Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

GRIP1-associated protein 1 (GRASP-1) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)]

 GRAP1_HUMAN             Reviewed;         841 AA.
Q4V328; A6NL78; Q3MJ75; Q4V327; Q4V330; Q5HYG1; Q6N046; Q96DH8;
Q9NQ43; Q9ULQ3;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
23-MAY-2018, entry version 114.
RecName: Full=GRIP1-associated protein 1;
Short=GRASP-1;
Contains:
RecName: Full=GRASP-1 C-terminal chain {ECO:0000250|UniProtKB:Q9JHZ4};
AltName: Full=30kDa C-terminus form;
Name=GRIPAP1; Synonyms=KIAA1167;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Prostate, and Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 4).
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-841 (ISOFORM 1).
TISSUE=Brain;
PubMed=10574461; DOI=10.1093/dnares/6.5.329;
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
"Characterization of cDNA clones selected by the GeneMark analysis
from size-fractionated cDNA libraries from human brain.";
DNA Res. 6:329-336(1999).
[5]
PROTEIN SEQUENCE OF 401-412, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 677-841.
TISSUE=Fetal brain;
PubMed=10908365; DOI=10.1093/nar/28.15.e72;
Holt L.J., Bussow K., Walter G., Tomlinson I.M.;
"By-passing selection: direct screening for antibody-antigen
interactions using protein arrays.";
Nucleic Acids Res. 28:72-72(2000).
[7]
SUBCELLULAR LOCATION, AND ROLE IN RAYNAUD SYNDROME.
PubMed=15897011; DOI=10.1016/j.clim.2005.03.021;
Stinton L.M., Selak S., Fritzler M.J.;
"Identification of GRASP-1 as a novel 97 kDa autoantigen localized to
endosomes.";
Clin. Immunol. 116:108-117(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
FUNCTION, AND INTERACTION WITH MAPK8 AND MAP3K1.
PubMed=17761173; DOI=10.1016/j.febslet.2007.08.008;
Ye B., Yu W.P., Thomas G.M., Huganir R.L.;
"GRASP-1 is a neuronal scaffold protein for the JNK signaling
pathway.";
FEBS Lett. 581:4403-4410(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-690 AND
SER-692, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
INTERACTION WITH RAB4A.
PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R.,
Oorschot V., Govers R., Monti M., Heck A.J., Sheng M., Klumperman J.,
Rehmann H., Jaarsma D., Kapitein L.C., van der Sluijs P.;
"Neuron specific Rab4 effector GRASP-1 coordinates membrane
specialization and maturation of recycling endosomes.";
PLoS Biol. 8:E1000283-E1000283(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Regulates the endosomal recycling back to the neuronal
plasma membrane, possibly by connecting early and late recycling
endosomal domains and promoting segregation of recycling endosomes
from early endosomal membranes. Involved in the localization of
recycling endosomes to dendritic spines, thereby playing a role in
the maintenance of dendritic spine morphology. Required for the
activity-induced AMPA receptor recycling to dendrite membranes and
for long-term potentiation and synaptic plasticity (By
similarity). {ECO:0000250|UniProtKB:Q9JHZ4}.
-!- FUNCTION: GRASP-1 C-terminal chain: Functions as a scaffold
protein to facilitate MAP3K1/MEKK1-mediated activation of the JNK1
kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and
JNK1 in close proximity. {ECO:0000269|PubMed:17761173}.
-!- SUBUNIT: Interacts with GRIP1, GRIP2 and AMPA receptors (By
similarity). Interacts (via C-terminus) with MAPK8/JNK1 and
MAP3K1/MEKK1; the interaction promotes MAP3K1-mediated
phosphorylation of MAPK8 (PubMed:17761173). Interacts (via N-
terminus) with RAB4A (in GTP-bound form) (PubMed:20098723).
Interacts (via C-terminus) with STX12 (By similarity).
{ECO:0000250|UniProtKB:Q9JHZ4, ECO:0000269|PubMed:17761173,
ECO:0000269|PubMed:20098723}.
-!- INTERACTION:
Q8IW40:CCDC103; NbExp=4; IntAct=EBI-717919, EBI-10261970;
P51946:CCNH; NbExp=4; IntAct=EBI-717919, EBI-741406;
Q8IYX8:CEP57L1; NbExp=6; IntAct=EBI-717919, EBI-1104570;
O95995:GAS8; NbExp=4; IntAct=EBI-717919, EBI-1052570;
Q8WYH8:ING5; NbExp=4; IntAct=EBI-717919, EBI-488533;
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-717919, EBI-739832;
Q4G0R1:PIBF1; NbExp=4; IntAct=EBI-717919, EBI-14066006;
P20338:RAB4A; NbExp=3; IntAct=EBI-717919, EBI-722284;
O75604:USP2; NbExp=4; IntAct=EBI-717919, EBI-743272;
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:15897011}; Peripheral membrane protein
{ECO:0000305}. Recycling endosome membrane
{ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, axon
{ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q9JHZ4}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q9JHZ4}. Note=Localizes to recycling
endosomal tubules that are emanating from early endosomes.
{ECO:0000250|UniProtKB:Q9JHZ4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q4V328-1; Sequence=Displayed;
Name=2;
IsoId=Q4V328-2; Sequence=VSP_015700, VSP_015703, VSP_015704,
VSP_015705;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q4V328-3; Sequence=VSP_015699, VSP_015701, VSP_015704,
VSP_015705;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q4V328-4; Sequence=VSP_015702;
Note=No experimental confirmation available.;
-!- PTM: Proteolytically cleaved by caspase-3. A minor C-terminal
proteolytic fragment of 30 kDa is produced. Proteolytic cleavage
is required for JNK signaling activation.
{ECO:0000250|UniProtKB:Q9JHZ4}.
-!- MISCELLANEOUS: Antibodies against GRIPAP1 have been found in sera
of a patient who developed Raynaud's syndrome and telangiectasias.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BX640704; CAE45824.1; -; mRNA.
EMBL; BX647804; CAI45985.1; ALT_TERM; mRNA.
EMBL; AF207550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX530088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001522; AAH01522.2; -; mRNA.
EMBL; BC101544; AAI01545.1; -; mRNA.
EMBL; BC101546; AAI01547.1; -; mRNA.
EMBL; AB032993; BAA86481.1; -; mRNA.
EMBL; AJ297364; CAB95949.1; -; mRNA.
CCDS; CCDS35248.1; -. [Q4V328-1]
RefSeq; NP_064522.3; NM_020137.4. [Q4V328-1]
UniGene; Hs.109929; -.
ProteinModelPortal; Q4V328; -.
SMR; Q4V328; -.
BioGrid; 121210; 51.
CORUM; Q4V328; -.
DIP; DIP-47299N; -.
IntAct; Q4V328; 59.
STRING; 9606.ENSP00000365624; -.
iPTMnet; Q4V328; -.
PhosphoSitePlus; Q4V328; -.
DMDM; 74753569; -.
EPD; Q4V328; -.
MaxQB; Q4V328; -.
PaxDb; Q4V328; -.
PeptideAtlas; Q4V328; -.
PRIDE; Q4V328; -.
DNASU; 56850; -.
Ensembl; ENST00000376423; ENSP00000365606; ENSG00000068400.
GeneID; 56850; -.
KEGG; hsa:56850; -.
UCSC; uc033ecr.2; human. [Q4V328-1]
CTD; 56850; -.
EuPathDB; HostDB:ENSG00000068400.13; -.
GeneCards; GRIPAP1; -.
HGNC; HGNC:18706; GRIPAP1.
HPA; HPA000282; -.
HPA; HPA000615; -.
MIM; 300408; gene.
neXtProt; NX_Q4V328; -.
PharmGKB; PA38650; -.
eggNOG; ENOG410IKP9; Eukaryota.
eggNOG; ENOG410YB89; LUCA.
HOVERGEN; HBG080243; -.
InParanoid; Q4V328; -.
OrthoDB; EOG091G0AQ8; -.
PhylomeDB; Q4V328; -.
TreeFam; TF329006; -.
ChiTaRS; GRIPAP1; human.
GeneWiki; GRIPAP1; -.
GenomeRNAi; 56850; -.
PMAP-CutDB; Q4V328; -.
PRO; PR:Q4V328; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000068400; -.
ExpressionAtlas; Q4V328; baseline and differential.
Genevisible; Q4V328; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0098837; C:postsynaptic recycling endosome; IEA:Ensembl.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
GO; GO:1905244; P:regulation of modification of synaptic structure; IEA:Ensembl.
InterPro; IPR026204; GRIPAP1.
PANTHER; PTHR18978; PTHR18978; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Cell projection;
Coiled coil; Complete proteome; Direct protein sequencing; Endosome;
Membrane; Phosphoprotein; Protein transport; Reference proteome;
Synapse; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 841 GRIP1-associated protein 1.
/FTId=PRO_0000087581.
CHAIN 599 841 GRASP-1 C-terminal chain.
/FTId=PRO_0000441811.
COILED 4 161 {ECO:0000255}.
COILED 208 641 {ECO:0000255}.
COILED 701 735 {ECO:0000255}.
COILED 785 814 {ECO:0000255}.
SITE 598 599 Cleavage; by caspase-3.
{ECO:0000250|UniProtKB:Q9JHZ4}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 655 655 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VD04}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VD04}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JHZ4}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 691 691 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VD04}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 1 110 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015699.
VAR_SEQ 103 155 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015700.
VAR_SEQ 111 152 EQENQQLKEGAAGAGVAQAGPLVDGELLRLQAENTALQKNV
A -> MWSFGTGTLPPEGLKASSPSIRGMARDFRDHLIHHI
FLFYSP (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015701.
VAR_SEQ 317 347 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_015702.
VAR_SEQ 534 559 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015703.
VAR_SEQ 688 704 SLSSSPQAQPPRPAELS -> VRGKEEPTAPASLNPKI
(in isoform 2 and isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015704.
VAR_SEQ 705 841 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015705.
CONFLICT 677 677 R -> G (in Ref. 6; CAB95949).
{ECO:0000305}.
SEQUENCE 841 AA; 95990 MW; 48877D04F6630213 CRC64;
MAQALSEEEF QRMQAQLLEL RTNNYQLSDE LRKNGVELTS LRQKVAYLDK EFSKAQKALS
KSKKAQEVEV LLSENEMLQA KLHSQEEDFR LQNSTLMAEF SKLCSQMEQL EQENQQLKEG
AAGAGVAQAG PLVDGELLRL QAENTALQKN VAALQERYGK EAGKFSAVSE GQGDPPGGPA
PTVLAPMPLA EVELKWEMEK EEKRLLWEQL QGLESSKQAE TSRLQEELAK LSEKLKKKQE
SFCRLQTEKE TLFNDSRNKI EELQQRKEAD HKAQLARTQK LQQELEAANQ SLAELRDQRQ
GERLEHAAAL RALQDQVSIQ SADAQEQVEG LLAENNALRT SLAALEQIQT AKTQELNMLR
EQTTGLAAEL QQQQAEYEDL MGQKDDLNSQ LQESLRANSR LLEQLQEIGQ EKEQLTQELQ
EARKSAEKRK AMLDELAMET LQEKSQHKEE LGAVRLRHEK EVLGVRARYE RELRELHEDK
KRQEEELRGQ IREEKARTRE LETLQQTVEE LQAQVHSMDG AKGWFERRLK EAEESLQQQQ
QEQEEALKQC REQHAAELKG KEEELQDVRD QLEQAQEERD CHLKTISSLK QEVKDTVDGQ
RILEKKGSAA LKDLKRQLHL ERKRADKLQE RLQDILTNSK SRSGLEELVL SEMNSPSRTQ
TGDSSSISSF SYREILREKE SSAVPARSLS SSPQAQPPRP AELSDEEVAE LFQRLAETQQ
EKWMLEEKVK HLEVSSASMA EDLCRKSAII ETYVMDSRID VSVAAGHTDR SGLGSVLRDL
VKPGDENLRE MNKKLQNMLE EQLTKNMHLH KDMEVLSQEI VRLSKECVGP PDPDLEPGET
S


Related products :

Catalog number Product name Quantity
18-662-20038 GRIP1-associated protein 1 - GRASP-1 Polyclonal 0.1 ml
LF-PA40524 anti-Grasp, Rabbit polyclonal to Grasp, Isotype IgG, Host Rabbit 50 ug
AHP1548 RABBIT ANTI RAT GRASP, Product Type Polyclonal Antibody, Specificity GRASP, Target Species Rat, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications WB, Clone 0.1 ml
SCH-AHP1548 RABBIT ANTI RAT GRASP, Product Type Polyclonal Antibody, Specificity GRASP, Target Species Rat, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications WB, Clone 0.1 ml
GWB-MT060F Grasp antibody - N-terminal region
gen0022 CD166_MOUSE Protein DM-GRASP ELISA tesk kit 1
gen0012 CD166_CHICK Protein DM-GRASP ELISA tesk kit 1
GRASP GRAP2 Gene GRB2-related adaptor protein 2
CSB-EL009885RA Rat General receptor for phosphoinositides 1-associated scaffold protein(GRASP) ELISA kit 96T
CSB-EL009885RA Rat General receptor for phosphoinositides 1-associated scaffold protein(GRASP) ELISA kit SpeciesRat 96T
CSB-EL009885MO Mouse General receptor for phosphoinositides 1-associated scaffold protein(GRASP) ELISA kit 96T
GRB10 GRASP Gene GRP1 (general receptor for phosphoinositides 1)-associated scaffold protein
CSB-EL009885HU Human General receptor for phosphoinositides 1-associated scaffold protein(GRASP) ELISA kit 96T
CSB-EL009885HU Human General receptor for phosphoinositides 1-associated scaffold protein(GRASP) ELISA kit SpeciesHuman 96T
CSB-EL009885MO Mouse General receptor for phosphoinositides 1-associated scaffold protein(GRASP) ELISA kit SpeciesMouse 96T
ABP-PAB-11641 General receptor for phosphoinositides 1_associated scaffold protein (Grasp) polyclonal antibody 100 ug
EIAAB09431 Atpgd1,ATP-grasp domain-containing protein 1,Carnosine synthase 1,Carns1,Kiaa1394,Mouse,Mus musculus
GRASP_MOUSE ELISA Kit FOR General receptor for phosphoinositides 1-associated scaffold protein; organism: Mouse; gene name: Grasp 96T
EIAAB09429 ATPGD1,ATP-grasp domain-containing protein 1,Carnosine synthase 1,CARNS1,Homo sapiens,Human,KIAA1394
060806A Grasp 250ul
009745A GRASP 250ul
AP09356PU-N GRASP 0.1 mg
NB300-310 GRASP 0.1 ml
AP05772PU-N GRASP 0.1 ml
045220A Grasp 250ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur