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Q9Y3R0

- GRIP1_HUMAN

UniProt

Q9Y3R0 - GRIP1_HUMAN

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
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    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 binding Source: IntAct
    4. protein C-terminus binding Source: UniProtKB
    5. receptor signaling complex scaffold activity Source: UniProtKB
    6. 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

    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 membrane-bounded vesicle Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. dendrite Source: Ensembl
    5. endoplasmic reticulum Source: UniProtKB-SubCell
    6. membrane raft Source: Ensembl
    7. neuron projection Source: BHF-UCL
    8. plasma membrane Source: BHF-UCL
    9. postsynaptic membrane Source: UniProtKB-SubCell
    10. recycling endosome Source: Ensembl

    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

    ArrayExpressiQ9Y3R0.
    BgeeiQ9Y3R0.
    CleanExiHS_GRIP1.
    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. 41 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.
    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

    MIAVSFKCRC QILRRLTKDE SPYTKSASQT KPPDGALAVR RQSIPEEFKG     50
    STVVELMKKE GTTLGLTVSG GIDKDGKPRV SNLRQGGIAA RSDQLDVGDY 100
    IKAVNGINLA KFRHDEIISL LKNVGERVVL EVEYELPPVS VQGSSVIFRT 150
    VEVTLHKEGN TFGFVIRGGA HDDRNKSRPV VITCVRPGGP ADREGTIKPG 200
    DRLLSVDGIR LLGTTHAEAM SILKQCGQEA ALLIEYDVSV MDSVATASGP 250
    LLVEVAKTPG ASLGVALTTS MCCNKQVIVI DKIKSASIAD RCGALHVGDH 300
    ILSIDGTSME YCTLAEATQF LANTTDQVKL EILPHHQTRL ALKGPDHVKI 350
    QRSDRQLTWD SWASNHSSLH TNHHYNTYHP DHCRVPALTF PKAPPPNSPP 400
    ALVSSSFSPT SMSAYSLSSL NMGTLPRSLY STSPRGTMMR RRLKKKDFKS 450
    SLSLASSTVG LAGQVVHTET TEVVLTADPV TGFGIQLQGS VFATETLSSP 500
    PLISYIEADS PAERCGVLQI GDRVMAINGI PTEDSTFEEA SQLLRDSSIT 550
    SKVTLEIEFD VAESVIPSSG TFHVKLPKKH NVELGITISS PSSRKPGDPL 600
    VISDIKKGSV AHRTGTLELG DKLLAIDNIR LDNCSMEDAV QILQQCEDLV 650
    KLKIRKDEDN SDEQESSGAI IYTVELKRYG GPLGITISGT EEPFDPIIIS 700
    SLTKGGLAER TGAIHIGDRI LAINSSSLKG KPLSEAIHLL QMAGETVTLK 750
    IKKQTDAQSA SSPKKFPISS HLSDLGDVEE DSSPAQKPGK LSDMYPSTVP 800
    SVDSAVDSWD GSAIDTSYGT QGTSFQASGY NFNTYDWRSP KQRGSLSPVT 850
    KPRSQTYPDV GLSYEDWDRS TASGFAGAAD SAETEQEENF WSQALEDLET 900
    CGQSGILREL EEKADRRVSL RNMTLLATIM SGSTMSLNHE APTPRSQLGR 950
    QASFQERSSS RPHYSQTTRS NTLPSDVGRK SVTLRKMKQE IKEIMSPTPV 1000
    ELHKVTLYKD SDMEDFGFSV ADGLLEKGVY VKNIRPAGPG DLGGLKPYDR 1050
    LLQVNHVRTR DFDCCLVVPL IAESGNKLDL VISRNPLASQ KSIDQQSLPG 1100
    DWSEQNSAFF QQPSHGGNLE TREPTNTL 1128
    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. 41 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.
    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

    ArrayExpressi Q9Y3R0.
    Bgeei Q9Y3R0.
    CleanExi HS_GRIP1.
    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

    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 1, 2014
    This is version 118 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