RABE2_HUMAN
ID RABE2_HUMAN Reviewed; 569 AA.
AC Q9H5N1;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Rab GTPase-binding effector protein 2;
DE AltName: Full=Rabaptin-5beta;
GN Name=RABEP2; Synonyms=RABPT5B;
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=Hepatoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RABGEF1.
RX PubMed=9524116; DOI=10.1093/emboj/17.7.1930;
RA Gournier H., Stenmark H., Rybin V., Lippe R., Zerial M.;
RT "Two distinct effectors of the small GTPase Rab5 cooperate in endocytic
RT membrane fusion.";
RL EMBO J. 17:1930-1940(1998).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SDCCAG8.
RX PubMed=27224062; DOI=10.1371/journal.pone.0156081;
RA Airik R., Schueler M., Airik M., Cho J., Ulanowicz K.A., Porath J.D.,
RA Hurd T.W., Bekker-Jensen S., Schroeder J.M., Andersen J.S., Hildebrandt F.;
RT "SDCCAG8 interacts with RAB effector proteins RABEP2 and ERC1 and is
RT required for Hedgehog Signaling.";
RL PLoS ONE 11:E0156081-E0156081(2016).
RN [9]
RP PHOSPHORYLATION AT SER-200 AND SER-204, AND SUBCELLULAR LOCATION.
RX PubMed=29247183; DOI=10.1038/s41598-017-17087-6;
RA Logie L., Van Aalten L., Knebel A., Force T., Hastie C.J., MacLauchlan H.,
RA Campbell D.G., Gourlay R., Prescott A., Davidson J., Fuller W.,
RA Sutherland C.;
RT "Rab-GTPase binding effector protein 2 (RABEP2) is a primed substrate for
RT Glycogen Synthase kinase-3 (GSK3).";
RL Sci. Rep. 7:17682-17682(2017).
RN [10]
RP FUNCTION, AND INTERACTION WITH RAB4A.
RX PubMed=29425100; DOI=10.1074/jbc.m117.812172;
RA Kofler N., Corti F., Rivera-Molina F., Deng Y., Toomre D., Simons M.;
RT "The Rab-effector protein RABEP2 regulates endosomal trafficking to mediate
RT vascular endothelial growth factor receptor-2 (VEGFR2)-dependent
RT signaling.";
RL J. Biol. Chem. 293:4805-4817(2018).
CC -!- FUNCTION: Plays a role in membrane trafficking and in homotypic early
CC endosome fusion (PubMed:9524116). Participates in arteriogenesis by
CC regulating vascular endothelial growth factor receptor 2/VEGFR2 cell
CC surface expression and endosomal trafficking (PubMed:29425100). By
CC interacting with SDCCAG8, localizes to centrosomes and plays a critical
CC role in ciliogenesis (PubMed:27224062). {ECO:0000269|PubMed:27224062,
CC ECO:0000269|PubMed:29425100, ECO:0000269|PubMed:9524116}.
CC -!- SUBUNIT: Heterodimer with RABGEF1. The dimer binds RAB5A that has been
CC activated by GTP-binding. Interacts with SDCCAG8; this interaction is
CC important for ciliogenesis regulation (PubMed:27224062). Interacts with
CC RAB4A; this interaction may mediate VEGFR2 cell surface expression
CC (PubMed:29425100). {ECO:0000269|PubMed:27224062,
CC ECO:0000269|PubMed:29425100}.
CC -!- INTERACTION:
CC Q9H5N1; Q86SQ7: SDCCAG8; NbExp=3; IntAct=EBI-3940735, EBI-1047850;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29247183,
CC ECO:0000269|PubMed:9524116}. Early endosome
CC {ECO:0000269|PubMed:9524116}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:27224062}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:27224062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H5N1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H5N1-2; Sequence=VSP_010458, VSP_010459;
CC -!- SIMILARITY: Belongs to the rabaptin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15594.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK026935; BAB15594.1; ALT_FRAME; mRNA.
DR EMBL; BC058900; AAH58900.1; -; mRNA.
DR CCDS; CCDS42140.1; -. [Q9H5N1-1]
DR RefSeq; NP_079092.2; NM_024816.2. [Q9H5N1-1]
DR AlphaFoldDB; Q9H5N1; -.
DR SMR; Q9H5N1; -.
DR BioGRID; 122962; 97.
DR IntAct; Q9H5N1; 17.
DR MINT; Q9H5N1; -.
DR STRING; 9606.ENSP00000350934; -.
DR GlyGen; Q9H5N1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H5N1; -.
DR PhosphoSitePlus; Q9H5N1; -.
DR BioMuta; RABEP2; -.
DR DMDM; 47606049; -.
DR EPD; Q9H5N1; -.
DR jPOST; Q9H5N1; -.
DR MassIVE; Q9H5N1; -.
DR MaxQB; Q9H5N1; -.
DR PaxDb; Q9H5N1; -.
DR PeptideAtlas; Q9H5N1; -.
DR PRIDE; Q9H5N1; -.
DR ProteomicsDB; 80920; -. [Q9H5N1-1]
DR ProteomicsDB; 80921; -. [Q9H5N1-2]
DR Antibodypedia; 26625; 134 antibodies from 26 providers.
DR DNASU; 79874; -.
DR Ensembl; ENST00000357573.10; ENSP00000350186.6; ENSG00000177548.13. [Q9H5N1-2]
DR Ensembl; ENST00000358201.9; ENSP00000350934.4; ENSG00000177548.13. [Q9H5N1-1]
DR GeneID; 79874; -.
DR KEGG; hsa:79874; -.
DR MANE-Select; ENST00000358201.9; ENSP00000350934.4; NM_024816.3; NP_079092.2.
DR UCSC; uc002drq.4; human. [Q9H5N1-1]
DR CTD; 79874; -.
DR DisGeNET; 79874; -.
DR GeneCards; RABEP2; -.
DR HGNC; HGNC:24817; RABEP2.
DR HPA; ENSG00000177548; Low tissue specificity.
DR MIM; 611869; gene.
DR neXtProt; NX_Q9H5N1; -.
DR OpenTargets; ENSG00000177548; -.
DR PharmGKB; PA134952719; -.
DR VEuPathDB; HostDB:ENSG00000177548; -.
DR eggNOG; KOG0993; Eukaryota.
DR GeneTree; ENSGT00530000063743; -.
DR HOGENOM; CLU_035043_0_0_1; -.
DR InParanoid; Q9H5N1; -.
DR OMA; QCDEEIQ; -.
DR OrthoDB; 1369937at2759; -.
DR PhylomeDB; Q9H5N1; -.
DR TreeFam; TF329365; -.
DR PathwayCommons; Q9H5N1; -.
DR SignaLink; Q9H5N1; -.
DR BioGRID-ORCS; 79874; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; RABEP2; human.
DR GenomeRNAi; 79874; -.
DR Pharos; Q9H5N1; Tbio.
DR PRO; PR:Q9H5N1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H5N1; protein.
DR Bgee; ENSG00000177548; Expressed in pancreatic ductal cell and 181 other tissues.
DR ExpressionAtlas; Q9H5N1; baseline and differential.
DR Genevisible; Q9H5N1; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR InterPro; IPR003914; Rabaptin.
DR InterPro; IPR029882; Rabaptin-5beta.
DR InterPro; IPR018514; Rabaptin_coiled-coil.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR PANTHER; PTHR31179; PTHR31179; 1.
DR PANTHER; PTHR31179:SF6; PTHR31179:SF6; 1.
DR Pfam; PF09311; Rab5-bind; 2.
DR Pfam; PF03528; Rabaptin; 1.
DR PRINTS; PR01432; RABAPTIN.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..569
FT /note="Rab GTPase-binding effector protein 2"
FT /id="PRO_0000187559"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..187
FT /evidence="ECO:0000255"
FT COILED 289..523
FT /evidence="ECO:0000255"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62835"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 200
FT /note="Phosphoserine; by GSK3-alpha"
FT /evidence="ECO:0000269|PubMed:29247183"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29247183"
FT VAR_SEQ 299..330
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010458"
FT VAR_SEQ 475..478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010459"
SQ SEQUENCE 569 AA; 63543 MW; 47451AAFA40CF23D CRC64;
MAAAAPVAAD DDERRRRPGA ALEDSRSQEG ANGEAESGEL SRLRAELAGA LAEMETMKAV
AEVSESTKAE AVAAVQRQCQ EEVASLQAIL KDSISSYEAQ ITALKQERQQ QQQDCEEKER
ELGRLKQLLS RAYPLDSLEK QMEKAHEDSE KLREIVLPME KEIEELKAKL LRAEELIQEI
QRRPRHAPSL HGSTELLPLS RDPSPPLEPL EELSGDGGPA AEAFAHNCDD SASISSFSLG
GGVGSSSSLP QSRQGLSPEQ EETASLVSTG TLVPEGIYLP PPGYQLVPDT QWEQLQTEGR
QLQKDLESVS RERDELQEGL RRSNEDCAKQ MQVLLAQVQN SEQLLRTLQG TVSQAQERVQ
LQMAELVTTH KCLHHEVKRL NEENQGLRAE QLPSSAPQGS QQEQGEEESL PSSVPELQQL
LCCTRQEARA RLQAQEHGAE RLRIEIVTLR EALEEETVAR ASLEGQLRVQ REETEVLEAS
LCSLRTEMER VQQEQSKAQL PDLLSEQRAK VLRLQAELET SEQVQRDFVR LSQALQVRLE
RIRQAETLEQ VRSIMDEAPL TDVRDIKDT
