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O14908 (GIPC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PDZ domain-containing protein GIPC1
Alternative name(s):
GAIP C-terminus-interacting protein
RGS-GAIP-interacting protein
RGS19-interacting protein 1
Synectin
Tax interaction protein 2
Short name=TIP-2
Gene names
Name:GIPC1
Synonyms:C19orf3, GIPC, RGS19IP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in G protein-linked signaling.

Subunit structure

Interacts with GLUT1 (C-terminus), ACTN1, KIF1B, MYO6, PLEKHG5, SDC4/syndecan-4 and SEMA4C/semaphorin-4C By similarity. Interacts with RGS19 C-terminus. Interacts with HTLV-I Tax through the PDZ domain. Ref.1 Ref.6

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein.

Tissue specificity

Widely expressed.

Sequence similarities

Belongs to the GIPC family.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Non-traceable author statement Ref.1. Source: UniProtKB

endothelial cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

glutamate secretion

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cytokinesis

Inferred from mutant phenotype PubMed 22888021. Source: UniProt

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

protein targeting

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of protein stability

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of synaptic plasticity

Inferred from sequence or structural similarity. Source: BHF-UCL

synaptic transmission

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentbrush border

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from direct assay PubMed 12857860. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 12857860. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic shaft

Inferred from sequence or structural similarity. Source: BHF-UCL

dendritic spine

Inferred from sequence or structural similarity. Source: BHF-UCL

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle

Inferred from sequence or structural similarity. Source: BHF-UCL

vesicle membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionactin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

myosin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 15459234. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TGFBR3Q031673EBI-373132,EBI-2852679
TYRP1P176433EBI-373132,EBI-7900408

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14908-1)

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: O14908-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333PDZ domain-containing protein GIPC1
PRO_0000087492

Regions

Domain133 – 21381PDZ
Compositional bias36 – 427Poly-Gly
Compositional bias48 – 525Poly-Pro

Amino acid modifications

Modified residue2251Phosphoserine Ref.8
Modified residue2321Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 9797Missing in isoform 2.
VSP_044296

Sequences

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

Last modified August 1, 1999. Version 2.
Checksum: AA980A4B907E3FD9

FASTA33336,049
        10         20         30         40         50         60 
MPLGLGRRKK APPLVENEEA EPGRGGLGVG EPGPLGGGGS GGPQMGLPPP PPALRPRLVF 

        70         80         90        100        110        120 
HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPTAEVMFC TLNTHKVDMD KLLGGQIGLE 

       130        140        150        160        170        180 
DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIH LISVGDMIEA 

       190        200        210        220        230        240 
INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGRP GSGPQLGTGR 

       250        260        270        280        290        300 
GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL 

       310        320        330 
AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY 

« Hide

Isoform 2 [UniParc].

Checksum: D1DEC176B95C53B1
Show »

FASTA23626,072

References

« Hide 'large scale' references
[1]"GIPC, a PDZ domain containing protein, interacts specifically with the C-terminus of RGS-GAIP."
De Vries L., Lou X., Zhao G., Zheng B., Farquhar M.G.
Proc. Natl. Acad. Sci. U.S.A. 95:12340-12345(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RGS19.
Tissue: Pituitary.
[2]"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 2).
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.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].
[5]"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: Lung and Muscle.
[6]"The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins."
Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.
Oncogene 16:643-654(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 78-333 (ISOFORM 1/2), INTERACTION WITH HTLV-I TAX.
[7]"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].
[8]"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-225 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF089816 mRNA. Translation: AAC67548.1.
AK290948 mRNA. Translation: BAF83637.1.
AC008569 Genomic DNA. No translation available.
AC012318 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84423.1.
CH471106 Genomic DNA. Translation: EAW84425.1.
BC000410 mRNA. Translation: AAH00410.1.
BC004226 mRNA. Translation: AAH04226.2.
BC012810 mRNA. Translation: AAH12810.1.
BC016169 mRNA. Translation: AAH16169.1.
AF028824 mRNA. Translation: AAB84249.1.
CCDSCCDS12310.1. [O14908-1]
CCDS12311.1. [O14908-2]
RefSeqNP_005707.1. NM_005716.3. [O14908-1]
NP_974197.1. NM_202468.2. [O14908-1]
NP_974198.1. NM_202469.2. [O14908-2]
NP_974199.1. NM_202470.2. [O14908-1]
NP_974223.1. NM_202494.2. [O14908-2]
UniGeneHs.655012.
Hs.741240.

3D structure databases

ProteinModelPortalO14908.
SMRO14908. Positions 127-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115978. 33 interactions.
IntActO14908. 10 interactions.
MINTMINT-5003771.
STRING9606.ENSP00000340698.

PTM databases

PhosphoSiteO14908.

Proteomic databases

MaxQBO14908.
PaxDbO14908.
PeptideAtlasO14908.
PRIDEO14908.

Protocols and materials databases

DNASU10755.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345425; ENSP00000340698; ENSG00000123159. [O14908-1]
ENST00000393028; ENSP00000376748; ENSG00000123159. [O14908-2]
ENST00000393029; ENSP00000376749; ENSG00000123159. [O14908-2]
ENST00000393033; ENSP00000376753; ENSG00000123159. [O14908-1]
ENST00000586027; ENSP00000466747; ENSG00000123159. [O14908-1]
ENST00000591349; ENSP00000467077; ENSG00000123159. [O14908-2]
GeneID10755.
KEGGhsa:10755.
UCSCuc002myt.4. human. [O14908-1]

Organism-specific databases

CTD10755.
GeneCardsGC19M014600.
HGNCHGNC:1226. GIPC1.
HPAHPA043958.
MIM605072. gene.
neXtProtNX_O14908.
PharmGKBPA34371.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313930.
HOGENOMHOG000293347.
HOVERGENHBG000898.
InParanoidO14908.
OMATHKVDME.
OrthoDBEOG793B86.
PhylomeDBO14908.
TreeFamTF313878.

Enzyme and pathway databases

SignaLinkO14908.

Gene expression databases

ArrayExpressO14908.
BgeeO14908.
CleanExHS_GIPC1.
GenevestigatorO14908.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
IPR017379. UCP038083_PDZ.
[Graphical view]
PfamPF00595. PDZ. 1 hit.
[Graphical view]
PIRSFPIRSF038083. UCP038083_GIPC. 1 hit.
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGIPC1. human.
GeneWikiGIPC1.
GenomeRNAi10755.
NextBio40843.
PROO14908.
SOURCESearch...

Entry information

Entry nameGIPC1_HUMAN
AccessionPrimary (citable) accession number: O14908
Secondary accession number(s): A8K4I3, A8MZG3, Q9BTC9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: August 1, 1999
Last modified: July 9, 2014
This is version 128 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM