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Q15398 (DLGP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:DLGAP5
Synonyms:DLG7, KIAA0008
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length846 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Cytoplasmcytoskeletonspindle. 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 846846Disks large-associated protein 5
PRO_0000174299

Regions

Coiled coil90 – 12031 Potential

Amino acid modifications

Modified residue671Phosphoserine; by CDK1 Ref.11
Modified residue3261Phosphothreonine Ref.16
Modified residue3291Phosphothreonine; by CDK1 Ref.11 Ref.16
Modified residue3381Phosphothreonine Ref.16
Modified residue4011Phosphothreonine; by CDK1 Ref.11
Modified residue4021Phosphothreonine; by CDK1 Ref.11
Modified residue6181Phosphoserine; by CDK1 Ref.11 Ref.16
Modified residue6271Phosphoserine; by AURKA Ref.12
Modified residue6391Phosphothreonine; by CDK1 Ref.11
Modified residue6421Phosphoserine; by CDK1 Ref.11
Modified residue6621Phosphoserine Ref.16 Ref.17 Ref.19
Modified residue7251Phosphoserine; by AURKA Ref.12 Ref.16 Ref.17
Modified residue7571Phosphoserine; by AURKA Ref.12
Modified residue7591Phosphothreonine; by CDK1 Ref.11
Modified residue7771Phosphoserine Ref.14 Ref.17 Ref.19
Modified residue7841Phosphothreonine Ref.16
Modified residue8061Phosphoserine Ref.15 Ref.16
Modified residue8121Phosphoserine Ref.15 Ref.16
Modified residue8301Phosphoserine; by AURKA Ref.12 Ref.17
Modified residue8391Phosphoserine; by CDK1 Ref.11 Ref.17

Natural variations

Alternative sequence1 – 8181Missing in isoform 2.
VSP_015550
Alternative sequence807 – 84640PGLNC…QPGEF → VGSCYVARAGLEVLGSSDPT TSASRVAGTTARSKLQ in isoform 3.
VSP_045341
Natural variant691G → E. Ref.1
Corresponds to variant rs2274271 [ dbSNP | Ensembl ].
VAR_023774
Natural variant3241Q → H.
Corresponds to variant rs8010791 [ dbSNP | Ensembl ].
VAR_057718
Natural variant4691T → I.
Corresponds to variant rs17128275 [ dbSNP | Ensembl ].
VAR_057719
Natural variant7531E → Q.
Corresponds to variant rs35954941 [ dbSNP | Ensembl ].
VAR_062147

Experimental info

Sequence conflict2531E → K in BAA02797. Ref.2
Sequence conflict3281M → T in BAG61340. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 588BAF238D6FFB72

FASTA84695,115
        10         20         30         40         50         60 
MSSSHFASRH RKDISTEMIR TKIAHRKSLS QKENRHKEYE RNRHFGLKDV NIPTLEGRIL 

        70         80         90        100        110        120 
VELDETSQGL VPEKTNVKPR AMKTILGDQR KQMLQKYKEE KQLQKLKEQR EKAKRGIFKV 

       130        140        150        160        170        180 
GRYRPDMPCF LLSNQNAVKA EPKKAIPSSV RITRSKAKDQ MEQTKIDNES DVRAIRPGPR 

       190        200        210        220        230        240 
QTSEKKVSDK EKKVVQPVMP TSLRMTRSAT QAAKQVPRTV SSTTARKPVT RAANENEPEG 

       250        260        270        280        290        300 
KVPSKGRPAK NVETKPDKGI SCKVDSEENT LNSQTNATSG MNPDGVLSKM ENLPEINTAK 

       310        320        330        340        350        360 
IKGKNSFAPK DFMFQPLDGL KTYQVTPMTP RSANAFLTPS YTWTPLKTEV DESQATKEIL 

       370        380        390        400        410        420 
AQKCKTYSTK TIQQDSNKLP CPLGPLTVWH EEHVLNKNEA TTKNLNGLPI KEVPSLERNE 

       430        440        450        460        470        480 
GRIAQPHHGV PYFRNILQSE TEKLTSHCFE WDRKLELDIP DDAKDLIRTA VGQTRLLMKE 

       490        500        510        520        530        540 
RFKQFEGLVD DCEYKRGIKE TTCTDLDGFW DMVSFQIEDV IHKFNNLIKL EESGWQVNNN 

       550        560        570        580        590        600 
MNHNMNKNVF RKKVVSGIAS KPKQDDAGRI AARNRLAAIK NAMRERIRQE ECAETAVSVI 

       610        620        630        640        650        660 
PKEVDKIVFD AGFFRVESPV KLFSGLSVSS EGPSQRLGTP KSVNKAVSQS RNEMGIPQQT 

       670        680        690        700        710        720 
TSPENAGPQN TKSEHVKKTL FLSIPESRSS IEDAQCPGLP DLIEENHVVN KTDLKVDCLS 

       730        740        750        760        770        780 
SERMSLPLLA GGVADDINTN KKEGISDVVE GMELNSSITS QDVLMSSPEK NTASQNSILE 

       790        800        810        820        830        840 
EGETKISQSE LFDNKSLTTE CHLLDSPGLN CSNPFTQLER RHQEHARHIS FGGNLITFSP 


LQPGEF 

« Hide

Isoform 2 [UniParc].

Checksum: 00AFF91A02387EA1
Show »

FASTA76585,668
Isoform 3 [UniParc].

Checksum: FDEF1E4B900F758C
Show »

FASTA84294,178

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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS53897.1. [Q15398-3]
CCDS9723.1. [Q15398-2]
RefSeqNP_001139487.1. NM_001146015.1. [Q15398-3]
NP_055565.3. NM_014750.4. [Q15398-2]
UniGeneHs.77695.

3D structure databases

ProteinModelPortalQ15398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115131. 8 interactions.
IntActQ15398. 2 interactions.
MINTMINT-1465344.
STRING9606.ENSP00000247191.

PTM databases

PhosphoSiteQ15398.

Polymorphism databases

DMDM82592583.

Proteomic databases

MaxQBQ15398.
PaxDbQ15398.
PRIDEQ15398.

Protocols and materials databases

DNASU9787.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247191; ENSP00000247191; ENSG00000126787. [Q15398-2]
ENST00000395425; ENSP00000378815; ENSG00000126787. [Q15398-3]
GeneID9787.
KEGGhsa:9787.
UCSCuc001xbs.3. human. [Q15398-2]
uc001xbt.3. human.

Organism-specific databases

CTD9787.
GeneCardsGC14M055614.
H-InvDBHIX0011684.
HGNCHGNC:16864. DLGAP5.
HPAHPA005546.
neXtProtNX_Q15398.
PharmGKBPA162383761.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270787.
HOGENOMHOG000054220.
HOVERGENHBG062172.
KOK16804.
OMAFAPKDFM.
OrthoDBEOG75QR37.
PhylomeDBQ15398.
TreeFamTF321382.

Gene expression databases

ArrayExpressQ15398.
BgeeQ15398.
CleanExHS_DLGAP5.
GenevestigatorQ15398.

Family and domain databases

InterProIPR005026. GKAP.
[Graphical view]
PfamPF03359. GKAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDLGAP5.
GenomeRNAi9787.
NextBio36854.
PROQ15398.

Entry information

Entry nameDLGP5_HUMAN
AccessionPrimary (citable) accession number: Q15398
Secondary accession number(s): A8MTM6 expand/collapse secondary AC list , B4DRM8, Q86T11, Q8NG58
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM