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Q15398

- DLGP5_HUMAN

UniProt

Q15398 - DLGP5_HUMAN

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Protein

Disks large-associated protein 5

Gene
DLGAP5, DLG7, KIAA0008
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. cell-cell signaling Source: InterPro
  2. cell proliferation Source: UniProtKB
  3. dephosphorylation Source: GOC
  4. mitotic chromosome movement towards spindle pole Source: UniProtKB
  5. mitotic M phase Source: UniProtKB
  6. positive regulation of mitotic metaphase/anaphase transition Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
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 namesi
Name:DLGAP5
Synonyms:DLG7, KIAA0008
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:16864. DLGAP5.

Subcellular locationi

Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle
Note: Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. microtubule organizing center Source: HPA
  3. nucleus Source: UniProtKB
  4. spindle pole centrosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162383761.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 846846Disks large-associated protein 5PRO_0000174299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine; by CDK11 Publication
Modified residuei326 – 3261Phosphothreonine1 Publication
Modified residuei329 – 3291Phosphothreonine; by CDK12 Publications
Modified residuei338 – 3381Phosphothreonine1 Publication
Modified residuei401 – 4011Phosphothreonine; by CDK11 Publication
Modified residuei402 – 4021Phosphothreonine; by CDK11 Publication
Modified residuei618 – 6181Phosphoserine; by CDK12 Publications
Modified residuei627 – 6271Phosphoserine; by AURKA1 Publication
Modified residuei639 – 6391Phosphothreonine; by CDK11 Publication
Modified residuei642 – 6421Phosphoserine; by CDK11 Publication
Modified residuei662 – 6621Phosphoserine3 Publications
Modified residuei725 – 7251Phosphoserine; by AURKA3 Publications
Modified residuei757 – 7571Phosphoserine; by AURKA1 Publication
Modified residuei759 – 7591Phosphothreonine; by CDK11 Publication
Modified residuei777 – 7771Phosphoserine3 Publications
Modified residuei784 – 7841Phosphothreonine1 Publication
Modified residuei806 – 8061Phosphoserine2 Publications
Modified residuei812 – 8121Phosphoserine2 Publications
Modified residuei830 – 8301Phosphoserine; by AURKA2 Publications
Modified residuei839 – 8391Phosphoserine; by CDK12 Publications

Post-translational modificationi

Ubiquitinated, leading to its degradation.1 Publication
Decreased phosphorylation levels are associated with the differentiation of intestinal epithelial cells.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15398.
PaxDbiQ15398.
PRIDEiQ15398.

PTM databases

PhosphoSiteiQ15398.

Expressioni

Tissue specificityi

Abundantly expressed in fetal liver. Expressed at lower levels in bone marrow, testis, colon, and placenta.1 Publication

Developmental stagei

Elevated levels of expression detected in the G2/M phase of synchronized cultures of HeLa cells.1 Publication

Gene expression databases

ArrayExpressiQ15398.
BgeeiQ15398.
CleanExiHS_DLGAP5.
GenevestigatoriQ15398.

Organism-specific databases

HPAiHPA005546.

Interactioni

Subunit structurei

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 CDH1.2 Publications

Protein-protein interaction databases

BioGridi115131. 8 interactions.
IntActiQ15398. 2 interactions.
MINTiMINT-1465344.
STRINGi9606.ENSP00000247191.

Structurei

3D structure databases

ProteinModelPortaliQ15398.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili90 – 12031 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the SAPAP family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG270787.
HOGENOMiHOG000054220.
HOVERGENiHBG062172.
KOiK16804.
OMAiFAPKDFM.
OrthoDBiEOG75QR37.
PhylomeDBiQ15398.
TreeFamiTF321382.

Family and domain databases

InterProiIPR005026. GKAP.
[Graphical view]
PfamiPF03359. GKAP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15398-2) [UniParc]FASTAAdd to Basket

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.

« Hide

MSSSHFASRH RKDISTEMIR TKIAHRKSLS QKENRHKEYE RNRHFGLKDV    50
NIPTLEGRIL VELDETSQGL VPEKTNVKPR AMKTILGDQR KQMLQKYKEE 100
KQLQKLKEQR EKAKRGIFKV GRYRPDMPCF LLSNQNAVKA EPKKAIPSSV 150
RITRSKAKDQ MEQTKIDNES DVRAIRPGPR QTSEKKVSDK EKKVVQPVMP 200
TSLRMTRSAT QAAKQVPRTV SSTTARKPVT RAANENEPEG KVPSKGRPAK 250
NVETKPDKGI SCKVDSEENT LNSQTNATSG MNPDGVLSKM ENLPEINTAK 300
IKGKNSFAPK DFMFQPLDGL KTYQVTPMTP RSANAFLTPS YTWTPLKTEV 350
DESQATKEIL AQKCKTYSTK TIQQDSNKLP CPLGPLTVWH EEHVLNKNEA 400
TTKNLNGLPI KEVPSLERNE GRIAQPHHGV PYFRNILQSE TEKLTSHCFE 450
WDRKLELDIP DDAKDLIRTA VGQTRLLMKE RFKQFEGLVD DCEYKRGIKE 500
TTCTDLDGFW DMVSFQIEDV IHKFNNLIKL EESGWQVNNN MNHNMNKNVF 550
RKKVVSGIAS KPKQDDAGRI AARNRLAAIK NAMRERIRQE ECAETAVSVI 600
PKEVDKIVFD AGFFRVESPV KLFSGLSVSS EGPSQRLGTP KSVNKAVSQS 650
RNEMGIPQQT TSPENAGPQN TKSEHVKKTL FLSIPESRSS IEDAQCPGLP 700
DLIEENHVVN KTDLKVDCLS SERMSLPLLA GGVADDINTN KKEGISDVVE 750
GMELNSSITS QDVLMSSPEK NTASQNSILE EGETKISQSE LFDNKSLTTE 800
CHLLDSPGLN CSNPFTQLER RHQEHARHIS FGGNLITFSP LQPGEF 846
Length:846
Mass (Da):95,115
Last modified:September 13, 2005 - v2
Checksum:i588BAF238D6FFB72
GO
Isoform 2 (identifier: Q15398-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Note: No experimental confirmation available.

Show »
Length:765
Mass (Da):85,668
Checksum:i00AFF91A02387EA1
GO
Isoform 3 (identifier: Q15398-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     807-846: PGLNCSNPFT...TFSPLQPGEF → VGSCYVARAG...AGTTARSKLQ

Note: No experimental confirmation available.

Show »
Length:842
Mass (Da):94,178
Checksum:iFDEF1E4B900F758C
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691G → E.1 Publication
Corresponds to variant rs2274271 [ dbSNP | Ensembl ].
VAR_023774
Natural varianti324 – 3241Q → H.
Corresponds to variant rs8010791 [ dbSNP | Ensembl ].
VAR_057718
Natural varianti469 – 4691T → I.
Corresponds to variant rs17128275 [ dbSNP | Ensembl ].
VAR_057719
Natural varianti753 – 7531E → Q.
Corresponds to variant rs35954941 [ dbSNP | Ensembl ].
VAR_062147

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8181Missing in isoform 2. VSP_015550Add
BLAST
Alternative sequencei807 – 84640PGLNC…QPGEF → VGSCYVARAGLEVLGSSDPT TSASRVAGTTARSKLQ in isoform 3. VSP_045341Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531E → K in BAA02797. 1 Publication
Sequence conflicti328 – 3281M → T in BAG61340. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS53897.1. [Q15398-3]
CCDS9723.1. [Q15398-2]
RefSeqiNP_001139487.1. NM_001146015.1. [Q15398-3]
NP_055565.3. NM_014750.4. [Q15398-2]
UniGeneiHs.77695.

Genome annotation databases

EnsembliENST00000247191; ENSP00000247191; ENSG00000126787. [Q15398-2]
ENST00000395425; ENSP00000378815; ENSG00000126787. [Q15398-3]
GeneIDi9787.
KEGGihsa:9787.
UCSCiuc001xbs.3. human. [Q15398-2]
uc001xbt.3. human.

Polymorphism databases

DMDMi82592583.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS53897.1. [Q15398-3 ]
CCDS9723.1. [Q15398-2 ]
RefSeqi NP_001139487.1. NM_001146015.1. [Q15398-3 ]
NP_055565.3. NM_014750.4. [Q15398-2 ]
UniGenei Hs.77695.

3D structure databases

ProteinModelPortali Q15398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115131. 8 interactions.
IntActi Q15398. 2 interactions.
MINTi MINT-1465344.
STRINGi 9606.ENSP00000247191.

PTM databases

PhosphoSitei Q15398.

Polymorphism databases

DMDMi 82592583.

Proteomic databases

MaxQBi Q15398.
PaxDbi Q15398.
PRIDEi Q15398.

Protocols and materials databases

DNASUi 9787.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247191 ; ENSP00000247191 ; ENSG00000126787 . [Q15398-2 ]
ENST00000395425 ; ENSP00000378815 ; ENSG00000126787 . [Q15398-3 ]
GeneIDi 9787.
KEGGi hsa:9787.
UCSCi uc001xbs.3. human. [Q15398-2 ]
uc001xbt.3. human.

Organism-specific databases

CTDi 9787.
GeneCardsi GC14M055614.
H-InvDB HIX0011684.
HGNCi HGNC:16864. DLGAP5.
HPAi HPA005546.
neXtProti NX_Q15398.
PharmGKBi PA162383761.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270787.
HOGENOMi HOG000054220.
HOVERGENi HBG062172.
KOi K16804.
OMAi FAPKDFM.
OrthoDBi EOG75QR37.
PhylomeDBi Q15398.
TreeFami TF321382.

Miscellaneous databases

GeneWikii DLGAP5.
GenomeRNAii 9787.
NextBioi 36854.
PROi Q15398.

Gene expression databases

ArrayExpressi Q15398.
Bgeei Q15398.
CleanExi HS_DLGAP5.
Genevestigatori Q15398.

Family and domain databases

InterProi IPR005026. GKAP.
[Graphical view ]
Pfami PF03359. GKAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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].

Entry informationi

Entry nameiDLGP5_HUMAN
AccessioniPrimary (citable) accession number: Q15398
Secondary accession number(s): A8MTM6
, B4DRM8, Q86T11, Q8NG58
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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