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Q3V6T2

- GRDN_HUMAN

UniProt

Q3V6T2 - GRDN_HUMAN

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Protein

Girdin

Gene

CCDC88A

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

Functioni

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.By similarity2 Publications

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. microtubule binding Source: UniProtKB
  3. phosphatidylinositol binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. protein kinase B binding Source: UniProtKB

GO - Biological processi

  1. activation of protein kinase B activity Source: UniProtKB
  2. cell migration Source: UniProtKB
  3. DNA replication Source: UniProtKB-KW
  4. lamellipodium assembly Source: UniProtKB
  5. membrane organization Source: UniProtKB
  6. regulation of actin cytoskeleton organization Source: UniProtKB
  7. regulation of cell proliferation Source: UniProtKB
  8. regulation of DNA replication Source: UniProtKB
  9. regulation of neuron projection development Source: UniProtKB
  10. regulation of protein phosphorylation Source: UniProtKB
  11. TOR signaling Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA replication, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CCDC88A
Synonyms:APEImported, GRDN, KIAA1212Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:25523. CCDC88A.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB
  4. Golgi apparatus Source: UniProtKB
  5. lamellipodium Source: UniProtKB
  6. membrane Source: UniProtKB
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1417 – 14171S → A: Disrupts actin organization, cell migration and lamellipodia formation. 1 Publication

Organism-specific databases

PharmGKBiPA162381751.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18711871GirdinPRO_0000287429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1387 – 13871Phosphoserine1 Publication
Modified residuei1417 – 14171Phosphoserine; by PKB/AKT11 Publication
Modified residuei1673 – 16731Phosphothreonine1 Publication
Modified residuei1675 – 16751PhosphoserineBy similarity
Modified residuei1837 – 18371Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3V6T2.
PaxDbiQ3V6T2.
PRIDEiQ3V6T2.

PTM databases

PhosphoSiteiQ3V6T2.

Expressioni

Tissue specificityi

Expressed ubiquitously.1 Publication

Gene expression databases

BgeeiQ3V6T2.
CleanExiHS_CCDC88A.
ExpressionAtlasiQ3V6T2. baseline and differential.
GenevestigatoriQ3V6T2.

Organism-specific databases

HPAiHPA038101.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi120829. 28 interactions.
IntActiQ3V6T2. 8 interactions.
STRINGi9606.ENSP00000338728.

Structurei

3D structure databases

ProteinModelPortaliQ3V6T2.
SMRiQ3V6T2. Positions 14-163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1390 – 140819Phosphoinositide-binding1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili196 – 425230Sequence AnalysisAdd
BLAST
Coiled coili458 – 1385928Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the CCDC88 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00690000101702.
HOVERGENiHBG057867.
InParanoidiQ3V6T2.
OMAiCIRLKEL.
OrthoDBiEOG7N0C3V.
PhylomeDBiQ3V6T2.
TreeFamiTF320231.

Family and domain databases

InterProiIPR027717. Girdin.
IPR008636. Hook-related_fam.
[Graphical view]
PANTHERiPTHR18947. PTHR18947. 1 hit.
PTHR18947:SF30. PTHR18947:SF30. 1 hit.
PfamiPF05622. HOOK. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q3V6T2-1) [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

        10         20         30         40         50
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ
60 70 80 90 100
VMLQINPKLE SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM
110 120 130 140 150
SLPNVLIIGK NPFSEQGTEE VKKLLLLLLG CAVQCQKKEE FIERIQGLDF
160 170 180 190 200
DTKAAVAAHI QEVTHNQENV FDLQWMEVTD MSQEDIEPLL KNMALHLKRL
210 220 230 240 250
IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM KRTESRQHLS
260 270 280 290 300
VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS
310 320 330 340 350
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK
360 370 380 390 400
EDNQVLLETK TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM
410 420 430 440 450
DRKKIEELME ENMTLEMAQK QSMDESLHLG WELEQISRTS ELSEAPQKSL
460 470 480 490 500
GHEVNELTSS RLLKLEMENQ SLTKTVEELR TTVDSVEGNA SKILKMEKEN
510 520 530 540 550
QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK TIETLRENSE
560 570 580 590 600
RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS
610 620 630 640 650
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN
660 670 680 690 700
LKITCEKIEA LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD
710 720 730 740 750
EENLELRRNV ESLKCASMKM AQLQLENKEL ESEKEQLKKG LELLKASFKK
760 770 780 790 800
TERLEVSYQG LDIENQRLQK TLENSNKKIQ QLESELQDLE MENQTLQKNL
810 820 830 840 850
EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR LRQQAEIKDT
860 870 880 890 900
TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID
910 920 930 940 950
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD
960 970 980 990 1000
DSRYKLLESK LESTLKKSLE IKEEKIAALE ARLEESTNYN QQLRQELKTV
1010 1020 1030 1040 1050
KKNYEALKQR QDEERMVQSS PPISGEDNKW ERESQETTRE LLKVKDRLIE
1060 1070 1080 1090 1100
VERNNATLQA EKQALKTQLK QLETQNNNLQ AQILALQRQT VSLQEQNTTL
1110 1120 1130 1140 1150
QTQNAKLQVE NSTLNSQSTS LMNQNAQLLI QQSSLENENE SVIKEREDLK
1160 1170 1180 1190 1200
SLYDSLIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHRDLED
1210 1220 1230 1240 1250
RYNQLLKQKG QLEDLEKMLK VEQEKMLLEN KNHETVAAEY KKLCGENDRL
1260 1270 1280 1290 1300
NHTYSQLLKE TEVLQTDHKN LKSLLNNSKL EQTRLEAEFS KLKEQYQQLD
1310 1320 1330 1340 1350
ITSTKLNNQC ELLSQLKGNL EEENRHLLDQ IQTLMLQNRT LLEQNMESKD
1360 1370 1380 1390 1400
LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ YKFYDPSPPR RRGNWITLKM
1410 1420 1430 1440 1450
RKLIKSKKDI NRERQKSLTL TPTRSDSSEG FLQLPHQDSQ DSSSVGSNSL
1460 1470 1480 1490 1500
EDGQTLGTKK SSMVALKRLP FLRNRPKDKD KMKACYRRSM SMNDLVQSMV
1510 1520 1530 1540 1550
LAGQWTGSTE NLEVPDDIST GKRRKELGAM AFSTTAINFS TVNSSAGFRS
1560 1570 1580 1590 1600
KQLVNNKDTT SFEDISPQGV SDDSSTGSRV HASRPASLDS GRTSTSNSNN
1610 1620 1630 1640 1650
NASLHEVKAG AVNNQSRPQS HSSGEFSLLH DHEAWSSSGS SPIQYLKRQT
1660 1670 1680 1690 1700
RSSPVLQHKI SETLESRHHK IKTGSPGSEV VTLQQFLEES NKLTSVQIKS
1710 1720 1730 1740 1750
SSQENLLDEV MKSLSVSSDF LGKDKPVSCG LARSVSGKTP GDFYDRRTTK
1760 1770 1780 1790 1800
PEFLRPGPRK TEDTYFISSA GKPTPGTQGK IKLVKESSLS RQSKDSNPYA
1810 1820 1830 1840 1850
TLPRASSVIS TAEGTTRRTS IHDFLTKDSR LPISVDSPPA AADSNTTAAS
1860 1870
NVDKVQESRN SKSRSREQQS S
Length:1,871
Mass (Da):216,042
Last modified:May 15, 2007 - v2
Checksum:i9DD2E06F2A235AA5
GO
Isoform 22 Publications (identifier: Q3V6T2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T

Show »
Length:1,843
Mass (Da):212,620
Checksum:i32BCF709F5ADEDC0
GO
Isoform 3 (identifier: Q3V6T2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.

Show »
Length:1,870
Mass (Da):215,954
Checksum:i259F771ECE3DDCFD
GO
Isoform 4 (identifier: Q3V6T2-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T

Show »
Length:1,842
Mass (Da):212,533
Checksum:i48C4D509CC7EEE68
GO
Isoform 5 (identifier: Q3V6T2-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     952-952: Missing.
     1733-1806: Missing.

Note: No experimental confirmation available.

Show »
Length:1,796
Mass (Da):207,797
Checksum:iDE7B152EACCC2422
GO

Sequence cautioni

The sequence AAY14932.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAD97945.1 differs from that shown. Reason: Intron retention at the C-terminus.Curated
The sequence CAI46020.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1066 – 10661K → E in CAI46020. (PubMed:17974005)Curated
Sequence conflicti1081 – 10811A → T in CAD97945. (PubMed:17974005)Curated
Sequence conflicti1661 – 16611S → P in CAD97945. (PubMed:17974005)Curated
Sequence conflicti1710 – 17101V → I in CAI46020. (PubMed:17974005)Curated
Sequence conflicti1799 – 17991Y → H in CAD98038. (PubMed:17974005)Curated
Sequence conflicti1836 – 18361D → G in CAI46020. (PubMed:17974005)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei952 – 9521Missing in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_040129
Alternative sequencei1463 – 149129MVALK…RRSMS → T in isoform 2 and isoform 4. 4 PublicationsVSP_052409Add
BLAST
Alternative sequencei1733 – 180674Missing in isoform 5. 1 PublicationVSP_044943Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33203.1. [Q3V6T2-2]
CCDS46288.1. [Q3V6T2-3]
CCDS58710.1. [Q3V6T2-5]
RefSeqiNP_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]
UniGeneiHs.292925.

Genome annotation databases

EnsembliENST00000263630; ENSP00000263630; ENSG00000115355. [Q3V6T2-2]
ENST00000336838; ENSP00000338728; ENSG00000115355. [Q3V6T2-3]
ENST00000413716; ENSP00000404431; ENSG00000115355. [Q3V6T2-5]
ENST00000436346; ENSP00000410608; ENSG00000115355. [Q3V6T2-1]
GeneIDi55704.
KEGGihsa:55704.
UCSCiuc002ryu.2. human. [Q3V6T2-4]
uc002ryv.2. human. [Q3V6T2-3]
uc010yoz.1. human. [Q3V6T2-2]
uc010ypa.1. human.

Polymorphism databases

DMDMi147644956.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS33203.1. [Q3V6T2-2 ]
CCDS46288.1. [Q3V6T2-3 ]
CCDS58710.1. [Q3V6T2-5 ]
RefSeqi NP_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 ]
UniGenei Hs.292925.

3D structure databases

ProteinModelPortali Q3V6T2.
SMRi Q3V6T2. Positions 14-163.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120829. 28 interactions.
IntActi Q3V6T2. 8 interactions.
STRINGi 9606.ENSP00000338728.

PTM databases

PhosphoSitei Q3V6T2.

Polymorphism databases

DMDMi 147644956.

Proteomic databases

MaxQBi Q3V6T2.
PaxDbi Q3V6T2.
PRIDEi Q3V6T2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263630 ; ENSP00000263630 ; ENSG00000115355 . [Q3V6T2-2 ]
ENST00000336838 ; ENSP00000338728 ; ENSG00000115355 . [Q3V6T2-3 ]
ENST00000413716 ; ENSP00000404431 ; ENSG00000115355 . [Q3V6T2-5 ]
ENST00000436346 ; ENSP00000410608 ; ENSG00000115355 . [Q3V6T2-1 ]
GeneIDi 55704.
KEGGi hsa:55704.
UCSCi uc002ryu.2. human. [Q3V6T2-4 ]
uc002ryv.2. human. [Q3V6T2-3 ]
uc010yoz.1. human. [Q3V6T2-2 ]
uc010ypa.1. human.

Organism-specific databases

CTDi 55704.
GeneCardsi GC02M055514.
HGNCi HGNC:25523. CCDC88A.
HPAi HPA038101.
MIMi 609736. gene.
neXtProti NX_Q3V6T2.
PharmGKBi PA162381751.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00690000101702.
HOVERGENi HBG057867.
InParanoidi Q3V6T2.
OMAi CIRLKEL.
OrthoDBi EOG7N0C3V.
PhylomeDBi Q3V6T2.
TreeFami TF320231.

Miscellaneous databases

ChiTaRSi CCDC88A. human.
GeneWikii CCDC88A.
GenomeRNAii 55704.
NextBioi 60553.
PROi Q3V6T2.
SOURCEi Search...

Gene expression databases

Bgeei Q3V6T2.
CleanExi HS_CCDC88A.
ExpressionAtlasi Q3V6T2. baseline and differential.
Genevestigatori Q3V6T2.

Family and domain databases

InterProi IPR027717. Girdin.
IPR008636. Hook-related_fam.
[Graphical view ]
PANTHERi PTHR18947. PTHR18947. 1 hit.
PTHR18947:SF30. PTHR18947:SF30. 1 hit.
Pfami PF05622. HOOK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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 brain1 Publication.
  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 brain1 Publication.
  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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiGRDN_HUMAN
AccessioniPrimary (citable) accession number: Q3V6T2
Secondary accession number(s): A1IGE7
, B7ZM78, C9JG83, Q53SF1, Q581G3, Q5HYD0, Q7Z339, Q7Z3C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: October 29, 2014
This is version 81 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3