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Q3V6T2 (GRDN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Girdin
Alternative name(s):
Akt phosphorylation enhancer
Short name=APE
Coiled-coil domain-containing protein 88A
G alpha-interacting vesicle-associated protein
Short name=GIV
Girders of actin filament
Hook-related protein 1
Short name=HkRP1
Gene names
Name:CCDC88A
Synonyms:APE, GRDN, KIAA1212
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1871 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB, but does not possess kinase activity itself. Phosphorylation of AKT1/PKB thereby induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation By similarity. Essential for the integrity of the actin cytoskeleton and for cell migration. Required for formation of actin stress fibers and lamellipodia. May be involved in membrane sorting in the early endosome. Ref.1 Ref.2

Subunit structure

Interacts (via C-terminus) with DISC1; the interaction is direct. Interacts with AKT proteins; the interaction is inhibited in presence of DISC1 By similarity. Homodimer. The non-phosphorylated form interacts with phosphatidylinositol 4-phosphate [PI4P] and weakly with phosphatidylinositol 3-phosphate [PI3P]. Interacts with microtubules. Interacts with actin through its C-terminal domain. Interacts with the C-terminus of AKT1/PKB. Ref.1

Subcellular location

Membrane. Cell membrane. Cytoplasmcytosol. Cytoplasmic vesicle. Cell projectionlamellipodium. Note: Localizes to the cell membrane through interaction with phosphoinositides. Ref.1 Ref.2 Ref.7

Tissue specificity

Expressed ubiquitously. Ref.1

Post-translational modification

Phosphorylation is induced by epidermal growth factor (EGF) in a phosphoinositide 3-kinase (PI3K)-dependent manner. Phosphorylation by AKT1/PKB is necessary for the delocalization from the cell membrane and for cell migration. Ref.1

Sequence similarities

Belongs to the CCDC88 family.

Sequence caution

The sequence AAY14932.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAD97945.1 differs from that shown. Reason: Intron retention at the C-terminus.

The sequence CAI46020.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDNA replication
Neurogenesis
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

TOR signaling

Inferred from sequence or structural similarity. Source: UniProtKB

activation of protein kinase B activity

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.1. Source: UniProtKB

lamellipodium assembly

Inferred from mutant phenotype Ref.1. Source: UniProtKB

membrane organization

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.2. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from direct assay Ref.2. Source: UniProtKB

cytosol

Inferred from direct assay Ref.7. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay Ref.2. Source: UniProtKB

lamellipodium

Inferred from direct assay Ref.1. Source: UniProtKB

membrane

Inferred from direct assay Ref.7Ref.2. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionactin binding

Inferred from direct assay Ref.1. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.1. Source: UniProtKB

protein kinase B binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.6 (identifier: Q3V6T2-1)

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 Ref.2 Ref.3 Ref.5 Ref.6 (identifier: Q3V6T2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T
Isoform 3 (identifier: Q3V6T2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.
Isoform 4 (identifier: Q3V6T2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T
Isoform 5 (identifier: Q3V6T2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.
     1733-1806: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18711871Girdin
PRO_0000287429

Regions

Region1390 – 140819Phosphoinositide-binding Ref.1
Coiled coil196 – 425230 Potential
Coiled coil458 – 1385928 Potential

Amino acid modifications

Modified residue13871Phosphoserine Ref.9 PubMed 16964243
Modified residue14171Phosphoserine; by PKB/AKT1 Ref.1
Modified residue16731Phosphothreonine Ref.9
Modified residue16751Phosphoserine By similarity UniProtKB Q5SNZ0
Modified residue18371Phosphoserine Ref.9

Natural variations

Alternative sequence9521Missing in isoform 3, isoform 4 and isoform 5.
VSP_040129
Alternative sequence1463 – 149129MVALK…RRSMS → T in isoform 2 and isoform 4. Ref.2 Ref.3 Ref.5 Ref.6
VSP_052409
Alternative sequence1733 – 180674Missing in isoform 5.
VSP_044943

Experimental info

Mutagenesis14171S → A: Disrupts actin organization, cell migration and lamellipodia formation. Ref.1
Sequence conflict10661K → E in CAI46020. Ref.6
Sequence conflict10811A → T in CAD97945. Ref.6
Sequence conflict16611S → P in CAD97945. Ref.6
Sequence conflict17101V → I in CAI46020. Ref.6
Sequence conflict17991Y → H in CAD98038. Ref.6
Sequence conflict18361D → G in CAI46020. Ref.6

Sequences

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

Last modified May 15, 2007. Version 2.
Checksum: 9DD2E06F2A235AA5

FASTA1,871216,042
        10         20         30         40         50         60 
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ VMLQINPKLE 

        70         80         90        100        110        120 
SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM SLPNVLIIGK NPFSEQGTEE 

       130        140        150        160        170        180 
VKKLLLLLLG CAVQCQKKEE FIERIQGLDF DTKAAVAAHI QEVTHNQENV FDLQWMEVTD 

       190        200        210        220        230        240 
MSQEDIEPLL KNMALHLKRL IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM 

       250        260        270        280        290        300 
KRTESRQHLS VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS 

       310        320        330        340        350        360 
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK EDNQVLLETK 

       370        380        390        400        410        420 
TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM DRKKIEELME ENMTLEMAQK 

       430        440        450        460        470        480 
QSMDESLHLG WELEQISRTS ELSEAPQKSL GHEVNELTSS RLLKLEMENQ SLTKTVEELR 

       490        500        510        520        530        540 
TTVDSVEGNA SKILKMEKEN QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK 

       550        560        570        580        590        600 
TIETLRENSE RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS 

       610        620        630        640        650        660 
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN LKITCEKIEA 

       670        680        690        700        710        720 
LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD EENLELRRNV ESLKCASMKM 

       730        740        750        760        770        780 
AQLQLENKEL ESEKEQLKKG LELLKASFKK TERLEVSYQG LDIENQRLQK TLENSNKKIQ 

       790        800        810        820        830        840 
QLESELQDLE MENQTLQKNL EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR 

       850        860        870        880        890        900 
LRQQAEIKDT TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID 

       910        920        930        940        950        960 
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD DSRYKLLESK 

       970        980        990       1000       1010       1020 
LESTLKKSLE IKEEKIAALE ARLEESTNYN QQLRQELKTV KKNYEALKQR QDEERMVQSS 

      1030       1040       1050       1060       1070       1080 
PPISGEDNKW ERESQETTRE LLKVKDRLIE VERNNATLQA EKQALKTQLK QLETQNNNLQ 

      1090       1100       1110       1120       1130       1140 
AQILALQRQT VSLQEQNTTL QTQNAKLQVE NSTLNSQSTS LMNQNAQLLI QQSSLENENE 

      1150       1160       1170       1180       1190       1200 
SVIKEREDLK SLYDSLIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHRDLED 

      1210       1220       1230       1240       1250       1260 
RYNQLLKQKG QLEDLEKMLK VEQEKMLLEN KNHETVAAEY KKLCGENDRL NHTYSQLLKE 

      1270       1280       1290       1300       1310       1320 
TEVLQTDHKN LKSLLNNSKL EQTRLEAEFS KLKEQYQQLD ITSTKLNNQC ELLSQLKGNL 

      1330       1340       1350       1360       1370       1380 
EEENRHLLDQ IQTLMLQNRT LLEQNMESKD LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ 

      1390       1400       1410       1420       1430       1440 
YKFYDPSPPR RRGNWITLKM RKLIKSKKDI NRERQKSLTL TPTRSDSSEG FLQLPHQDSQ 

      1450       1460       1470       1480       1490       1500 
DSSSVGSNSL EDGQTLGTKK SSMVALKRLP FLRNRPKDKD KMKACYRRSM SMNDLVQSMV 

      1510       1520       1530       1540       1550       1560 
LAGQWTGSTE NLEVPDDIST GKRRKELGAM AFSTTAINFS TVNSSAGFRS KQLVNNKDTT 

      1570       1580       1590       1600       1610       1620 
SFEDISPQGV SDDSSTGSRV HASRPASLDS GRTSTSNSNN NASLHEVKAG AVNNQSRPQS 

      1630       1640       1650       1660       1670       1680 
HSSGEFSLLH DHEAWSSSGS SPIQYLKRQT RSSPVLQHKI SETLESRHHK IKTGSPGSEV 

      1690       1700       1710       1720       1730       1740 
VTLQQFLEES NKLTSVQIKS SSQENLLDEV MKSLSVSSDF LGKDKPVSCG LARSVSGKTP 

      1750       1760       1770       1780       1790       1800 
GDFYDRRTTK PEFLRPGPRK TEDTYFISSA GKPTPGTQGK IKLVKESSLS RQSKDSNPYA 

      1810       1820       1830       1840       1850       1860 
TLPRASSVIS TAEGTTRRTS IHDFLTKDSR LPISVDSPPA AADSNTTAAS NVDKVQESRN 

      1870 
SKSRSREQQS S 

« Hide

Isoform 2 [UniParc].

Checksum: 32BCF709F5ADEDC0
Show »

FASTA1,843212,620
Isoform 3 [UniParc].

Checksum: 259F771ECE3DDCFD
Show »

FASTA1,870215,954
Isoform 4 [UniParc].

Checksum: 48C4D509CC7EEE68
Show »

FASTA1,842212,533
Isoform 5 [UniParc].

Checksum: DE7B152EACCC2422
Show »

FASTA1,796207,797

References

« Hide 'large scale' references
[1]"Akt/PKB regulates actin organization and cell motility via Girdin/APE."
Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
Tissue: Fetal brain.
[2]"A novel hook-related protein family and the characterization of hook-related protein 1."
Simpson F., Martin S., Evans T.M., Kerr M., James D.E., Parton R.G., Teasdale R.D., Wicking C.
Traffic 6:442-458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
Tissue: Fetal brain.
[3]Anai M.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 2 AND 5).
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 811-1871 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1850 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 851-1871 (ISOFORM 4).
Tissue: Amygdala and Testis.
[7]"Identification and characterization of GIV, a novel Galpha i/s-interacting protein found on COPI, endoplasmic reticulum-Golgi transport vesicles."
Le-Niculescu H., Niesman I., Fischer T., DeVries L., Farquhar M.G.
J. Biol. Chem. 280:22012-22020(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, SUBCELLULAR LOCATION.
[8]"Girdin, a novel actin-binding protein, and its family of proteins possess versatile functions in the Akt and Wnt signaling pathways."
Enomoto A., Ping J., Takahashi M.
Ann. N. Y. Acad. Sci. 1086:169-184(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"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 SER-1387; THR-1673 AND SER-1837, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB201172 mRNA. Translation: BAE44387.1.
AB125644 mRNA. Translation: BAF44475.1.
AC019198 Genomic DNA. Translation: AAY14932.1. Different initiation.
AC092176 Genomic DNA. Translation: AAX82029.1.
AC012358 Genomic DNA. No translation available.
BC132736 mRNA. Translation: AAI32737.1.
BC144320 mRNA. Translation: AAI44321.1.
BX537985 mRNA. Translation: CAD97945.1. Sequence problems.
BX538154 mRNA. Translation: CAD98038.1.
BX648138 mRNA. Translation: CAI46020.1. Different initiation.
CCDSCCDS33203.1. [Q3V6T2-2]
CCDS46288.1. [Q3V6T2-3]
CCDS58710.1. [Q3V6T2-5]
RefSeqNP_001129069.1. NM_001135597.1. [Q3V6T2-3]
NP_001241872.1. NM_001254943.1. [Q3V6T2-5]
NP_060554.3. NM_018084.4. [Q3V6T2-2]
XP_005264480.1. XM_005264423.1. [Q3V6T2-4]
UniGeneHs.292925.

3D structure databases

ProteinModelPortalQ3V6T2.
SMRQ3V6T2. Positions 14-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120829. 15 interactions.
IntActQ3V6T2. 8 interactions.
STRING9606.ENSP00000338728.

PTM databases

PhosphoSiteQ3V6T2.

Polymorphism databases

DMDM147644956.

Proteomic databases

MaxQBQ3V6T2.
PaxDbQ3V6T2.
PRIDEQ3V6T2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263630; ENSP00000263630; ENSG00000115355. [Q3V6T2-2]
ENST00000336838; ENSP00000338728; ENSG00000115355. [Q3V6T2-3]
ENST00000413716; ENSP00000404431; ENSG00000115355. [Q3V6T2-5]
ENST00000436346; ENSP00000410608; ENSG00000115355. [Q3V6T2-1]
GeneID55704.
KEGGhsa:55704.
UCSCuc002ryu.2. human. [Q3V6T2-4]
uc002ryv.2. human. [Q3V6T2-3]
uc010yoz.1. human. [Q3V6T2-2]
uc010ypa.1. human.

Organism-specific databases

CTD55704.
GeneCardsGC02M055514.
HGNCHGNC:25523. CCDC88A.
HPAHPA038101.
MIM609736. gene.
neXtProtNX_Q3V6T2.
PharmGKBPA162381751.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG057867.
InParanoidQ3V6T2.
OMACIRLKEL.
OrthoDBEOG7N0C3V.
PhylomeDBQ3V6T2.
TreeFamTF320231.

Gene expression databases

ArrayExpressQ3V6T2.
BgeeQ3V6T2.
CleanExHS_CCDC88A.
GenevestigatorQ3V6T2.

Family and domain databases

InterProIPR027717. Girdin.
IPR008636. Hook-related_fam.
[Graphical view]
PANTHERPTHR18947. PTHR18947. 1 hit.
PTHR18947:SF30. PTHR18947:SF30. 1 hit.
PfamPF05622. HOOK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCCDC88A. human.
GeneWikiCCDC88A.
GenomeRNAi55704.
NextBio60553.
PROQ3V6T2.
SOURCESearch...

Entry information

Entry nameGRDN_HUMAN
AccessionPrimary (citable) accession number: Q3V6T2
Secondary accession number(s): A1IGE7 expand/collapse secondary AC list , B7ZM78, C9JG83, Q53SF1, Q581G3, Q5HYD0, Q7Z339, Q7Z3C5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 79 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 2

Human chromosome 2: entries, gene names and cross-references to MIM