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Q9Y3R0 (GRIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Glutamate receptor-interacting protein 1

Short name=GRIP-1
Gene names
Name:GRIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1128 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons. Ref.3

Subunit structure

Interacts with EPHA7, EPHB2, KIF5A, KIF5B, KIF5C, GRIA2, GRIA3, GRIPAP1/GRASP1, PPFIA1, PPFIA4, FRAS1, PLCD4, PTPRF and liprins-alpha. Can form homomultimers or heteromultimers with GRIP2. Forms a ternary complex with GRIA2 and CSPG4 By similarity. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIA2 and leads to AMPAR complex disassembly By similarity. Interacts with EFNB1, EFNB3 and the C-terminal tail of PRLHR. Interacts with SLC30A9 By similarity. Ref.3 Ref.4

Subcellular location

Cytoplasmic vesicle. Endoplasmic reticulum. Cell junctionsynapsepostsynaptic cell membrane By similarity. Note: Cytoplasmic and membrane-associated with vesicles, peri-Golgi complexes and endoplasmic reticulum. Enriched in postsynaptic plasma membrane and postsynaptic densities By similarity. Ref.3

Domain

PDZ 6 mediates interaction with the PDZ recognition motif of EFNB1 and EPHB2 and with the C-terminus of PPFIA1 and PPFIA4. PDZ 4 and PDZ 5 mediate interaction with the C-terminus of GRIA2 and GRIA3. PDZ 4, PDZ 5 and PDZ 6 mediate homomultimers. PDZ 7 mediates interaction with PDZ domain of GRASP1. PDZ 7 domain binds CSPG4. PDZ 6 mediates interaction with the C-terminus of liprins-alpha. PDZ 1, PDZ 2 and PDZ 3 mediate interaction with the PDZ-binding motif of FRAS1 By similarity. PDZ 4 and PDZ 5 mediate interaction with PRLHR.

Involvement in disease

Fraser syndrome (FRASS) [MIM:219000]: Multisystem malformation usually comprising cryptophthalmos, cutaneous syndactyly, ear abnormalities, renal agenesis and congenital heart defects.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

Contains 7 PDZ (DHR) domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasmic vesicle
Endoplasmic reticulum
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

intracellular signal transduction

Non-traceable author statement Ref.3. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

protein localization

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuron projection

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

plasma membrane

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

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionandrogen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

beta-catenin binding

Traceable author statement PubMed 16344550. Source: AgBase

protein C-terminus binding

Inferred from physical interaction PubMed 16344550. Source: UniProtKB

receptor signaling complex scaffold activity

Non-traceable author statement Ref.3. Source: UniProtKB

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y3R0-1)

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: Q9Y3R0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     912-926: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9Y3R0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     348-400: VKIQRSDRQLTWDSWASNHSSLHTNHHYNTYHPDHCRVPALTFPKAPPPNSPP → A

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11281128Glutamate receptor-interacting protein 1
PRO_0000083849

Regions

Domain53 – 13684PDZ 1
Domain150 – 23889PDZ 2
Domain252 – 33685PDZ 3
Domain472 – 56190PDZ 4
Domain573 – 65886PDZ 5
Domain673 – 75583PDZ 6
Domain1004 – 108683PDZ 7

Natural variations

Alternative sequence348 – 40053VKIQR…PNSPP → A in isoform 3.
VSP_040281
Alternative sequence912 – 92615Missing in isoform 2.
VSP_009743
Natural variant3221A → T.
Corresponds to variant rs17102531 [ dbSNP | Ensembl ].
VAR_056904

Experimental info

Sequence conflict8211Q → E in AAI15394. Ref.2
Sequence conflict8211Q → E in CAB39895. Ref.3

Secondary structure

............... 1128
Helix Strand Turn

Details...

Sequences

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

Last modified November 30, 2010. Version 3.
Checksum: D97B96ADF2C3796B

FASTA1,128122,422
        10         20         30         40         50         60 
MIAVSFKCRC QILRRLTKDE SPYTKSASQT KPPDGALAVR RQSIPEEFKG STVVELMKKE 

        70         80         90        100        110        120 
GTTLGLTVSG GIDKDGKPRV SNLRQGGIAA RSDQLDVGDY IKAVNGINLA KFRHDEIISL 

       130        140        150        160        170        180 
LKNVGERVVL EVEYELPPVS VQGSSVIFRT VEVTLHKEGN TFGFVIRGGA HDDRNKSRPV 

       190        200        210        220        230        240 
VITCVRPGGP ADREGTIKPG DRLLSVDGIR LLGTTHAEAM SILKQCGQEA ALLIEYDVSV 

       250        260        270        280        290        300 
MDSVATASGP LLVEVAKTPG ASLGVALTTS MCCNKQVIVI DKIKSASIAD RCGALHVGDH 

       310        320        330        340        350        360 
ILSIDGTSME YCTLAEATQF LANTTDQVKL EILPHHQTRL ALKGPDHVKI QRSDRQLTWD 

       370        380        390        400        410        420 
SWASNHSSLH TNHHYNTYHP DHCRVPALTF PKAPPPNSPP ALVSSSFSPT SMSAYSLSSL 

       430        440        450        460        470        480 
NMGTLPRSLY STSPRGTMMR RRLKKKDFKS SLSLASSTVG LAGQVVHTET TEVVLTADPV 

       490        500        510        520        530        540 
TGFGIQLQGS VFATETLSSP PLISYIEADS PAERCGVLQI GDRVMAINGI PTEDSTFEEA 

       550        560        570        580        590        600 
SQLLRDSSIT SKVTLEIEFD VAESVIPSSG TFHVKLPKKH NVELGITISS PSSRKPGDPL 

       610        620        630        640        650        660 
VISDIKKGSV AHRTGTLELG DKLLAIDNIR LDNCSMEDAV QILQQCEDLV KLKIRKDEDN 

       670        680        690        700        710        720 
SDEQESSGAI IYTVELKRYG GPLGITISGT EEPFDPIIIS SLTKGGLAER TGAIHIGDRI 

       730        740        750        760        770        780 
LAINSSSLKG KPLSEAIHLL QMAGETVTLK IKKQTDAQSA SSPKKFPISS HLSDLGDVEE 

       790        800        810        820        830        840 
DSSPAQKPGK LSDMYPSTVP SVDSAVDSWD GSAIDTSYGT QGTSFQASGY NFNTYDWRSP 

       850        860        870        880        890        900 
KQRGSLSPVT KPRSQTYPDV GLSYEDWDRS TASGFAGAAD SAETEQEENF WSQALEDLET 

       910        920        930        940        950        960 
CGQSGILREL EEKADRRVSL RNMTLLATIM SGSTMSLNHE APTPRSQLGR QASFQERSSS 

       970        980        990       1000       1010       1020 
RPHYSQTTRS NTLPSDVGRK SVTLRKMKQE IKEIMSPTPV ELHKVTLYKD SDMEDFGFSV 

      1030       1040       1050       1060       1070       1080 
ADGLLEKGVY VKNIRPAGPG DLGGLKPYDR LLQVNHVRTR DFDCCLVVPL IAESGNKLDL 

      1090       1100       1110       1120 
VISRNPLASQ KSIDQQSLPG DWSEQNSAFF QQPSHGGNLE TREPTNTL 

« Hide

Isoform 2 [UniParc].

Checksum: 238CCE7D74B02257
Show »

FASTA1,113120,638
Isoform 3 [UniParc].

Checksum: E5A5A1C1EAD662C6
Show »

FASTA1,076116,371

References

« Hide 'large scale' references
[1]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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 3).
[3]"EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains."
Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H., Klein R.
Neuron 22:511-524(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 265-1128 (ISOFORM 2), FUNCTION, INTERACTION WITH EFNB1 AND EFNB3, SUBCELLULAR LOCATION.
Tissue: Fetal brain.
[4]"The carboxyl terminus of the prolactin-releasing peptide receptor interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor clustering."
Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.
Mol. Pharmacol. 60:916-923(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRLHR.
[5]"Mutations in GRIP1 cause Fraser syndrome."
Vogel M.J., van Zon P., Brueton L., Gijzen M., van Tuil M.C., Cox P., Schanze D., Kariminejad A., Ghaderi-Sohi S., Blair E., Zenker M., Scambler P.J., Ploos van Amstel H.K., van Haelst M.M.
J. Med. Genet. 49:303-306(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FRASS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC078889 Genomic DNA. No translation available.
AC090710 Genomic DNA. No translation available.
AC122686 Genomic DNA. No translation available.
AC135251 Genomic DNA. No translation available.
BC115393 mRNA. Translation: AAI15394.1.
BC115394 mRNA. Translation: AAI15395.1.
AJ133439 mRNA. Translation: CAB39895.1.
RefSeqNP_001171545.1. NM_001178074.1.
NP_066973.2. NM_021150.3.
UniGeneHs.505946.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JILX-ray1.50A/B149-239[»]
ProteinModelPortalQ9Y3R0.
SMRQ9Y3R0. Positions 48-343, 464-793, 996-1086.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116995. 40 interactions.
IntActQ9Y3R0. 12 interactions.
MINTMINT-1186452.
STRING9606.ENSP00000381098.

PTM databases

PhosphoSiteQ9Y3R0.

Polymorphism databases

DMDM313104231.

Proteomic databases

PaxDbQ9Y3R0.
PRIDEQ9Y3R0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286445; ENSP00000286445; ENSG00000155974. [Q9Y3R0-2]
ENST00000359742; ENSP00000352780; ENSG00000155974. [Q9Y3R0-1]
ENST00000398016; ENSP00000381098; ENSG00000155974. [Q9Y3R0-3]
GeneID23426.
KEGGhsa:23426.
UCSCuc001stk.3. human. [Q9Y3R0-3]
uc001stl.1. human. [Q9Y3R0-2]

Organism-specific databases

CTD23426.
GeneCardsGC12M066741.
HGNCHGNC:18708. GRIP1.
HPAHPA038856.
MIM219000. phenotype.
604597. gene.
neXtProtNX_Q9Y3R0.
Orphanet2052. Fraser syndrome.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297474.
HOGENOMHOG000043120.
HOVERGENHBG051841.
InParanoidQ9Y3R0.
OMAKKQTDAQ.
OrthoDBEOG7XM31C.
PhylomeDBQ9Y3R0.
TreeFamTF326909.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkQ9Y3R0.

Gene expression databases

ArrayExpressQ9Y3R0.
BgeeQ9Y3R0.
CleanExHS_GRIP1.
GenevestigatorQ9Y3R0.

Family and domain databases

Gene3D2.30.42.10. 7 hits.
InterProIPR001478. PDZ.
[Graphical view]
PfamPF00595. PDZ. 7 hits.
[Graphical view]
SMARTSM00228. PDZ. 7 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 7 hits.
PROSITEPS50106. PDZ. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y3R0.
GeneWikiGRIP1_(gene).
GenomeRNAi23426.
NextBio45651.
PROQ9Y3R0.
SOURCESearch...

Entry information

Entry nameGRIP1_HUMAN
AccessionPrimary (citable) accession number: Q9Y3R0
Secondary accession number(s): C9JT59, Q1RLM0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 113 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM