RAB3I_HUMAN
ID RAB3I_HUMAN Reviewed; 476 AA.
AC Q96QF0; B7WPJ6; Q6PCE4; Q96A24; Q96QE6; Q96QE7; Q96QE8; Q96QE9; Q96QF1;
AC Q9H673;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Rab-3A-interacting protein;
DE Short=Rab3A-interacting protein;
DE AltName: Full=Rabin-3;
DE AltName: Full=SSX2-interacting protein;
GN Name=RAB3IP {ECO:0000312|EMBL:CAC59836.1}; Synonyms=RABIN8;
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] {ECO:0000305, ECO:0000312|EMBL:CAC59836.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), INTERACTION WITH
RP SSX2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis {ECO:0000269|PubMed:12007189};
RX PubMed=12007189; DOI=10.1002/gcc.10073;
RA de Bruijn D.R.H., dos Santos N.R., Kater-Baats E., Thijssen J.,
RA van den Berk L., Stap J., Balemans M., Schepens M., Merkx G.,
RA van Kessel A.G.;
RT "The cancer-related protein SSX2 interacts with the human homologue of a
RT Ras-like GTPase interactor, RAB3IP, and a novel nuclear protein, SSX2IP.";
RL Genes Chromosomes Cancer 34:285-298(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAB3A; RAB8A AND
RP RAB8B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12221131; DOI=10.1091/mbc.e02-03-0143;
RA Hattula K., Furuhjelm J., Arffman A., Peranen J.;
RT "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling
RT and polarized membrane transport.";
RL Mol. Biol. Cell 13:3268-3280(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB15391.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 8).
RC TISSUE=Small intestine {ECO:0000312|EMBL:BAB15391.1}, and
RC Teratocarcinoma {ECO:0000312|EMBL:BAB55202.1};
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH59358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH59358.1}, and
RC Colon {ECO:0000312|EMBL:AAH15548.1};
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
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 [10]
RP FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [11]
RP FUNCTION.
RX PubMed=20890297; DOI=10.1038/ncb2106;
RA Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J.,
RA Martin-Belmonte F., Mostov K.E.;
RT "A molecular network for de novo generation of the apical surface and
RT lumen.";
RL Nat. Cell Biol. 12:1035-1045(2010).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP INTERACTION WITH DCDC1.
RX PubMed=22159412; DOI=10.1242/jcs.085407;
RA Kaplan A., Reiner O.;
RT "Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody
RT during cytokinesis by the doublecortin domain-containing 5 protein.";
RL J. Cell Sci. 124:3989-4000(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-266 AND SER-288, AND
RP IDENTIFICATION BY 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 [15]
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).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH RAB8A.
RX PubMed=26824392; DOI=10.7554/elife.12813;
RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S.,
RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J.,
RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.;
RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates
RT a subset of Rab GTPases.";
RL Elife 5:0-0(2016).
RN [17]
RP INTERACTION WITH TRAPPC14, AND SUBCELLULAR LOCATION.
RX PubMed=31467083; DOI=10.1074/jbc.ra119.008615;
RA Cuenca A., Insinna C., Zhao H., John P., Weiss M.A., Lu Q., Walia V.,
RA Specht S., Manivannan S., Stauffer J., Peden A.A., Westlake C.J.;
RT "The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for
RT preciliary vesicle tethering at the mother centriole during ciliogenesis.";
RL J. Biol. Chem. 294:15418-15434(2019).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate
CC RAB8A and RAB8B (PubMed:12221131, PubMed:26824392). Promotes the
CC exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into
CC their active GTP-bound form (PubMed:12221131, PubMed:26824392).
CC Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or
CC RAB5 (PubMed:20937701, PubMed:26824392). Modulates actin organization
CC and promotes polarized transport of RAB8A-specific vesicles to the cell
CC surface (PubMed:12221131). Together with RAB11A, RAB8A, the exocyst
CC complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of
CC PODXL to the apical membrane initiation sites (AMIS), apical surface
CC formation and lumenogenesis (PubMed:20890297).
CC {ECO:0000269|PubMed:12221131, ECO:0000269|PubMed:20890297,
CC ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:26824392}.
CC -!- SUBUNIT: Interacts with the N-terminal region of SSX2
CC (PubMed:12007189). Interacts with the GDP-bound forms of RAB8A and
CC RAB8B (PubMed:26824392, PubMed:12221131). The interaction with RAB8A is
CC prevented by phosphorylation of RAB8A at 'Thr-72' (PubMed:26824392).
CC Interacts with the GDP-bound forms of RAB3A and RAB3D
CC (PubMed:12221131). Interacts with DCDC1 (PubMed:22159412,
CC PubMed:12007189, PubMed:12221131, PubMed:26824392). Interacts (via the
CC N-terminal region) with TRAPPC14; this interaction mediates RAB3IP
CC association with the TRAPP II complex (PubMed:31467083).
CC {ECO:0000269|PubMed:12007189, ECO:0000269|PubMed:12221131,
CC ECO:0000269|PubMed:22159412, ECO:0000269|PubMed:26824392,
CC ECO:0000269|PubMed:31467083}.
CC -!- INTERACTION:
CC Q96QF0; Q8N9N5: BANP; NbExp=3; IntAct=EBI-747844, EBI-744695;
CC Q96QF0; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-747844, EBI-743375;
CC Q96QF0; Q86V42: FAM124A; NbExp=3; IntAct=EBI-747844, EBI-744506;
CC Q96QF0; Q6A162: KRT40; NbExp=3; IntAct=EBI-747844, EBI-10171697;
CC Q96QF0; P41227: NAA10; NbExp=3; IntAct=EBI-747844, EBI-747693;
CC Q96QF0; O60568: PLOD3; NbExp=4; IntAct=EBI-747844, EBI-741582;
CC Q96QF0; O60437: PPL; NbExp=3; IntAct=EBI-747844, EBI-368321;
CC Q96QF0; P20336: RAB3A; NbExp=3; IntAct=EBI-747844, EBI-1045943;
CC Q96QF0; Q8TBN0: RAB3IL1; NbExp=9; IntAct=EBI-747844, EBI-743796;
CC Q96QF0; P61006: RAB8A; NbExp=5; IntAct=EBI-747844, EBI-722293;
CC Q96QF0; Q96T51: RUFY1; NbExp=3; IntAct=EBI-747844, EBI-3941207;
CC Q96QF0; P31947: SFN; NbExp=3; IntAct=EBI-747844, EBI-476295;
CC Q96QF0; Q16385: SSX2B; NbExp=4; IntAct=EBI-747844, EBI-2210673;
CC Q96QF0; P48553: TRAPPC10; NbExp=7; IntAct=EBI-747844, EBI-6160572;
CC Q96QF0; O75865: TRAPPC6A; NbExp=4; IntAct=EBI-747844, EBI-743573;
CC Q96QF0; Q86VK4: ZNF410; NbExp=3; IntAct=EBI-747844, EBI-720304;
CC Q96QF0; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-747844, EBI-25492395;
CC Q96QF0-1; Q8NFJ9: BBS1; NbExp=2; IntAct=EBI-747860, EBI-1805484;
CC Q96QF0-2; O60568: PLOD3; NbExp=3; IntAct=EBI-747865, EBI-741582;
CC Q96QF0-2; P62491: RAB11A; NbExp=8; IntAct=EBI-747865, EBI-745098;
CC Q96QF0-2; O75154-1: RAB11FIP3; NbExp=6; IntAct=EBI-747865, EBI-15605207;
CC Q96QF0-2; Q96QF0-2: RAB3IP; NbExp=2; IntAct=EBI-747865, EBI-747865;
CC Q96QF0-2; P61006: RAB8A; NbExp=2; IntAct=EBI-747865, EBI-722293;
CC Q96QF0-2; Q16385: SSX2B; NbExp=4; IntAct=EBI-747865, EBI-2210673;
CC Q96QF0-7; P46379-2: BAG6; NbExp=3; IntAct=EBI-11984839, EBI-10988864;
CC Q96QF0-7; Q8N9N5-2: BANP; NbExp=6; IntAct=EBI-11984839, EBI-11524452;
CC Q96QF0-7; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-11984839, EBI-16429296;
CC Q96QF0-7; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-11984839, EBI-10181422;
CC Q96QF0-7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-11984839, EBI-10976677;
CC Q96QF0-7; P59910: DNAJB13; NbExp=3; IntAct=EBI-11984839, EBI-11514233;
CC Q96QF0-7; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-11984839, EBI-12593112;
CC Q96QF0-7; P50570-2: DNM2; NbExp=3; IntAct=EBI-11984839, EBI-10968534;
CC Q96QF0-7; P14136: GFAP; NbExp=3; IntAct=EBI-11984839, EBI-744302;
CC Q96QF0-7; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-11984839, EBI-6398041;
CC Q96QF0-7; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-11984839, EBI-1055254;
CC Q96QF0-7; O14901: KLF11; NbExp=3; IntAct=EBI-11984839, EBI-948266;
CC Q96QF0-7; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-11984839, EBI-11323212;
CC Q96QF0-7; O95983-2: MBD3; NbExp=3; IntAct=EBI-11984839, EBI-11978579;
CC Q96QF0-7; P41227: NAA10; NbExp=3; IntAct=EBI-11984839, EBI-747693;
CC Q96QF0-7; P19404: NDUFV2; NbExp=3; IntAct=EBI-11984839, EBI-713665;
CC Q96QF0-7; Q86TG7-2: PEG10; NbExp=3; IntAct=EBI-11984839, EBI-6259410;
CC Q96QF0-7; Q16512: PKN1; NbExp=3; IntAct=EBI-11984839, EBI-602382;
CC Q96QF0-7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-11984839, EBI-25882629;
CC Q96QF0-7; O60437: PPL; NbExp=3; IntAct=EBI-11984839, EBI-368321;
CC Q96QF0-7; O43741: PRKAB2; NbExp=3; IntAct=EBI-11984839, EBI-1053424;
CC Q96QF0-7; P20336: RAB3A; NbExp=3; IntAct=EBI-11984839, EBI-1045943;
CC Q96QF0-7; O95716: RAB3D; NbExp=3; IntAct=EBI-11984839, EBI-3386067;
CC Q96QF0-7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-11984839, EBI-5235340;
CC Q96QF0-7; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-11984839, EBI-12018146;
CC Q96QF0-7; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-11984839, EBI-11139477;
CC Q96QF0-7; O14656-2: TOR1A; NbExp=3; IntAct=EBI-11984839, EBI-25847109;
CC Q96QF0-7; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-11984839, EBI-8451480;
CC Q96QF0-7; Q05516: ZBTB16; NbExp=3; IntAct=EBI-11984839, EBI-711925;
CC Q96QF0-7; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-11984839, EBI-11741890;
CC Q96QF0-7; P36508: ZNF76; NbExp=3; IntAct=EBI-11984839, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12007189,
CC ECO:0000269|PubMed:31467083}. Nucleus {ECO:0000269|PubMed:12007189}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12221131}. Cell projection,
CC lamellipodium. Vesicle {ECO:0000269|PubMed:31467083}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:31467083}. Note=Predominantly cytoplasmic but a
CC small proportion colocalizes with SSX2 in the nucleus. Activation of
CC protein kinase C results in redistribution to the periphery of
CC lamellipodia. {ECO:0000269|PubMed:12007189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=2 {ECO:0000269|PubMed:12007189}; Synonyms=alpha2
CC {ECO:0000303|PubMed:12007189};
CC IsoId=Q96QF0-1; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:12007189}; Synonyms=alpha1
CC {ECO:0000303|PubMed:12007189};
CC IsoId=Q96QF0-2; Sequence=VSP_051755;
CC Name=3 {ECO:0000269|PubMed:12007189}; Synonyms=beta1
CC {ECO:0000303|PubMed:12007189};
CC IsoId=Q96QF0-3; Sequence=VSP_051755, VSP_051761, VSP_051762;
CC Name=4 {ECO:0000269|PubMed:12007189}; Synonyms=beta2
CC {ECO:0000303|PubMed:12007189};
CC IsoId=Q96QF0-4; Sequence=VSP_051761, VSP_051762;
CC Name=5 {ECO:0000269|PubMed:12007189}; Synonyms=gamma1
CC {ECO:0000303|PubMed:12007189};
CC IsoId=Q96QF0-5; Sequence=VSP_051755, VSP_051757, VSP_051759;
CC Name=6 {ECO:0000269|PubMed:12007189}; Synonyms=gamma2
CC {ECO:0000303|PubMed:12007189};
CC IsoId=Q96QF0-6; Sequence=VSP_051757, VSP_051759;
CC Name=7 {ECO:0000305};
CC IsoId=Q96QF0-7; Sequence=VSP_051755, VSP_051758, VSP_051760;
CC Name=8 {ECO:0000305};
CC IsoId=Q96QF0-8; Sequence=VSP_051756;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, heart, pancreas and
CC placenta. Not detected in skeletal muscle or liver.
CC {ECO:0000269|PubMed:12007189, ECO:0000269|PubMed:12221131}.
CC -!- SIMILARITY: Belongs to the SEC2 family. {ECO:0000255}.
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; AJ312896; CAC59835.1; -; mRNA.
DR EMBL; AJ312897; CAC59836.1; -; mRNA.
DR EMBL; AJ312898; CAC59837.1; -; mRNA.
DR EMBL; AJ312899; CAC59838.1; -; mRNA.
DR EMBL; AJ312900; CAC59839.1; -; mRNA.
DR EMBL; AJ312901; CAC59840.1; -; mRNA.
DR EMBL; AK026201; BAB15391.1; -; mRNA.
DR EMBL; AK027566; BAB55202.1; -; mRNA.
DR EMBL; AK027671; BAB55283.1; -; mRNA.
DR EMBL; AC025263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015548; AAH15548.1; -; mRNA.
DR EMBL; BC059358; AAH59358.1; -; mRNA.
DR CCDS; CCDS41811.1; -. [Q96QF0-4]
DR CCDS; CCDS44942.1; -. [Q96QF0-8]
DR CCDS; CCDS8993.1; -. [Q96QF0-1]
DR CCDS; CCDS8995.1; -. [Q96QF0-2]
DR CCDS; CCDS8996.1; -. [Q96QF0-3]
DR RefSeq; NP_001019818.1; NM_001024647.3. [Q96QF0-8]
DR RefSeq; NP_001265331.1; NM_001278402.1. [Q96QF0-8]
DR RefSeq; NP_071901.2; NM_022456.4. [Q96QF0-2]
DR RefSeq; NP_783322.1; NM_175623.3. [Q96QF0-1]
DR RefSeq; NP_783323.1; NM_175624.3. [Q96QF0-3]
DR RefSeq; NP_783324.1; NM_175625.3. [Q96QF0-4]
DR RefSeq; XP_016874262.1; XM_017018773.1. [Q96QF0-2]
DR RefSeq; XP_016874265.1; XM_017018776.1.
DR RefSeq; XP_016874266.1; XM_017018777.1. [Q96QF0-8]
DR PDB; 4LHX; X-ray; 3.05 A; C/D/E/F=173-248.
DR PDB; 4LHY; X-ray; 3.10 A; C/D/E/F=173-248.
DR PDB; 4LHZ; X-ray; 3.20 A; C/D/E/F=173-248.
DR PDB; 4UJ3; X-ray; 3.00 A; B/E/H/K/N/Q/T/W=286-476.
DR PDB; 4UJ4; X-ray; 4.20 A; B/E/H/K=286-476.
DR PDB; 4UJ5; X-ray; 2.60 A; C/D=286-476.
DR PDB; 6F6P; X-ray; 2.45 A; A/B/C/D=159-261.
DR PDBsum; 4LHX; -.
DR PDBsum; 4LHY; -.
DR PDBsum; 4LHZ; -.
DR PDBsum; 4UJ3; -.
DR PDBsum; 4UJ4; -.
DR PDBsum; 4UJ5; -.
DR PDBsum; 6F6P; -.
DR AlphaFoldDB; Q96QF0; -.
DR SMR; Q96QF0; -.
DR BioGRID; 125566; 109.
DR DIP; DIP-41703N; -.
DR IntAct; Q96QF0; 91.
DR MINT; Q96QF0; -.
DR STRING; 9606.ENSP00000447300; -.
DR GlyGen; Q96QF0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96QF0; -.
DR PhosphoSitePlus; Q96QF0; -.
DR BioMuta; RAB3IP; -.
DR DMDM; 71152025; -.
DR EPD; Q96QF0; -.
DR jPOST; Q96QF0; -.
DR MassIVE; Q96QF0; -.
DR MaxQB; Q96QF0; -.
DR PaxDb; Q96QF0; -.
DR PeptideAtlas; Q96QF0; -.
DR PRIDE; Q96QF0; -.
DR ProteomicsDB; 77867; -. [Q96QF0-1]
DR ProteomicsDB; 77868; -. [Q96QF0-2]
DR ProteomicsDB; 77869; -. [Q96QF0-3]
DR ProteomicsDB; 77870; -. [Q96QF0-4]
DR ProteomicsDB; 77871; -. [Q96QF0-5]
DR ProteomicsDB; 77872; -. [Q96QF0-6]
DR ProteomicsDB; 77873; -. [Q96QF0-7]
DR ProteomicsDB; 77874; -. [Q96QF0-8]
DR Antibodypedia; 29437; 235 antibodies from 24 providers.
DR DNASU; 117177; -.
DR Ensembl; ENST00000247833.12; ENSP00000247833.7; ENSG00000127328.22. [Q96QF0-2]
DR Ensembl; ENST00000362025.9; ENSP00000355381.5; ENSG00000127328.22. [Q96QF0-4]
DR Ensembl; ENST00000378815.10; ENSP00000368092.6; ENSG00000127328.22. [Q96QF0-7]
DR Ensembl; ENST00000417413.7; ENSP00000436304.2; ENSG00000127328.22. [Q96QF0-5]
DR Ensembl; ENST00000483530.6; ENSP00000419216.2; ENSG00000127328.22. [Q96QF0-3]
DR Ensembl; ENST00000550536.5; ENSP00000447300.1; ENSG00000127328.22. [Q96QF0-1]
DR Ensembl; ENST00000551641.5; ENSP00000448773.1; ENSG00000127328.22. [Q96QF0-8]
DR Ensembl; ENST00000552199.5; ENSP00000448944.1; ENSG00000127328.22. [Q96QF0-6]
DR Ensembl; ENST00000553099.5; ENSP00000448027.1; ENSG00000127328.22. [Q96QF0-8]
DR GeneID; 117177; -.
DR KEGG; hsa:117177; -.
DR MANE-Select; ENST00000247833.12; ENSP00000247833.7; NM_022456.5; NP_071901.2. [Q96QF0-2]
DR UCSC; uc001svm.5; human. [Q96QF0-1]
DR CTD; 117177; -.
DR DisGeNET; 117177; -.
DR GeneCards; RAB3IP; -.
DR HGNC; HGNC:16508; RAB3IP.
DR HPA; ENSG00000127328; Low tissue specificity.
DR MIM; 608686; gene.
DR neXtProt; NX_Q96QF0; -.
DR OpenTargets; ENSG00000127328; -.
DR PharmGKB; PA34136; -.
DR VEuPathDB; HostDB:ENSG00000127328; -.
DR eggNOG; KOG4324; Eukaryota.
DR GeneTree; ENSGT00940000157998; -.
DR HOGENOM; CLU_038204_2_0_1; -.
DR InParanoid; Q96QF0; -.
DR OMA; WAMASEP; -.
DR OrthoDB; 619794at2759; -.
DR PhylomeDB; Q96QF0; -.
DR TreeFam; TF313748; -.
DR PathwayCommons; Q96QF0; -.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q96QF0; -.
DR SIGNOR; Q96QF0; -.
DR BioGRID-ORCS; 117177; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; RAB3IP; human.
DR GeneWiki; RAB3IP; -.
DR GenomeRNAi; 117177; -.
DR Pharos; Q96QF0; Tbio.
DR PRO; PR:Q96QF0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96QF0; protein.
DR Bgee; ENSG00000127328; Expressed in right testis and 141 other tissues.
DR ExpressionAtlas; Q96QF0; baseline and differential.
DR Genevisible; Q96QF0; HS.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0036064; C:ciliary basal body; TAS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0070319; C:Golgi to plasma membrane transport vesicle; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:1990635; C:proximal dendrite; IEA:Ensembl.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
DR GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; TAS:BHF-UCL.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0033365; P:protein localization to organelle; IMP:BHF-UCL.
DR GO; GO:0006612; P:protein targeting to membrane; IDA:UniProtKB.
DR InterPro; IPR040351; RAB3IL/RAB3IP/Sec2.
DR InterPro; IPR009449; Sec2_N.
DR PANTHER; PTHR14430; PTHR14430; 1.
DR Pfam; PF06428; Sec2p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Guanine-nucleotide releasing factor; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..476
FT /note="Rab-3A-interacting protein"
FT /id="PRO_0000097144"
FT REGION 262..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..260
FT /evidence="ECO:0000255"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF0"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF0"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051756"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 1, isoform 3, isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:12007189,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_051755"
FT VAR_SEQ 313..331
FT /note="ADLSLYNEFRLWKDEPTMD -> VTHQGLSPLTLLILVSSHH (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051758"
FT VAR_SEQ 313..320
FT /note="ADLSLYNE -> KMCSHWPE (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12007189"
FT /id="VSP_051757"
FT VAR_SEQ 321..476
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12007189"
FT /id="VSP_051759"
FT VAR_SEQ 332..476
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051760"
FT VAR_SEQ 394..411
FT /note="KCALTGQSKSCKHRIKLG -> SLLYVTFLHTFDTFSRDS (in isoform
FT 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12007189"
FT /id="VSP_051761"
FT VAR_SEQ 412..476
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12007189"
FT /id="VSP_051762"
FT CONFLICT 164
FT /note="P -> Q (in Ref. 5; AAH59358)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="N -> D (in Ref. 3; BAB15391)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="Missing (in Ref. 3; BAB15391)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="M -> V (in Ref. 3; BAB15391)"
FT /evidence="ECO:0000305"
FT HELIX 165..260
FT /evidence="ECO:0007829|PDB:6F6P"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4UJ3"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:4UJ5"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:4UJ5"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:4UJ5"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:4UJ5"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:4UJ5"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:4UJ3"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:4UJ5"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:4UJ5"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:4UJ5"
FT HELIX 421..441
FT /evidence="ECO:0007829|PDB:4UJ5"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:4UJ5"
FT HELIX 450..468
FT /evidence="ECO:0007829|PDB:4UJ5"
SQ SEQUENCE 476 AA; 53021 MW; DD77781823038F15 CRC64;
MGLKKMKGLS YDEAFAMAND PLEGFHEVNL ASPTSPDLLG VYESGTQEQT TSPSVIYRPH
PSALSSVPIQ ANALDVSELP TQPVYSSPRR LNCAEISSIS FHVTDPAPCS TSGVTAGLTK
LTTRKDNYNA EREFLQGATI TEACDGSDDI FGLSTDSLSR LRSPSVLEVR EKGYERLKEE
LAKAQRELKL KDEECERLSK VRDQLGQELE ELTASLFEEA HKMVREANIK QATAEKQLKE
AQGKIDVLQA EVAALKTLVL SSSPTSPTQE PLPGGKTPFK KGHTRNKSTS SAMSGSHQDL
SVIQPIVKDC KEADLSLYNE FRLWKDEPTM DRTCPFLDKI YQEDIFPCLT FSKSELASAV
LEAVENNTLS IEPVGLQPIR FVKASAVECG GPKKCALTGQ SKSCKHRIKL GDSSNYYYIS
PFCRYRITSV CNFFTYIRYI QQGLVKQQDV DQMFWEVMQL RKEMSLAKLG YFKEEL
