GRAP1_HUMAN
ID GRAP1_HUMAN Reviewed; 841 AA.
AC Q4V328; A6NL78; Q3MJ75; Q4V327; Q4V330; Q5HYG1; Q6N046; Q96DH8; Q9NQ43;
AC Q9ULQ3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=GRIP1-associated protein 1 {ECO:0000305};
DE Short=GRASP-1;
DE Contains:
DE RecName: Full=GRASP-1 C-terminal chain {ECO:0000250|UniProtKB:Q9JHZ4};
DE AltName: Full=30kDa C-terminus form;
GN Name=GRIPAP1 {ECO:0000312|HGNC:HGNC:18706}; Synonyms=KIAA1167;
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 2), AND VARIANT PRO-179.
RC TISSUE=Prostate, and Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-179.
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-841 (ISOFORM 1), AND VARIANT
RP PRO-179.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [5]
RP PROTEIN SEQUENCE OF 401-412, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 677-841.
RC TISSUE=Fetal brain;
RX PubMed=10908365; DOI=10.1093/nar/28.15.e72;
RA Holt L.J., Bussow K., Walter G., Tomlinson I.M.;
RT "By-passing selection: direct screening for antibody-antigen interactions
RT using protein arrays.";
RL Nucleic Acids Res. 28:72-72(2000).
RN [7]
RP SUBCELLULAR LOCATION, AND ROLE IN RAYNAUD SYNDROME.
RX PubMed=15897011; DOI=10.1016/j.clim.2005.03.021;
RA Stinton L.M., Selak S., Fritzler M.J.;
RT "Identification of GRASP-1 as a novel 97 kDa autoantigen localized to
RT endosomes.";
RL Clin. Immunol. 116:108-117(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH MAPK8 AND MAP3K1.
RX PubMed=17761173; DOI=10.1016/j.febslet.2007.08.008;
RA Ye B., Yu W.P., Thomas G.M., Huganir R.L.;
RT "GRASP-1 is a neuronal scaffold protein for the JNK signaling pathway.";
RL FEBS Lett. 581:4403-4410(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-690 AND SER-692, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP INTERACTION WITH RAB4A.
RX PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
RA Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
RA Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R., Oorschot V.,
RA Govers R., Monti M., Heck A.J., Sheng M., Klumperman J., Rehmann H.,
RA Jaarsma D., Kapitein L.C., van der Sluijs P.;
RT "Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization
RT and maturation of recycling endosomes.";
RL PLoS Biol. 8:E1000283-E1000283(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Regulates the endosomal recycling back to the neuronal plasma
CC membrane, possibly by connecting early and late recycling endosomal
CC domains and promoting segregation of recycling endosomes from early
CC endosomal membranes. Involved in the localization of recycling
CC endosomes to dendritic spines, thereby playing a role in the
CC maintenance of dendritic spine morphology. Required for the activity-
CC induced AMPA receptor recycling to dendrite membranes and for long-term
CC potentiation and synaptic plasticity (By similarity).
CC {ECO:0000250|UniProtKB:Q9JHZ4}.
CC -!- FUNCTION: [GRASP-1 C-terminal chain]: Functions as a scaffold protein
CC to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by
CC phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close
CC proximity. {ECO:0000269|PubMed:17761173}.
CC -!- SUBUNIT: Interacts with GRIP1, GRIP2 and AMPA receptors (By
CC similarity). Interacts (via C-terminus) with MAPK8/JNK1 and
CC MAP3K1/MEKK1; the interaction promotes MAP3K1-mediated phosphorylation
CC of MAPK8 (PubMed:17761173). Interacts (via N-terminus) with RAB4A (in
CC GTP-bound form) (PubMed:20098723). Interacts (via C-terminus) with
CC STX12 (By similarity). {ECO:0000250|UniProtKB:Q9JHZ4,
CC ECO:0000269|PubMed:17761173, ECO:0000269|PubMed:20098723}.
CC -!- INTERACTION:
CC Q4V328; Q4LEZ3: AARD; NbExp=3; IntAct=EBI-717919, EBI-5463075;
CC Q4V328; X5D778: ANKRD11; NbExp=3; IntAct=EBI-717919, EBI-17183751;
CC Q4V328; Q9H1Y0: ATG5; NbExp=3; IntAct=EBI-717919, EBI-1047414;
CC Q4V328; Q13895: BYSL; NbExp=3; IntAct=EBI-717919, EBI-358049;
CC Q4V328; Q9HC52: CBX8; NbExp=3; IntAct=EBI-717919, EBI-712912;
CC Q4V328; Q8IW40: CCDC103; NbExp=8; IntAct=EBI-717919, EBI-10261970;
CC Q4V328; Q8N715: CCDC185; NbExp=3; IntAct=EBI-717919, EBI-740814;
CC Q4V328; P51946: CCNH; NbExp=3; IntAct=EBI-717919, EBI-741406;
CC Q4V328; Q16543: CDC37; NbExp=3; IntAct=EBI-717919, EBI-295634;
CC Q4V328; Q8IYX8: CEP57L1; NbExp=6; IntAct=EBI-717919, EBI-1104570;
CC Q4V328; Q96M91: CFAP53; NbExp=3; IntAct=EBI-717919, EBI-742422;
CC Q4V328; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-717919, EBI-5453285;
CC Q4V328; Q9UER7: DAXX; NbExp=3; IntAct=EBI-717919, EBI-77321;
CC Q4V328; Q9NRI5: DISC1; NbExp=5; IntAct=EBI-717919, EBI-529989;
CC Q4V328; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-717919, EBI-11988027;
CC Q4V328; Q9BV47: DUSP26; NbExp=3; IntAct=EBI-717919, EBI-2924519;
CC Q4V328; Q08426: EHHADH; NbExp=3; IntAct=EBI-717919, EBI-2339219;
CC Q4V328; Q14241: ELOA; NbExp=3; IntAct=EBI-717919, EBI-742350;
CC Q4V328; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-717919, EBI-744099;
CC Q4V328; Q3B820: FAM161A; NbExp=3; IntAct=EBI-717919, EBI-719941;
CC Q4V328; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-717919, EBI-742802;
CC Q4V328; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-717919, EBI-6658203;
CC Q4V328; O95995: GAS8; NbExp=3; IntAct=EBI-717919, EBI-1052570;
CC Q4V328; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-717919, EBI-717919;
CC Q4V328; P56524-2: HDAC4; NbExp=3; IntAct=EBI-717919, EBI-11953488;
CC Q4V328; Q9UNL4: ING4; NbExp=3; IntAct=EBI-717919, EBI-2866661;
CC Q4V328; Q8WYH8: ING5; NbExp=6; IntAct=EBI-717919, EBI-488533;
CC Q4V328; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-717919, EBI-739832;
CC Q4V328; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-717919, EBI-16439278;
CC Q4V328; P55081: MFAP1; NbExp=3; IntAct=EBI-717919, EBI-1048159;
CC Q4V328; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-717919, EBI-14086479;
CC Q4V328; P55198: MLLT6; NbExp=3; IntAct=EBI-717919, EBI-740216;
CC Q4V328; Q9H093: NUAK2; NbExp=3; IntAct=EBI-717919, EBI-1181722;
CC Q4V328; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-717919, EBI-14066006;
CC Q4V328; Q99959-2: PKP2; NbExp=3; IntAct=EBI-717919, EBI-10987518;
CC Q4V328; Q6NYC8: PPP1R18; NbExp=4; IntAct=EBI-717919, EBI-2557469;
CC Q4V328; Q99633: PRPF18; NbExp=3; IntAct=EBI-717919, EBI-2798416;
CC Q4V328; P20618: PSMB1; NbExp=3; IntAct=EBI-717919, EBI-372273;
CC Q4V328; P20338: RAB4A; NbExp=4; IntAct=EBI-717919, EBI-722284;
CC Q4V328; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-717919, EBI-1504830;
CC Q4V328; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-717919, EBI-455078;
CC Q4V328; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-717919, EBI-12004298;
CC Q4V328; Q13573: SNW1; NbExp=3; IntAct=EBI-717919, EBI-632715;
CC Q4V328; Q9ULZ2: STAP1; NbExp=3; IntAct=EBI-717919, EBI-6083058;
CC Q4V328; Q9Y2I9-2: TBC1D30; NbExp=3; IntAct=EBI-717919, EBI-17455779;
CC Q4V328; Q15560: TCEA2; NbExp=3; IntAct=EBI-717919, EBI-710310;
CC Q4V328; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-717919, EBI-3923210;
CC Q4V328; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-717919, EBI-11139477;
CC Q4V328; Q12933: TRAF2; NbExp=3; IntAct=EBI-717919, EBI-355744;
CC Q4V328; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-717919, EBI-10241197;
CC Q4V328; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-717919, EBI-10687282;
CC Q4V328; Q99598: TSNAX; NbExp=3; IntAct=EBI-717919, EBI-742638;
CC Q4V328; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-717919, EBI-9090990;
CC Q4V328; O75604: USP2; NbExp=3; IntAct=EBI-717919, EBI-743272;
CC Q4V328; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-717919, EBI-2682299;
CC Q4V328; Q9P2Y4: ZNF219; NbExp=3; IntAct=EBI-717919, EBI-3937106;
CC Q4V328; P15622-3: ZNF250; NbExp=3; IntAct=EBI-717919, EBI-10177272;
CC Q4V328; P13682: ZNF35; NbExp=3; IntAct=EBI-717919, EBI-11041653;
CC Q4V328; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-717919, EBI-5667516;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:15897011}; Peripheral membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9JHZ4}. Synapse {ECO:0000250|UniProtKB:Q9JHZ4}.
CC Note=Localizes to recycling endosomal tubules that are emanating from
CC early endosomes. {ECO:0000250|UniProtKB:Q9JHZ4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q4V328-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4V328-2; Sequence=VSP_015700, VSP_015703, VSP_015704,
CC VSP_015705;
CC Name=3;
CC IsoId=Q4V328-4; Sequence=VSP_015702;
CC -!- PTM: Proteolytically cleaved by caspase-3. A minor C-terminal
CC proteolytic fragment of 30 kDa is produced. Proteolytic cleavage is
CC required for JNK signaling activation. {ECO:0000250|UniProtKB:Q9JHZ4}.
CC -!- MISCELLANEOUS: Antibodies against GRIPAP1 have been found in sera of a
CC patient who developed Raynaud's syndrome and telangiectasias.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE45824.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX640704; CAE45824.1; ALT_SEQ; mRNA.
DR EMBL; BX647804; CAI45985.1; ALT_TERM; mRNA.
DR EMBL; AF207550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX530088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001522; AAH01522.2; -; mRNA.
DR EMBL; BC101544; AAI01545.1; -; mRNA.
DR EMBL; BC101546; AAI01547.1; -; mRNA.
DR EMBL; AB032993; BAA86481.1; -; mRNA.
DR EMBL; AJ297364; CAB95949.1; -; mRNA.
DR CCDS; CCDS35248.1; -. [Q4V328-1]
DR RefSeq; NP_064522.3; NM_020137.4. [Q4V328-1]
DR AlphaFoldDB; Q4V328; -.
DR SMR; Q4V328; -.
DR BioGRID; 121210; 162.
DR CORUM; Q4V328; -.
DR DIP; DIP-47299N; -.
DR IntAct; Q4V328; 79.
DR MINT; Q4V328; -.
DR STRING; 9606.ENSP00000365606; -.
DR GlyGen; Q4V328; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q4V328; -.
DR MetOSite; Q4V328; -.
DR PhosphoSitePlus; Q4V328; -.
DR BioMuta; GRIPAP1; -.
DR DMDM; 74753569; -.
DR EPD; Q4V328; -.
DR jPOST; Q4V328; -.
DR MassIVE; Q4V328; -.
DR PaxDb; Q4V328; -.
DR PeptideAtlas; Q4V328; -.
DR PRIDE; Q4V328; -.
DR ProteomicsDB; 62272; -. [Q4V328-1]
DR ProteomicsDB; 62273; -. [Q4V328-2]
DR ProteomicsDB; 62275; -. [Q4V328-4]
DR Antibodypedia; 355; 230 antibodies from 32 providers.
DR DNASU; 56850; -.
DR Ensembl; ENST00000376423.8; ENSP00000365606.5; ENSG00000068400.13. [Q4V328-1]
DR Ensembl; ENST00000593475.5; ENSP00000469842.2; ENSG00000068400.13. [Q4V328-4]
DR GeneID; 56850; -.
DR KEGG; hsa:56850; -.
DR MANE-Select; ENST00000376423.8; ENSP00000365606.5; NM_020137.5; NP_064522.4.
DR UCSC; uc033ecr.2; human. [Q4V328-1]
DR CTD; 56850; -.
DR GeneCards; GRIPAP1; -.
DR HGNC; HGNC:18706; GRIPAP1.
DR HPA; ENSG00000068400; Low tissue specificity.
DR MIM; 300408; gene.
DR neXtProt; NX_Q4V328; -.
DR OpenTargets; ENSG00000068400; -.
DR PharmGKB; PA38650; -.
DR VEuPathDB; HostDB:ENSG00000068400; -.
DR eggNOG; ENOG502QTUD; Eukaryota.
DR GeneTree; ENSGT00720000108868; -.
DR HOGENOM; CLU_019728_1_0_1; -.
DR InParanoid; Q4V328; -.
DR OMA; LQKNVAX; -.
DR OrthoDB; 1273136at2759; -.
DR PhylomeDB; Q4V328; -.
DR TreeFam; TF329006; -.
DR PathwayCommons; Q4V328; -.
DR SignaLink; Q4V328; -.
DR SIGNOR; Q4V328; -.
DR BioGRID-ORCS; 56850; 11 hits in 711 CRISPR screens.
DR ChiTaRS; GRIPAP1; human.
DR GeneWiki; GRIPAP1; -.
DR GenomeRNAi; 56850; -.
DR Pharos; Q4V328; Tbio.
DR PRO; PR:Q4V328; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q4V328; protein.
DR Bgee; ENSG00000068400; Expressed in right hemisphere of cerebellum and 170 other tissues.
DR ExpressionAtlas; Q4V328; baseline and differential.
DR Genevisible; Q4V328; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098998; C:extrinsic component of postsynaptic early endosome membrane; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; IBA:GO_Central.
DR GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0099158; P:regulation of recycling endosome localization within postsynapse; IBA:GO_Central.
DR InterPro; IPR026204; GRIPAP1.
DR PANTHER; PTHR18978; PTHR18978; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil;
KW Direct protein sequencing; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..841
FT /note="GRIP1-associated protein 1"
FT /id="PRO_0000087581"
FT CHAIN 599..841
FT /note="GRASP-1 C-terminal chain"
FT /id="PRO_0000441811"
FT REGION 532..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..161
FT /evidence="ECO:0000255"
FT COILED 208..641
FT /evidence="ECO:0000255"
FT COILED 701..735
FT /evidence="ECO:0000255"
FT COILED 785..814
FT /evidence="ECO:0000255"
FT COMPBIAS 684..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 598..599
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q9JHZ4"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD04"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD04"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHZ4"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD04"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 103..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015700"
FT VAR_SEQ 317..347
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_015702"
FT VAR_SEQ 534..559
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015703"
FT VAR_SEQ 688..704
FT /note="SLSSSPQAQPPRPAELS -> VRGKEEPTAPASLNPKI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015704"
FT VAR_SEQ 705..841
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015705"
FT VARIANT 179
FT /note="L -> P (in dbSNP:rs61735977)"
FT /evidence="ECO:0000269|PubMed:10574461,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_080637"
FT CONFLICT 677
FT /note="R -> G (in Ref. 6; CAB95949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 841 AA; 96006 MW; 10B6A50DAFBBC9D9 CRC64;
MAQALSEEEF QRMQAQLLEL RTNNYQLSDE LRKNGVELTS LRQKVAYLDK EFSKAQKALS
KSKKAQEVEV LLSENEMLQA KLHSQEEDFR LQNSTLMAEF SKLCSQMEQL EQENQQLKEG
AAGAGVAQAG PLVDGELLRL QAENTALQKN VAALQERYGK EAGKFSAVSE GQGDPPGGLA
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
