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Q9Y3R0

- GRIP1_HUMAN

UniProt

Q9Y3R0 - GRIP1_HUMAN

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Protein

Glutamate receptor-interacting protein 1

Gene

GRIP1

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

Functioni

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.1 Publication

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. beta-catenin binding Source: AgBase
  3. protein C-terminus binding Source: UniProtKB
  4. receptor signaling complex scaffold activity Source: UniProtKB
  5. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. intracellular signal transduction Source: UniProtKB
  3. positive regulation of transcription, DNA-templated Source: UniProtKB
  4. protein localization Source: Ensembl
  5. synaptic transmission Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_18422. Trafficking of GluR2-containing AMPA receptors.
SignaLinkiQ9Y3R0.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor-interacting protein 1
Short name:
GRIP-1
Gene namesi
Name:GRIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:18708. GRIP1.

Subcellular locationi

Cytoplasmic vesicle 1 Publication. Endoplasmic reticulum 1 Publication. 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).By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. cytosol Source: Reactome
  4. dendrite Source: Ensembl
  5. endoplasmic reticulum Source: UniProtKB-KW
  6. membrane raft Source: Ensembl
  7. neuron projection Source: BHF-UCL
  8. plasma membrane Source: BHF-UCL
  9. postsynaptic membrane Source: UniProtKB-KW
  10. recycling endosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

Fraser syndrome (FRASS) [MIM:219000]: Multisystem malformation usually comprising cryptophthalmos, cutaneous syndactyly, ear abnormalities, renal agenesis and congenital heart defects.1 Publication
Note: The disease may be caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi219000. phenotype.
Orphaneti2052. Fraser syndrome.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11281128Glutamate receptor-interacting protein 1PRO_0000083849Add
BLAST

Proteomic databases

MaxQBiQ9Y3R0.
PaxDbiQ9Y3R0.
PRIDEiQ9Y3R0.

PTM databases

PhosphoSiteiQ9Y3R0.

Expressioni

Gene expression databases

BgeeiQ9Y3R0.
CleanExiHS_GRIP1.
ExpressionAtlasiQ9Y3R0. baseline and differential.
GenevestigatoriQ9Y3R0.

Organism-specific databases

HPAiHPA038856.

Interactioni

Subunit structurei

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). Interacts with WBSCR22.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033722EBI-5349621,EBI-78473
IRF3Q146532EBI-5349621,EBI-2650369
PRLHRP496832EBI-5349621,EBI-8009236
PSMB9P280653EBI-5349621,EBI-603300

Protein-protein interaction databases

BioGridi116995. 42 interactions.
IntActiQ9Y3R0. 12 interactions.
MINTiMINT-1186452.
STRINGi9606.ENSP00000381098.

Structurei

Secondary structure

1
1128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi149 – 1568
Beta strandi163 – 1697
Beta strandi178 – 1858
Helixi190 – 1945
Beta strandi202 – 2065
Helixi216 – 22510
Beta strandi228 – 23710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JILX-ray1.50A/B149-239[»]
ProteinModelPortaliQ9Y3R0.
SMRiQ9Y3R0. Positions 48-343, 464-793, 996-1086.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3R0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 13684PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini150 – 23889PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini252 – 33685PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini472 – 56190PDZ 4PROSITE-ProRule annotationAdd
BLAST
Domaini573 – 65886PDZ 5PROSITE-ProRule annotationAdd
BLAST
Domaini673 – 75583PDZ 6PROSITE-ProRule annotationAdd
BLAST
Domaini1004 – 108683PDZ 7PROSITE-ProRule annotationAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Contains 7 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297474.
GeneTreeiENSGT00390000013494.
HOGENOMiHOG000043120.
HOVERGENiHBG051841.
InParanoidiQ9Y3R0.
OMAiKKQTDAQ.
OrthoDBiEOG7XM31C.
PhylomeDBiQ9Y3R0.
TreeFamiTF326909.

Family and domain databases

Gene3Di2.30.42.10. 7 hits.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 7 hits.
[Graphical view]
SMARTiSM00228. PDZ. 7 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 7 hits.
PROSITEiPS50106. PDZ. 7 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y3R0-1) [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
MIAVSFKCRC QILRRLTKDE SPYTKSASQT KPPDGALAVR RQSIPEEFKG
60 70 80 90 100
STVVELMKKE GTTLGLTVSG GIDKDGKPRV SNLRQGGIAA RSDQLDVGDY
110 120 130 140 150
IKAVNGINLA KFRHDEIISL LKNVGERVVL EVEYELPPVS VQGSSVIFRT
160 170 180 190 200
VEVTLHKEGN TFGFVIRGGA HDDRNKSRPV VITCVRPGGP ADREGTIKPG
210 220 230 240 250
DRLLSVDGIR LLGTTHAEAM SILKQCGQEA ALLIEYDVSV MDSVATASGP
260 270 280 290 300
LLVEVAKTPG ASLGVALTTS MCCNKQVIVI DKIKSASIAD RCGALHVGDH
310 320 330 340 350
ILSIDGTSME YCTLAEATQF LANTTDQVKL EILPHHQTRL ALKGPDHVKI
360 370 380 390 400
QRSDRQLTWD SWASNHSSLH TNHHYNTYHP DHCRVPALTF PKAPPPNSPP
410 420 430 440 450
ALVSSSFSPT SMSAYSLSSL NMGTLPRSLY STSPRGTMMR RRLKKKDFKS
460 470 480 490 500
SLSLASSTVG LAGQVVHTET TEVVLTADPV TGFGIQLQGS VFATETLSSP
510 520 530 540 550
PLISYIEADS PAERCGVLQI GDRVMAINGI PTEDSTFEEA SQLLRDSSIT
560 570 580 590 600
SKVTLEIEFD VAESVIPSSG TFHVKLPKKH NVELGITISS PSSRKPGDPL
610 620 630 640 650
VISDIKKGSV AHRTGTLELG DKLLAIDNIR LDNCSMEDAV QILQQCEDLV
660 670 680 690 700
KLKIRKDEDN SDEQESSGAI IYTVELKRYG GPLGITISGT EEPFDPIIIS
710 720 730 740 750
SLTKGGLAER TGAIHIGDRI LAINSSSLKG KPLSEAIHLL QMAGETVTLK
760 770 780 790 800
IKKQTDAQSA SSPKKFPISS HLSDLGDVEE DSSPAQKPGK LSDMYPSTVP
810 820 830 840 850
SVDSAVDSWD GSAIDTSYGT QGTSFQASGY NFNTYDWRSP KQRGSLSPVT
860 870 880 890 900
KPRSQTYPDV GLSYEDWDRS TASGFAGAAD SAETEQEENF WSQALEDLET
910 920 930 940 950
CGQSGILREL EEKADRRVSL RNMTLLATIM SGSTMSLNHE APTPRSQLGR
960 970 980 990 1000
QASFQERSSS RPHYSQTTRS NTLPSDVGRK SVTLRKMKQE IKEIMSPTPV
1010 1020 1030 1040 1050
ELHKVTLYKD SDMEDFGFSV ADGLLEKGVY VKNIRPAGPG DLGGLKPYDR
1060 1070 1080 1090 1100
LLQVNHVRTR DFDCCLVVPL IAESGNKLDL VISRNPLASQ KSIDQQSLPG
1110 1120
DWSEQNSAFF QQPSHGGNLE TREPTNTL
Length:1,128
Mass (Da):122,422
Last modified:November 30, 2010 - v3
Checksum:iD97B96ADF2C3796B
GO
Isoform 2 (identifier: Q9Y3R0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     912-926: Missing.

Note: No experimental confirmation available.

Show »
Length:1,113
Mass (Da):120,638
Checksum:i238CCE7D74B02257
GO
Isoform 3 (identifier: Q9Y3R0-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,076
Mass (Da):116,371
Checksum:iE5A5A1C1EAD662C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti821 – 8211Q → E in AAI15394. (PubMed:15489334)Curated
Sequence conflicti821 – 8211Q → E in CAB39895. (PubMed:10197531)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti322 – 3221A → T.
Corresponds to variant rs17102531 [ dbSNP | Ensembl ].
VAR_056904

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei348 – 40053VKIQR…PNSPP → A in isoform 3. 1 PublicationVSP_040281Add
BLAST
Alternative sequencei912 – 92615Missing in isoform 2. 1 PublicationVSP_009743Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41807.1. [Q9Y3R0-3]
RefSeqiNP_001171545.1. NM_001178074.1.
NP_066973.2. NM_021150.3. [Q9Y3R0-3]
UniGeneiHs.505946.

Genome annotation databases

EnsembliENST00000359742; ENSP00000352780; ENSG00000155974. [Q9Y3R0-1]
ENST00000398016; ENSP00000381098; ENSG00000155974. [Q9Y3R0-3]
GeneIDi23426.
KEGGihsa:23426.
UCSCiuc001stk.3. human. [Q9Y3R0-3]
uc001stl.1. human. [Q9Y3R0-2]

Polymorphism databases

DMDMi313104231.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS41807.1. [Q9Y3R0-3 ]
RefSeqi NP_001171545.1. NM_001178074.1.
NP_066973.2. NM_021150.3. [Q9Y3R0-3 ]
UniGenei Hs.505946.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JIL X-ray 1.50 A/B 149-239 [» ]
ProteinModelPortali Q9Y3R0.
SMRi Q9Y3R0. Positions 48-343, 464-793, 996-1086.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116995. 42 interactions.
IntActi Q9Y3R0. 12 interactions.
MINTi MINT-1186452.
STRINGi 9606.ENSP00000381098.

PTM databases

PhosphoSitei Q9Y3R0.

Polymorphism databases

DMDMi 313104231.

Proteomic databases

MaxQBi Q9Y3R0.
PaxDbi Q9Y3R0.
PRIDEi Q9Y3R0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359742 ; ENSP00000352780 ; ENSG00000155974 . [Q9Y3R0-1 ]
ENST00000398016 ; ENSP00000381098 ; ENSG00000155974 . [Q9Y3R0-3 ]
GeneIDi 23426.
KEGGi hsa:23426.
UCSCi uc001stk.3. human. [Q9Y3R0-3 ]
uc001stl.1. human. [Q9Y3R0-2 ]

Organism-specific databases

CTDi 23426.
GeneCardsi GC12M066741.
HGNCi HGNC:18708. GRIP1.
HPAi HPA038856.
MIMi 219000. phenotype.
604597. gene.
neXtProti NX_Q9Y3R0.
Orphaneti 2052. Fraser syndrome.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297474.
GeneTreei ENSGT00390000013494.
HOGENOMi HOG000043120.
HOVERGENi HBG051841.
InParanoidi Q9Y3R0.
OMAi KKQTDAQ.
OrthoDBi EOG7XM31C.
PhylomeDBi Q9Y3R0.
TreeFami TF326909.

Enzyme and pathway databases

Reactomei REACT_18422. Trafficking of GluR2-containing AMPA receptors.
SignaLinki Q9Y3R0.

Miscellaneous databases

EvolutionaryTracei Q9Y3R0.
GeneWikii GRIP1_(gene).
GenomeRNAii 23426.
NextBioi 45651.
PROi Q9Y3R0.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y3R0.
CleanExi HS_GRIP1.
ExpressionAtlasi Q9Y3R0. baseline and differential.
Genevestigatori Q9Y3R0.

Family and domain databases

Gene3Di 2.30.42.10. 7 hits.
InterProi IPR001478. PDZ.
[Graphical view ]
Pfami PF00595. PDZ. 7 hits.
[Graphical view ]
SMARTi SM00228. PDZ. 7 hits.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 7 hits.
PROSITEi PS50106. PDZ. 7 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: INVOLVEMENT IN FRASS.
  6. "The methyltransferase WBSCR22/Merm1 enhances glucocorticoid receptor function and is regulated in lung inflammation and cancer."
    Jangani M., Poolman T.M., Matthews L., Yang N., Farrow S.N., Berry A., Hanley N., Williamson A.J., Whetton A.D., Donn R., Ray D.W.
    J. Biol. Chem. 289:8931-8946(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WBSCR22.

Entry informationi

Entry nameiGRIP1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3R0
Secondary accession number(s): C9JT59, Q1RLM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 119 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3