; AAH16276.2; -; mRNA.
DR CCDS; CCDS53897.1; -. [Q15398-3]
DR CCDS; CCDS9723.1; -. [Q15398-2]
DR RefSeq; NP_001139487.1; NM_001146015.1. [Q15398-3]
DR RefSeq; NP_055565.3; NM_014750.4. [Q15398-2]
DR RefSeq; XP_016877329.1; XM_017021840.1. [Q15398-2]
DR AlphaFoldDB; Q15398; -.
DR SMR; Q15398; -.
DR BioGRID; 115131; 48.
DR ELM; Q15398; -.
DR IntAct; Q15398; 23.
DR MINT; Q15398; -.
DR STRING; 9606.ENSP00000247191; -.
DR GlyGen; Q15398; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15398; -.
DR MetOSite; Q15398; -.
DR PhosphoSitePlus; Q15398; -.
DR BioMuta; DLGAP5; -.
DR DMDM; 82592583; -.
DR CPTAC; CPTAC-1204; -.
DR CPTAC; CPTAC-1205; -.
DR EPD; Q15398; -.
DR jPOST; Q15398; -.
DR MassIVE; Q15398; -.
DR MaxQB; Q15398; -.
DR PaxDb; Q15398; -.
DR PeptideAtlas; Q15398; -.
DR PRIDE; Q15398; -.
DR ProteomicsDB; 2036; -.
DR ProteomicsDB; 60567; -. [Q15398-2]
DR ProteomicsDB; 60568; -. [Q15398-1]
DR ABCD; Q15398; 3 sequenced antibodies.
DR Antibodypedia; 5; 260 antibodies from 31 providers.
DR DNASU; 9787; -.
DR Ensembl; ENST00000247191.7; ENSP00000247191.2; ENSG00000126787.13. [Q15398-2]
DR Ensembl; ENST00000395425.6; ENSP00000378815.2; ENSG00000126787.13. [Q15398-3]
DR GeneID; 9787; -.
DR KEGG; hsa:9787; -.
DR MANE-Select; ENST00000247191.7; ENSP00000247191.2; NM_014750.5; NP_055565.3.
DR UCSC; uc001xbs.4; human. [Q15398-2]
DR CTD; 9787; -.
DR DisGeNET; 9787; -.
DR GeneCards; DLGAP5; -.
DR HGNC; HGNC:16864; DLGAP5.
DR HPA; ENSG00000126787; Group enriched (bone marrow, lymphoid tissue, testis).
DR MIM; 617859; gene.
DR neXtProt; NX_Q15398; -.
DR OpenTargets; ENSG00000126787; -.
DR PharmGKB; PA162383761; -.
DR VEuPathDB; HostDB:ENSG00000126787; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000158652; -.
DR HOGENOM; CLU_018126_0_0_1; -.
DR InParanoid; Q15398; -.
DR OMA; PSERMNL; -.
DR OrthoDB; 566337at2759; -.
DR PhylomeDB; Q15398; -.
DR TreeFam; TF321382; -.
DR PathwayCommons; Q15398; -.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR SignaLink; Q15398; -.
DR SIGNOR; Q15398; -.
DR BioGRID-ORCS; 9787; 52 hits in 1091 CRISPR screens.
DR ChiTaRS; DLGAP5; human.
DR GeneWiki; DLGAP5; -.
DR GenomeRNAi; 9787; -.
DR Pharos; Q15398; Tbio.
DR PRO; PR:Q15398; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q15398; protein.
DR Bgee; ENSG00000126787; Expressed in secondary oocyte and 125 other tissues.
DR ExpressionAtlas; Q15398; baseline and differential.
DR Genevisible; Q15398; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051382; P:kinetochore assembly; IBA:GO_Central.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; NAS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; NAS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; IEA:InterPro.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..846
FT /note="Disks large-associated protein 5"
FT /id="PRO_0000174299"
FT REGION 153..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..120
FT /evidence="ECO:0000255"
FT COMPBIAS 155..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 329
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 401
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941"
FT MOD_RES 402
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941"
FT MOD_RES 618
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 627
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:15987997,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 639
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941"
FT MOD_RES 642
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 725
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:15987997,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 757
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:15987997"
FT MOD_RES 759
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 784
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 830
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:15987997,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 839
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15145941,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 347
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_015550"
FT VAR_SEQ 807..846
FT /note="PGLNCSNPFTQLERRHQEHARHISFGGNLITFSPLQPGEF -> VGSCYVAR
FT AGLEVLGSSDPTTSASRVAGTTARSKLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045341"
FT VARIANT 69
FT /note="G -> E (in dbSNP:rs2274271)"
FT /evidence="ECO:0000269|PubMed:12527899"
FT /id="VAR_023774"
FT VARIANT 324
FT /note="Q -> H (in dbSNP:rs8010791)"
FT /id="VAR_057718"
FT VARIANT 469
FT /note="T -> I (in dbSNP:rs17128275)"
FT /id="VAR_057719"
FT VARIANT 753
FT /note="E -> Q (in dbSNP:rs35954941)"
FT /id="VAR_062147"
FT CONFLICT 253
FT /note="E -> K (in Ref. 2; BAA02797)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="M -> T (in Ref. 6; BAG61340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 95115 MW; 588BAF238D6FFB72 CRC64;
MSSSHFASRH RKDISTEMIR TKIAHRKSLS QKENRHKEYE RNRHFGLKDV NIPTLEGRIL
VELDETSQGL VPEKTNVKPR AMKTILGDQR KQMLQKYKEE KQLQKLKEQR EKAKRGIFKV
GRYRPDMPCF LLSNQNAVKA EPKKAIPSSV RITRSKAKDQ MEQTKIDNES DVRAIRPGPR
QTSEKKVSDK EKKVVQPVMP TSLRMTRSAT QAAKQVPRTV SSTTARKPVT RAANENEPEG
KVPSKGRPAK NVETKPDKGI SCKVDSEENT LNSQTNATSG MNPDGVLSKM ENLPEINTAK
IKGKNSFAPK DFMFQPLDGL KTYQVTPMTP RSANAFLTPS YTWTPLKTEV DESQATKEIL
AQKCKTYSTK TIQQDSNKLP CPLGPLTVWH EEHVLNKNEA TTKNLNGLPI KEVPSLERNE
GRIAQPHHGV PYFRNILQSE TEKLTSHCFE WDRKLELDIP DDAKDLIRTA VGQTRLLMKE
RFKQFEGLVD DCEYKRGIKE TTCTDLDGFW DMVSFQIEDV IHKFNNLIKL EESGWQVNNN
MNHNMNKNVF RKKVVSGIAS KPKQDDAGRI AARNRLAAIK NAMRERIRQE ECAETAVSVI
PKEVDKIVFD AGFFRVESPV KLFSGLSVSS EGPSQRLGTP KSVNKAVSQS RNEMGIPQQT
TSPENAGPQN TKSEHVKKTL FLSIPESRSS IEDAQCPGLP DLIEENHVVN KTDLKVDCLS
SERMSLPLLA GGVADDINTN KKEGISDVVE GMELNSSITS QDVLMSSPEK NTASQNSILE
EGETKISQSE LFDNKSLTTE CHLLDSPGLN CSNPFTQLER RHQEHARHIS FGGNLITFSP
LQPGEF
