RGPD8_HUMAN
ID RGPD8_HUMAN Reviewed; 1765 AA.
AC O14715; Q5CZA8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=RANBP2-like and GRIP domain-containing protein 8;
DE AltName: Full=Ran-binding protein 2-like 3;
DE Short=RanBP2-like 3;
DE Short=RanBP2L3;
GN Name=RGPD8; Synonyms=RANBP2ALPHA, RANBP2L1, RANBP2L3;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1011-1765.
RX PubMed=9480752; DOI=10.1006/geno.1997.5119;
RA Nothwang H.G., Rensing C., Kubler M., Denich D., Brandl B., Stubanus M.,
RA Haaf T., Kurnit D., Hildebrandt F.;
RT "Identification of a novel Ran binding protein 2 related gene (RANBP2L1)
RT and detection of a gene cluster on human chromosome 2q11-q12.";
RL Genomics 47:383-392(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1640-1765.
RC TISSUE=Amygdala;
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 [4]
RP INTERACTION WITH ARL1.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-21, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- SUBUNIT: Interacts with GTP-bound ARL1. {ECO:0000269|PubMed:11303027}.
CC -!- MISCELLANEOUS: One of the 8 copies of RANBP2 clustered close to the
CC chromosome 2 centromere.
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DR EMBL; AF012086; AAC05596.1; -; mRNA.
DR EMBL; CR936614; CAI56757.1; -; mRNA.
DR CCDS; CCDS46394.1; -.
DR RefSeq; NP_001157935.1; NM_001164463.1.
DR AlphaFoldDB; O14715; -.
DR SMR; O14715; -.
DR BioGRID; 608294; 79.
DR IntAct; O14715; 31.
DR MINT; O14715; -.
DR STRING; 9606.ENSP00000306637; -.
DR GlyGen; O14715; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14715; -.
DR PhosphoSitePlus; O14715; -.
DR BioMuta; RGPD8; -.
DR EPD; O14715; -.
DR jPOST; O14715; -.
DR MassIVE; O14715; -.
DR MaxQB; O14715; -.
DR PaxDb; O14715; -.
DR PeptideAtlas; O14715; -.
DR PRIDE; O14715; -.
DR ProteomicsDB; 48174; -.
DR Antibodypedia; 70727; 8 antibodies from 8 providers.
DR DNASU; 727851; -.
DR Ensembl; ENST00000302558.8; ENSP00000306637.3; ENSG00000169629.12.
DR GeneID; 727851; -.
DR KEGG; hsa:727851; -.
DR MANE-Select; ENST00000302558.8; ENSP00000306637.3; NM_001164463.1; NP_001157935.1.
DR UCSC; uc002ths.3; human.
DR CTD; 727851; -.
DR GeneCards; RGPD8; -.
DR HGNC; HGNC:9849; RGPD8.
DR HPA; ENSG00000169629; Tissue enhanced (testis).
DR MIM; 602752; gene.
DR neXtProt; NX_O14715; -.
DR OpenTargets; ENSG00000169629; -.
DR PharmGKB; PA34210; -.
DR VEuPathDB; HostDB:ENSG00000169629; -.
DR eggNOG; KOG0864; Eukaryota.
DR GeneTree; ENSGT00940000164065; -.
DR HOGENOM; CLU_004100_0_0_1; -.
DR InParanoid; O14715; -.
DR OMA; CKENMEL; -.
DR OrthoDB; 1339144at2759; -.
DR PhylomeDB; O14715; -.
DR TreeFam; TF314797; -.
DR PathwayCommons; O14715; -.
DR SignaLink; O14715; -.
DR BioGRID-ORCS; 727851; 18 hits in 218 CRISPR screens.
DR ChiTaRS; RGPD8; human.
DR GenomeRNAi; 727851; -.
DR Pharos; O14715; Tdark.
DR PRO; PR:O14715; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O14715; protein.
DR Bgee; ENSG00000169629; Expressed in calcaneal tendon and 102 other tissues.
DR ExpressionAtlas; O14715; baseline and differential.
DR Genevisible; O14715; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; NAS:UniProtKB.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR032023; GCC2_Rab_bind.
DR InterPro; IPR000237; GRIP_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR23138; PTHR23138; 2.
DR Pfam; PF01465; GRIP; 1.
DR Pfam; PF16704; Rab_bind; 1.
DR Pfam; PF00638; Ran_BP1; 2.
DR SMART; SM00755; Grip; 1.
DR SMART; SM00160; RanBD; 2.
DR SMART; SM00028; TPR; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50913; GRIP; 1.
DR PROSITE; PS50196; RANBD1; 2.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1765
FT /note="RANBP2-like and GRIP domain-containing protein 8"
FT /id="PRO_0000204917"
FT REPEAT 26..59
FT /note="TPR 1"
FT REPEAT 60..93
FT /note="TPR 2"
FT REPEAT 648..681
FT /note="TPR 3"
FT DOMAIN 1036..1172
FT /note="RanBD1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT DOMAIN 1333..1469
FT /note="RanBD1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT DOMAIN 1702..1752
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 760..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CONFLICT 1541
FT /note="V -> G (in Ref. 2; AAC05596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1640
FT /note="K -> A (in Ref. 3; CAI56757)"
FT /evidence="ECO:0000305"
FT CONFLICT 1741
FT /note="L -> P (in Ref. 3; CAI56757)"
FT /evidence="ECO:0000305"
FT CONFLICT 1760
FT /note="P -> A (in Ref. 3; CAI56757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1765 AA; 198993 MW; E8B7462EE211D670 CRC64;
MRRSKADVER YVASVLGLTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP
KAHRFLGLLY ELEENTEKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVELYRSTKR
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA
NLMLLTLSTR DVQENRELLE SFDSALQSAK SSLGGNDELS ATFLEMKGHF YMYAGSLLLK
MGQHGNNVQW RALSELAALC YLIAFQVPRP KIKLREGKAG QNLLEMMACD RLSQSGHMLL
SLSRGKQDFL KEVVETFANK IGQSALYDAL FSSQSPKDTS FLGSDDIGKI DVQEPELEDL
ARYDVGAIRA HNGSLQHLTW LGLQWNSLPA LPGIRKWLKQ LFHRLPHETS RLETNAPESI
CILDLEVFLL GVVYTSHLQL KEKCNSHHSS YQPLCLPFPV CKQLCTERQK SWWDAVCTLI
HRKAVPGNLA KLRLLVQHEI NTLRAQEKHG LQPALLVHWA KYLQKTGSGL NSFYGQLEYI
GRSVHYWKKV LPLLKIIKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA HITFAILDAV
NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS PEEQEECRNY LTKTRDYLIK
IIDDGDSNLS VVKKLPVPLE SVKQMLNSVM QELEDYSEGG PLYKNGSLRN ADSEIKHSTP
SPTKYSLSPS KSYKYSPETP PRWTEDRNSL LNMICQQVEA IKKEMQELKL NSSKSASRHR
WPTENYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
SSNTEFKSTK EGFSIPVSAD GFKFGISEPG NQEKKREKPL ENDTGLQAQD IRGRKKGRGV
IFGQTSSTFT FADVAKSTSG EGFQFGKKDL NFKGFSGAGE KLFSSRYGKM ANKANTSGDF
EKDDDAYKTE DSDDIHFEPV VQMPEKVELV TGEEGEKVLY SQGVKLFRFD AEVRQWKERG
LGNLKILKNE VNGKLRMLMR REQVLKVCAN HWITTTMNLK PLSGSDRAWM WSASDFSDGD
AKLERLAAKF KTPELAEEFK QKFEECQRLL LDIPLQTPHK LVDTGRAAKL IQRAEEMKSG
LKDFKTFLTN DQTKVTEEEN KGSGTGVAGA SDTTIKPNAE NTGPTLEWDN YDLREDALDD
SVSSSSVHAS PLASSPVRKN LFRFDESTTG SNFSFKSALS LSKSPAKLNQ SGTSVGTDEE
SVVTQEEERD GQYFEPVVPL PDLVEVSSGE ENEQVVFSHR AEIYRYDKDV GQWKERGIGD
IKILQNYDNK QVRIVMRRDQ VLKLCANHRI TPDMSLQNMK GTERVWVWTA CDFADGERKV
EHLAVRFKLQ DVADSFKKIF DEAKTAQEKD SLITPHVSRS STPRESPCGK IAVAVLEEIT
RERTDVIQGD DVADAASEVE VSSTSETTTK AVVSPPKFVF VSESVKRIFS SEKSKPFAFG
NSSATGSLFG FSFNAPLKSN NSETSSVAQS GSESKVEPKK CELSKNSDIE QSSDSKVKNL
SASFPTEESS INYTFKTPEK EPPLWHAEFT KEELVQKLRS TTKSADHLNG LLREIEATNA
VLMEQIKLLK SEIRRLERNQ EREKSAANLE YLKNVLLQFI FLKPGSERER LLPVINTMLQ
LSPEEKGKLA AVAQDEEENP SRSSG
