Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01083
Entry Name
UniProt Accession
Theoretical PI
6.29
Molecular Weight
112488.48
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Glutamate receptor-interacting protein 2
Protein Synonyms/Alias
GRIP-2; AMPA receptor-interacting protein GRIP2;
Gene Name
Grip2
Gene Synonyms/Alias
Created Date
29-MAR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
11
Isoform 4
WRRNLALCLQRLPDE
[1][2]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] DeSouza S, Fu J, States BA, Ziff EB. Differential palmitoylation directs theAMPA receptor-binding protein ABP to spines or to intracellular clusters. JNeurosci. 2002 May 1;22(9):3493-503.[PMID:11978826]
[2] Misra C, Restituito S, Ferreira J, Rameau GA, Fu J, Ziff EB. Regulation ofsynaptic structure and function by palmitoylated AMPA receptor binding protein.Mol Cell Neurosci. 2010 Apr;43(4):341-52. doi: 10.1016/j.mcn.2010.01.001. Epub2010 Jan 18.[PMID:20083202]
Functional Description
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.
Sequence Annotation
Domain: 53 136 PDZ 1.
Domain: 153 239 PDZ 2.
Domain: 253 337 PDZ 3.
Domain: 458 547 PDZ 4.
Domain: 559 643 PDZ 5.
Domain: 658 740 PDZ 6.
Domain: 942 1024 PDZ 7.
Protein Length
1043 AA.
Protein Sequence
(Isoform 4)
MRGWRRNLAL CLQRLPDEDD GPYSKGGKDT AGTDGALVCR RQSIPEEFRG ITMVELIKRE  60
GSTLGLTISG GTDKDGKPRV SNLRPGGLAA RSDLLNVGDY IRSVNGIRLT RLRHDEIITL  120
LKNVGERVVL EVEYELPPPA PENNPRIISK TVDVSLYKEG NSFGFVLRGG AHEDLHKSRP  180
LVLTYVRPGG PADREGSLKV GDRLLSIDGI PLHGASHATA IATLQQCSHE ALFQVEYDVA  240
TPDTVANASG PLVVEIAKTP GSALGISLTT GSHRNKPAIT IDRIKPASVV DRSGALHAGD  300
HILAIDGTST EHCSLVEATK LLASVTEKVR LEILPAPQSR RPLKPPEAVR IQRSEQLHHW  360
DPCVPSCHSP RPSHCRAPTW APGGQDQSRS VSSTPFSSPT MNPAFPCANA STLPRGPMSP  420
RTTAGRRRQR RKEHRSSLSL ASSTVGPGGQ IVHTETTEVV LCGDPLSGFG LQLQGGIFAT  480
ETLSSPPLVR FIEPDSPAER CGLLQVGDRV LAINGIATED GTMEEANQLL RDAALARKVV  540
LEIEFDVAES VIPSSGTFHV KLPKRRGVEL GITISSASRK RGEPLIISDI KKGSVAHRTG  600
TLEPGDKLLA IDNIRLDHCP MEYAVQILRQ CEDLVKLKIR KDEDNSDEQE SSGAVSYTVE  660
LKRYGGPLGI TISGTEEPFD PIIISGLTKR GLAERTGAIH VGDRILAINS VSLKGRPLSE  720
AIHLLQVAGE TVTLKIKKQL DRPLLPRQSG SLSEASDVDE DPPEALKGGL LTTHFSPAVP  780
SVDSAVESWG SSATEGGFGG SGSYTPQVAV RSVTPQEWRS SRLKSSPPPL EPRRTSYTPG  840
PTDESFPEEE EGDWEPPMSP APGPAREEGF WRVLGEALED LESCGQSELL RELEASIMTG  900
TVQSVAVDGR PGSRPWRRSR EVGTSPEDLQ ELLLPTPLEM HRVTLHKDPV RNDFGFSVSD  960
GLLEKGVYVH TVRIDGPAQH GGLQPFDRLL QVNHVRTRDF DCCLAVPLLA EAGDILELVV  1020
SRNPLAQSRR TPGAPGPSSP QMI                                          1043
FASTA
(Isoform 4)
>LipidDB-10116-01083|Q9WTW1-4
MRGWRRNLALCLQRLPDEDDGPYSKGGKDTAGTDGALVCRRQSIPEEFRGITMVELIKRE
GSTLGLTISGGTDKDGKPRVSNLRPGGLAARSDLLNVGDYIRSVNGIRLTRLRHDEIITL
LKNVGERVVLEVEYELPPPAPENNPRIISKTVDVSLYKEGNSFGFVLRGGAHEDLHKSRP
LVLTYVRPGGPADREGSLKVGDRLLSIDGIPLHGASHATAIATLQQCSHEALFQVEYDVA
TPDTVANASGPLVVEIAKTPGSALGISLTTGSHRNKPAITIDRIKPASVVDRSGALHAGD
HILAIDGTSTEHCSLVEATKLLASVTEKVRLEILPAPQSRRPLKPPEAVRIQRSEQLHHW
DPCVPSCHSPRPSHCRAPTWAPGGQDQSRSVSSTPFSSPTMNPAFPCANASTLPRGPMSP
RTTAGRRRQRRKEHRSSLSLASSTVGPGGQIVHTETTEVVLCGDPLSGFGLQLQGGIFAT
ETLSSPPLVRFIEPDSPAERCGLLQVGDRVLAINGIATEDGTMEEANQLLRDAALARKVV
LEIEFDVAESVIPSSGTFHVKLPKRRGVELGITISSASRKRGEPLIISDIKKGSVAHRTG
TLEPGDKLLAIDNIRLDHCPMEYAVQILRQCEDLVKLKIRKDEDNSDEQESSGAVSYTVE
LKRYGGPLGITISGTEEPFDPIIISGLTKRGLAERTGAIHVGDRILAINSVSLKGRPLSE
AIHLLQVAGETVTLKIKKQLDRPLLPRQSGSLSEASDVDEDPPEALKGGLLTTHFSPAVP
SVDSAVESWGSSATEGGFGGSGSYTPQVAVRSVTPQEWRSSRLKSSPPPLEPRRTSYTPG
PTDESFPEEEEGDWEPPMSPAPGPAREEGFWRVLGEALEDLESCGQSELLRELEASIMTG
TVQSVAVDGRPGSRPWRRSREVGTSPEDLQELLLPTPLEMHRVTLHKDPVRNDFGFSVSD
GLLEKGVYVHTVRIDGPAQHGGLQPFDRLLQVNHVRTRDFDCCLAVPLLAEAGDILELVV
SRNPLAQSRRTPGAPGPSSPQMI
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0030425; C:dendrite; IDA:UniProtKB
GO:0043198; C:dendritic shaft; IDA:UniProtKB
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:RGD
GO:0014069; C:postsynaptic density; IDA:UniProtKB
GO:0045211; C:postsynaptic membrane; IDA:UniProtKB
GO:0008022; F:protein C-terminus binding; IPI:UniProtKB
GO:0015031; P:protein transport; IMP:RGD
Interpro
InterPro; IPR001478; PDZ
Pfam
Pfam; PF00595; PDZ;
SMART
SMART; SM00228; PDZ;
PROSITE
PROSITE; PS50106; PDZ;
PRINTS