Q15398 (DLGP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 112.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Disks large-associated protein 5 Short name=DAP-5 Alternative name(s): Discs large homolog 7 Disks large-associated protein DLG7 Hepatoma up-regulated protein Short name=HURP | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 846 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. Ref.1 Ref.10 Ref.11 |
| Subunit structure | Interacts with CDK1. Interacts with the C-terminal proline-rich region of FBXO7. Recruited by FBXO7 to a SCF (SKP1-CUL1-F-box) protein complex in a CDK1/Cyclin B-phosphorylation dependent manner. Interacts with CDH1. Ref.10 Ref.11 |
| Subcellular location | Nucleus. Cytoplasm. Cytoplasm › cytoskeleton › spindle. Note: Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells. Ref.1 Ref.10 Ref.13 |
| Tissue specificity | Abundantly expressed in fetal liver. Expressed at lower levels in bone marrow, testis, colon, and placenta. Ref.1 |
| Developmental stage | Elevated levels of expression detected in the G2/M phase of synchronized cultures of HeLa cells. Ref.1 |
| Post-translational modification | Ubiquitinated, leading to its degradation. Ref.11 Decreased phosphorylation levels are associated with the differentiation of intestinal epithelial cells. |
| Sequence similarities | Belongs to the SAPAP family. |
| Caution | It was localized to the spindle and the spindle pole (Ref.1) but was later found to be localized to the spindle and to be excluded from the spindle pole (Ref.13). |
| Sequence caution | The sequence BAA02797.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAD62583.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle |
| Cellular component | Cytoplasm Cytoskeleton Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil |
| PTM | Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell proliferation Non-traceable author statement Ref.1. Source: UniProtKB cell-cell signalingInferred from electronic annotation. Source: InterPro mitotic chromosome movement towards spindle poleNon-traceable author statement Ref.1. Source: UniProtKB positive regulation of mitotic metaphase/anaphase transitionNon-traceable author statement Ref.1. Source: UniProtKB |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from direct assay Ref.1. Source: UniProtKB spindle pole centrosomeInferred from direct assay Ref.1. Source: UniProtKB |
| Molecular_function | phosphoprotein phosphatase activity Inferred from direct assay Ref.11. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q15398-2) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q15398-1) The sequence of this isoform differs from the canonical sequence as follows: 1-81: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q15398-3) The sequence of this isoform differs from the canonical sequence as follows: 807-846: PGLNCSNPFT...TFSPLQPGEF → VGSCYVARAG...AGTTARSKLQ | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 846 | 846 | Disks large-associated protein 5 | PRO_0000174299 | |||||
Regions | |||||||||
| Coiled coil | 90 – 120 | 31 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 67 | 1 | Phosphoserine; by CDK1 Ref.11 | ||||||
| Modified residue | 219 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 326 | 1 | Phosphothreonine Ref.16 | ||||||
| Modified residue | 329 | 1 | Phosphothreonine; by CDK1 Ref.11 Ref.16 | ||||||
| Modified residue | 338 | 1 | Phosphothreonine Ref.16 | ||||||
| Modified residue | 401 | 1 | Phosphothreonine; by CDK1 Ref.11 | ||||||
| Modified residue | 402 | 1 | Phosphothreonine; by CDK1 Ref.11 | ||||||
| Modified residue | 618 | 1 | Phosphoserine; by CDK1 Ref.11 Ref.16 | ||||||
| Modified residue | 627 | 1 | Phosphoserine; by AURKA Ref.12 | ||||||
| Modified residue | 639 | 1 | Phosphothreonine; by CDK1 Ref.11 | ||||||
| Modified residue | 642 | 1 | Phosphoserine; by CDK1 Ref.11 | ||||||
| Modified residue | 662 | 1 | Phosphoserine Ref.16 Ref.17 Ref.19 | ||||||
| Modified residue | 725 | 1 | Phosphoserine; by AURKA Ref.12 Ref.16 Ref.17 | ||||||
| Modified residue | 757 | 1 | Phosphoserine; by AURKA Ref.12 | ||||||
| Modified residue | 759 | 1 | Phosphothreonine; by CDK1 Ref.11 | ||||||
| Modified residue | 777 | 1 | Phosphoserine Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 784 | 1 | Phosphothreonine Ref.16 | ||||||
| Modified residue | 806 | 1 | Phosphoserine Ref.15 Ref.16 | ||||||
| Modified residue | 812 | 1 | Phosphoserine Ref.15 Ref.16 | ||||||
| Modified residue | 830 | 1 | Phosphoserine; by AURKA Ref.12 Ref.17 | ||||||
| Modified residue | 839 | 1 | Phosphoserine; by CDK1 Ref.11 Ref.17 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 81 | 81 | Missing in isoform 2. | VSP_015550 | |||||
| Alternative sequence | 807 – 846 | 40 | PGLNC…QPGEF → VGSCYVARAGLEVLGSSDPT TSASRVAGTTARSKLQ in isoform 3. | VSP_045341 | |||||
| Natural variant | 69 | 1 | G → E. Ref.1 Corresponds to variant rs2274271 [ dbSNP | Ensembl ]. | VAR_023774 | |||||
| Natural variant | 324 | 1 | Q → H. Corresponds to variant rs8010791 [ dbSNP | Ensembl ]. | VAR_057718 | |||||
| Natural variant | 469 | 1 | T → I. Corresponds to variant rs17128275 [ dbSNP | Ensembl ]. | VAR_057719 | |||||
| Natural variant | 753 | 1 | E → Q. Corresponds to variant rs35954941 [ dbSNP | Ensembl ]. | VAR_062147 | |||||
Experimental info | |||||||||
| Sequence conflict | 253 | 1 | E → K in BAA02797. Ref.2 | ||||||
| Sequence conflict | 328 | 1 | M → T in BAG61340. Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of a novel cell cycle regulated gene, HURP, overexpressed in human hepatocellular carcinoma." Tsou A.-P., Yang C.-W., Huang C.-Y.F., Yu R.C.-T., Lee Y.-C.G., Chang C.-W., Chen B.-R., Chung Y.-F., Fann M.-J., Chi C.-W., Chiu J.-H., Chou C.-K. Oncogene 22:298-307(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-69, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. |
| [2] | "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow. |
| [3] | Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 253. |
| [4] | "Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: T-cell. |
| [5] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). |
| [6] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). |
| [7] | "The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. Weissenbach J.Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [8] | Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [9] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye and Lung. |
| [10] | "Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells." Laprise P., Viel A., Rivard N. J. Biol. Chem. 279:10157-10166(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDH1, SUBCELLULAR LOCATION, PHOSPHORYLATION. |
| [11] | "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region." Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F. J. Biol. Chem. 279:32592-32602(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDK1; FBXO7 AND SCF COMPLEX, UBIQUITINATION, PHOSPHORYLATION AT SER-67; THR-329; THR-401; THR-402; SER-618; THR-639; SER-642; THR-759 AND SER-839. |
| [12] | "Phosphorylation and stabilization of HURP by Aurora-A: implication of HURP as a transforming target of Aurora-A." Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y. Mol. Cell. Biol. 25:5789-5800(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-627; SER-725; SER-757 AND SER-830. |
| [13] | "Proteome analysis of the human mitotic spindle." Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W. Mol. Cell. Proteomics 4:35-43(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY. |
| [14] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-806 AND SER-812, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [16] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326; THR-329; THR-338; SER-618; SER-662; SER-725; THR-784; SER-806 AND SER-812, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-725; SER-777; SER-830 AND SER-839, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [19] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-777, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB076695 mRNA. Translation: BAB97376.1. D13633 mRNA. Translation: BAA02797.3. Different initiation. BX248255 mRNA. Translation: CAD62583.1. Different initiation. BT007344 mRNA. Translation: AAP36008.1. AK299338 mRNA. Translation: BAG61340.1. AL139316 Genomic DNA. No translation available. CH471061 Genomic DNA. Translation: EAW80664.1. BC010658 mRNA. Translation: AAH10658.2. BC016276 mRNA. Translation: AAH16276.2. |
| IPI | IPI00184997. IPI00647106. IPI00647892. |
| RefSeq | NP_001139487.1. NM_001146015.1. NP_055565.3. NM_014750.4. |
| UniGene | Hs.77695. |
3D structure databases | |
| ProteinModelPortal | Q15398. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q15398. 2 interactions. |
| STRING | 9606.ENSP00000247191. |
PTM databases | |
| PhosphoSite | Q15398. |
Polymorphism databases | |
| DMDM | 82592583. |
Proteomic databases | |
| PaxDb | Q15398. |
| PRIDE | Q15398. |
Protocols and materials databases | |
| DNASU | 9787. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000247191; ENSP00000247191; ENSG00000126787. ENST00000395425; ENSP00000378815; ENSG00000126787. |
| GeneID | 9787. |
| KEGG | hsa:9787. |
| UCSC | uc001xbs.3. human. |
Organism-specific databases | |
| CTD | 9787. |
| GeneCards | GC14M055614. |
| H-InvDB | HIX0011684. |
| HGNC | HGNC:16864. DLGAP5. |
| HPA | HPA005546. |
| neXtProt | NX_Q15398. |
| PharmGKB | PA162383761. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG270787. |
| HOGENOM | HOG000054220. |
| HOVERGEN | HBG062172. |
| KO | K16804. |
| OMA | FAPKDFM. |
| OrthoDB | EOG4RXXZQ. |
Enzyme and pathway databases | |
| Pathway_Interaction_DB | aurora_a_pathway. Aurora A signaling. |
Gene expression databases | |
| ArrayExpress | Q15398. |
| Bgee | Q15398. |
| CleanEx | HS_DLGAP5. |
| Genevestigator | Q15398. |
| GermOnline | ENSG00000126787. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR005026. GKAP. [Graphical view] |
| Pfam | PF03359. GKAP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| GenomeRNAi | 9787. |
| NextBio | 36854. |
Entry information
| Entry name | DLGP5_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q15398 Secondary accession number(s): A8MTM6 Q8NG58 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 14 Human chromosome 14: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| SIMILARITY comments Index of protein domains and families |

Clusters with
