Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5SNZ0 (GRDN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Grdn, Kiaa1212
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1873 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 similarity. 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. Ref.1 Ref.9

Subunit structure

Homodimer. The non-phosphorylated form interacts with phosphatidylinositol 4-phosphate [Pi4P] and weakly with phosphatidylinositol 3-phosphate [Pi3P] By similarity. Interacts with microtubules. Interacts AKT1/PKB (via C-terminus). Interacts (via C-terminus) with DISC1; the interaction is direct. Interacts with AKT proteins; the interaction is inhibited in presence of DISC1. Ref.1 Ref.7 Ref.9 UniProtKB Q3V6T2

Subcellular location

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

Tissue specificity

Expressed in the dentate gyrus, pyramidal cell layer of hippocampal regions CA1 and CA3 at postnatal 15. Expressed highly in neurons. Weakly in neuron progenitors (at protein level). Expressed in the dentate granule cell layer of the hippocampus. Expressed highly in the adult testis, moderately in the brain and at a low level in the spleen, lungs and fat. Ref.1 Ref.7 Ref.9

Developmental stage

Temporally and spatially restricted during embryogenesis. At E10.5, expressed in the branchial arches, nasal processes, limbs, somites and dorsal root ganglia. At E11.5, expression persists at these sites in addition to the eye and fore-, mid- and hindbrain. By E12.5, expressed in the interdigital mesenchyme of the limbs. At E13.5, expression in the limbs flanks the digits and also appears in a subset of tendons in the hind- and forelimbs. Ref.7

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 By similarity. UniProtKB Q3V6T2

Sequence similarities

Belongs to the CCDC88 family.

Sequence caution

The sequence AAH37020.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI24877.1 differs from that shown. Reason: Erroneous gene model prediction.

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 direct assay Ref.9. Source: UniProtKB

activation of protein kinase B activity

Inferred from direct assay Ref.1. Source: UniProtKB

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

membrane organization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA replication

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell proliferation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of neuron projection development

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionactin binding

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.7. Source: UniProtKB

phosphatidylinositol binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.2 (identifier: Q5SNZ0-1)

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.
Note: No experimental confirmation available.
Isoform 2 Ref.1 (identifier: Q5SNZ0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T
Isoform 3 Ref.2 (identifier: Q5SNZ0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1000-1054: Missing.
     1463-1491: MVALKRLPFLRNRPKDKDKMKACYRRSMS → T
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18731873Girdin
PRO_0000287430

Regions

Region1390 – 140819Phosphoinositide-binding By similarity UniProtKB Q3V6T2
Coiled coil196 – 425230 Potential
Coiled coil458 – 1232775 Potential
Coiled coil1268 – 1385118 Potential

Amino acid modifications

Modified residue13871Phosphoserine By similarity UniProtKB Q3V6T2
Modified residue14171Phosphoserine; by PKB/AKT1 By similarity UniProtKB Q3V6T2
Modified residue16771Phosphoserine Ref.5
Modified residue18391Phosphoserine By similarity

Natural variations

Alternative sequence1000 – 105455Missing in isoform 3. Ref.2
VSP_052410
Alternative sequence1463 – 149129MVALK…RRSMS → T in isoform 2 and isoform 3. Ref.1 Ref.2
VSP_052411

Experimental info

Sequence conflict9521Missing in CAI35999. Ref.2
Sequence conflict1086 – 10894LQRQ → PRVR in AAH37020. Ref.3

Sequences

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

Last modified May 15, 2007. Version 2.
Checksum: 0E827E3D9336161F

FASTA1,873215,918
        10         20         30         40         50         60 
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ VMLQINPKSE 

        70         80         90        100        110        120 
SQRVNKKVNN DASLRIHNLS ILVKQIKFYY QETLQQLIMM PLPDILIIGK NPFSEQGTEE 

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

       190        200        210        220        230        240 
MSQEDIEPLL KNMVSHLRRL IDERDEHSET IVELSEERDG VHFLPHASSS AQSPCGSPGM 

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

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

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

       430        440        450        460        470        480 
QSMDESLHLG WELEQISRTS ELAEAPQKSL GHEVNELTSS KLLKLEMENQ SLTKTVEELR 

       490        500        510        520        530        540 
STADSAAGST SKILKVEKEN QRLNKKVEIL ENEIIQEKQS LQNCQNLSKD LMKEKAQLEK 

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

       610        620        630        640        650        660 
GKLSKIEFEK RQMKKELELY KEKGERAEEL ENELNHLGKE NELLQKKITN LKITCEKLET 

       670        680        690        700        710        720 
LEQENSELER ENRKFKKTLD SFKNLTFQLE SLEKENSQLD EENLELRRSV ESLKCASMRM 

       730        740        750        760        770        780 
AQLQLENKEL ESEKEQLRKG LELMRASFKK TERLEVSYQG LDTENQRLQK ALENSNKKIQ 

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

       850        860        870        880        890        900 
LRQQAEIKDT TLEENNVKIG NLEKENKTLF KEINVYKESC VRLKELEKEN KELVKRATID 

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

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

      1030       1040       1050       1060       1070       1080 
IPVSGEDDKW GRESQEATRE LLKVKDRLIE VERNNATLQA EKQALKTQLK QLETQNNNLQ 

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

      1150       1160       1170       1180       1190       1200 
SIMKEREDLK SLYDALIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHKDLED 

      1210       1220       1230       1240       1250       1260 
RYNQLLKQKG QLEDLEKMIK TEQEKMLLES KNHEVVASEY KKLCGENDRL NYTYSQLLKE 

      1270       1280       1290       1300       1310       1320 
TEILQMDHKN LKSVLNNSKL 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 
LAGGQWTGST ENLEVPDDIS TGKRRKELGA MAFSTTAINF STVNSSAAFR SKQLVNNKDT 

      1570       1580       1590       1600       1610       1620 
TSFEDISPQG ISDDSSTGSR VHASRPASLD SGRTSTSNSN NNASLHEVKA GAVNIQSRPQ 

      1630       1640       1650       1660       1670       1680 
SHSSGDFSLL HDHETWSSSG SSPIQYLKRQ TRSSPMLQHK ISETIESRAH HKMKAGSPGS 

      1690       1700       1710       1720       1730       1740 
EVVTLQQFLE ESNKLTSIQL KSSSQENLLD EVMKSLSVSS DFLGKDKPVS CTLARSVSGK 

      1750       1760       1770       1780       1790       1800 
TPGDFYDRRT TKPEFLRTGP QKTEDAYTIS SAGKPTPSTQ GKIKLVKETS VSRQSKDSNP 

      1810       1820       1830       1840       1850       1860 
YATLPRASSV ISTAEGTTRR TSIHDFLSKD SRLPVSVDSS PPTAGSSSTT ASNVNKVQES 

      1870 
RNSKSRSREQ QSS 

« Hide

Isoform 2 [UniParc].

Checksum: 87AEDC047EA4A72A
Show »

FASTA1,845212,497
Isoform 3 [UniParc].

Checksum: CD0309B2B554AB94
Show »

FASTA1,790205,970

References

« Hide 'large scale' references
[1]"A novel protein kinase B (PKB)/AKT-binding protein enhances PKB kinase activity and regulates DNA synthesis."
Anai M., Shojima N., Katagiri H., Ogihara T., Sakoda H., Onishi Y., Ono H., Fujishiro M., Fukushima Y., Horike N., Viana A., Kikuchi M., Noguchi N., Takahashi S., Takata K., Oka Y., Uchijima Y., Kurihara H., Asano T.
J. Biol. Chem. 280:18525-18535(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH AKT1, TISSUE SPECIFICITY.
Tissue: Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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] OF 1086-1873 (ISOFORMS 2/3).
Strain: C57BL/6.
Tissue: Retina.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1623-1873.
Strain: C57BL/6J.
Tissue: Embryonic stem cell.
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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: SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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]"DISC1 regulates new neuron development in the adult brain via modulation of AKT-mTOR signaling through KIAA1212."
Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N., Kang E., Song H., Ming G.L.
Neuron 63:761-773(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DISC1 AND AKT PROTEINS, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB087827 mRNA. Translation: BAD98263.1.
AL935054 Genomic DNA. Translation: CAI24877.1. Sequence problems.
AL935054, BX284634 Genomic DNA. Translation: CAI24878.1.
BX284634 Genomic DNA. Translation: CAI35999.1.
BX284634 Genomic DNA. Translation: CAI36000.1.
BX284634, AL935054 Genomic DNA. Translation: CAI36001.1.
BX284634 Genomic DNA. Translation: CAI36002.1.
BC037020 mRNA. Translation: AAH37020.1. Different initiation.
AK082771 mRNA. Translation: BAC38612.1.
CCDSCCDS24494.1. [Q5SNZ0-2]
RefSeqNP_789811.2. NM_176841.4. [Q5SNZ0-2]
XP_006514518.1. XM_006514455.1. [Q5SNZ0-1]
UniGeneMm.338284.
Mm.441367.

3D structure databases

ProteinModelPortalQ5SNZ0.
SMRQ5SNZ0. Positions 14-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid224370. 2 interactions.
IntActQ5SNZ0. 1 interaction.

PTM databases

PhosphoSiteQ5SNZ0.

Proteomic databases

MaxQBQ5SNZ0.
PaxDbQ5SNZ0.
PRIDEQ5SNZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040182; ENSMUSP00000048978; ENSMUSG00000032740. [Q5SNZ0-2]
GeneID108686.
KEGGmmu:108686.
UCSCuc007igw.1. mouse. [Q5SNZ0-2]

Organism-specific databases

CTD55704.
MGIMGI:1925177. Ccdc88a.
RougeSearch...

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00690000101702.
HOVERGENHBG057867.
OMACIRLKEL.
OrthoDBEOG7N0C3V.
PhylomeDBQ5SNZ0.
TreeFamTF320231.

Gene expression databases

BgeeQ5SNZ0.
CleanExMM_CCDC88A.
GenevestigatorQ5SNZ0.

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

NextBio361223.
PROQ5SNZ0.
SOURCESearch...

Entry information

Entry nameGRDN_MOUSE
AccessionPrimary (citable) accession number: Q5SNZ0
Secondary accession number(s): Q5M6X2 expand/collapse secondary AC list , Q5M6X4, Q5M6X5, Q5SNZ1, Q8C486, Q8CFU7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot