GRIP2_HUMAN
ID GRIP2_HUMAN Reviewed; 1043 AA.
AC Q9C0E4; A0A087WU38; Q8TEH9; Q9H7H3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Glutamate receptor-interacting protein 2 {ECO:0000305};
DE Short=GRIP-2;
GN Name=GRIP2 {ECO:0000312|HGNC:HGNC:23841};
GN Synonyms=KIAA1719 {ECO:0000303|PubMed:10574462};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-1043 (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP INTERACTION WITH PRLHR.
RX PubMed=11641419; DOI=10.1124/mol.60.5.916;
RA Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.;
RT "The carboxyl terminus of the prolactin-releasing peptide receptor
RT interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-
RT methylisoxazole-4-propionic acid receptor clustering.";
RL Mol. Pharmacol. 60:916-923(2001).
RN [7]
RP STRUCTURE BY NMR OF 238-341 AND 446-544.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 3rd and the 4th PDZ domain of GRIP2.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: May play a role as a localized scaffold for the assembly of a
CC multiprotein signaling complex and as mediator of the trafficking of
CC its binding partners at specific subcellular location in neurons.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EFNB1, EFNB3, GRIA2, GRIA3, CSPG4 and GRIPAP1.
CC Can form homomultimers and heteromultimers with GRIP1 (By similarity).
CC Interacts with the C-terminal tail of PRLHR. {ECO:0000250,
CC ECO:0000269|PubMed:11641419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0E4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0E4-2; Sequence=VSP_009757, VSP_009758;
CC -!- DOMAIN: PDZ 5 mediates the C-terminal binding of GRIA2 and GRIA3. PDZ 6
CC mediates interaction with the PDZ recognition motif of EFNB1. PDZ 7
CC mediates interaction with CSPG4 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GRIP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21810.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84971.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AB051506; BAB21810.2; ALT_INIT; mRNA.
DR EMBL; ABBA01025158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64198.1; -; Genomic_DNA.
DR EMBL; AK074145; BAB84971.1; ALT_SEQ; mRNA.
DR EMBL; AK024507; BAB15797.1; -; mRNA.
DR CCDS; CCDS46766.2; -. [Q9C0E4-1]
DR RefSeq; NP_001073892.3; NM_001080423.3. [Q9C0E4-1]
DR PDB; 1V62; NMR; -; A=238-341.
DR PDB; 1X5R; NMR; -; A=446-544.
DR PDBsum; 1V62; -.
DR PDBsum; 1X5R; -.
DR AlphaFoldDB; Q9C0E4; -.
DR SMR; Q9C0E4; -.
DR BioGRID; 123330; 8.
DR IntAct; Q9C0E4; 8.
DR MINT; Q9C0E4; -.
DR STRING; 9606.ENSP00000480660; -.
DR iPTMnet; Q9C0E4; -.
DR PhosphoSitePlus; Q9C0E4; -.
DR BioMuta; GRIP2; -.
DR jPOST; Q9C0E4; -.
DR MassIVE; Q9C0E4; -.
DR PeptideAtlas; Q9C0E4; -.
DR PRIDE; Q9C0E4; -.
DR ProteomicsDB; 80020; -. [Q9C0E4-1]
DR ProteomicsDB; 80021; -. [Q9C0E4-2]
DR Antibodypedia; 73462; 75 antibodies from 12 providers.
DR DNASU; 80852; -.
DR Ensembl; ENST00000621039.5; ENSP00000478352.1; ENSG00000144596.13. [Q9C0E4-1]
DR GeneID; 80852; -.
DR KEGG; hsa:80852; -.
DR MANE-Select; ENST00000621039.5; ENSP00000478352.1; NM_001080423.4; NP_001073892.3.
DR UCSC; uc062gzy.1; human.
DR CTD; 80852; -.
DR DisGeNET; 80852; -.
DR GeneCards; GRIP2; -.
DR HGNC; HGNC:23841; GRIP2.
DR HPA; ENSG00000144596; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR neXtProt; NX_Q9C0E4; -.
DR OpenTargets; ENSG00000144596; -.
DR VEuPathDB; HostDB:ENSG00000144596; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155615; -.
DR InParanoid; Q9C0E4; -.
DR OMA; MNHAFSC; -.
DR OrthoDB; 65191at2759; -.
DR PhylomeDB; Q9C0E4; -.
DR PathwayCommons; Q9C0E4; -.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
DR SignaLink; Q9C0E4; -.
DR BioGRID-ORCS; 80852; 1 hit in 136 CRISPR screens.
DR ChiTaRS; GRIP2; human.
DR EvolutionaryTrace; Q9C0E4; -.
DR GeneWiki; GRIP2; -.
DR GenomeRNAi; 80852; -.
DR Pharos; Q9C0E4; Tdark.
DR PRO; PR:Q9C0E4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9C0E4; protein.
DR Bgee; ENSG00000144596; Expressed in apex of heart and 154 other tissues.
DR ExpressionAtlas; Q9C0E4; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0035254; F:glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IEA:InterPro.
DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IEA:Ensembl.
DR Gene3D; 2.30.42.10; -; 7.
DR InterPro; IPR043545; GRIP1/2.
DR InterPro; IPR030029; GRIP2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR46227; PTHR46227; 1.
DR PANTHER; PTHR46227:SF4; PTHR46227:SF4; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 7.
DR SUPFAM; SSF50156; SSF50156; 7.
DR PROSITE; PS50106; PDZ; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1043
FT /note="Glutamate receptor-interacting protein 2"
FT /id="PRO_0000083852"
FT DOMAIN 48..131
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 148..234
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 248..332
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 456..545
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 557..641
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 656..738
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 941..1023
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTW1"
FT VAR_SEQ 858..873
FT /note="SPAPGPAREEGFWRMF -> RHPVSPLSTPSHLPLF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_009757"
FT VAR_SEQ 874..1043
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_009758"
FT CONFLICT 850
FT /note="E -> G (in Ref. 1; BAB21810)"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:1V62"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1V62"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1V62"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:1V62"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:1V62"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1V62"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:1V62"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:1V62"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:1X5R"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:1X5R"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:1X5R"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:1X5R"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:1X5R"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:1X5R"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:1X5R"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:1X5R"
FT HELIX 521..532
FT /evidence="ECO:0007829|PDB:1X5R"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:1X5R"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:1X5R"
SQ SEQUENCE 1043 AA; 112573 MW; 24686D50E5FB827F CRC64;
MLCGLSRETP GEADDGPYSK GGKDAGGADV SLACRRQSIP EEFRGITVVE LIKKEGSTLG
LTISGGTDKD GKPRVSNLRP GGLAARSDLL NIGDYIRSVN GIHLTRLRHD EIITLLKNVG
ERVVLEVEYE LPPPAPENNP RIISKTVDVS LYKEGNSFGF VLRGGAHEDG HKSRPLVLTY
VRPGGPADRE GSLKVGDRLL SVDGIPLHGA SHATALATLR QCSHEALFQV EYDVATPDTV
ANASGPLMVE IVKTPGSALG ISLTTTSLRN KSVITIDRIK PASVVDRSGA LHPGDHILSI
DGTSMEHCSL LEATKLLASI SEKVRLEILP VPQSQRPLRP SEAVKVQRSE QLHRWDPCVP
SCHSPRPGHC RMPTWATPAG QDQSRSLSST PFSSPTLNHA FSCNNPSTLP RGSQPMSPRT
TMGRRRQRRR EHKSSLSLAS STVGPGGQIV HTETTEVVLC GDPLSGFGLQ LQGGIFATET
LSSPPLVCFI EPDSPAERCG LLQVGDRVLS INGIATEDGT MEEANQLLRD AALAHKVVLE
VEFDVAESVI PSSGTFHVKL PKKRSVELGI TISSASRKRG EPLIISDIKK GSVAHRTGTL
EPGDKLLAID NIRLDNCPME DAVQILRQCE DLVKLKIRKD EDNSDELETT GAVSYTVELK
RYGGPLGITI SGTEEPFDPI VISGLTKRGL AERTGAIHVG DRILAINNVS LKGRPLSEAI
HLLQVAGETV TLKIKKQLDR PLLPRKSGSL SETSDADEDP ADALKGGLPA ARFSPAVPSV
DSAVESWDSS ATEGGFGGPG SYTPQAAARG TTPQERRPGW LRGSPPPTEP RRTSYTPTPA
DESFPEEEEE DDWEPPTSPA PGPAREEGFW RMFGEALEDL ESCGQSELLR ELEASIMTGT
VQRVALEGRP GHRPWQRGRE VRASPAEMEE LLLPTPLEMH KVTLHKDPMR HDFGFSVSDG
LLEKGVYVHT VRPDGPAHRG GLQPFDRVLQ VNHVRTRDFD CCLAVPLLAE AGDVLELIIS
RKPHTAHSSR APRSPGPSSP RML
