Full text data of RGPD5
RGPD5
(RANBP2L2, RGP6)
[Confidence: low (only semi-automatic identification from reviews)]
RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2; RanBP2-like 1/2; RanBP2L1; RanBP2L2; Sperm membrane protein BS-63)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2; RanBP2-like 1/2; RanBP2L1; RanBP2L2; Sperm membrane protein BS-63)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99666
ID RGPD5_HUMAN Reviewed; 1765 AA.
AC Q99666; Q53QN2; Q53T03; Q59GM7; Q9H0B2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=RANBP2-like and GRIP domain-containing protein 5/6;
DE AltName: Full=Ran-binding protein 2-like 1/2;
DE Short=RanBP2-like 1/2;
DE Short=RanBP2L1;
DE Short=RanBP2L2;
DE AltName: Full=Sperm membrane protein BS-63;
GN Name=RGPD5; Synonyms=RANBP2L1, RGP5, RGP7, RGPD7;
GN and
GN Name=RGPD6; Synonyms=RANBP2L2, RGP6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10101573; DOI=10.1080/014850199262904;
RA Wang L.F., Zhu H.D., Miao S.Y., Cao D.F., Wu Y.W., Zong S.D.,
RA Koide S.S.;
RT "Molecular cloning and characterization of a novel testis-specific
RT nucleoporin-related gene.";
RL Arch. Androl. 42:71-84(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1009-1765 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15710750; DOI=10.1101/gr.3266405;
RA Ciccarelli F.D., von Mering C., Suyama M., Harrington E.D.,
RA Izaurralde E., Bork P.;
RT "Complex genomic rearrangements lead to novel primate gene function.";
RL Genome Res. 15:343-351(2005).
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-21, AND MASS
RP SPECTROMETRY.
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99666-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99666-2; Sequence=VSP_038968, VSP_038969;
CC -!- TISSUE SPECIFICITY: Expressed in testis.
CC -!- MISCELLANEOUS: One of the 8 copies of RANBP2 clustered close to
CC the chromosome 2 centromere.
CC -!- SIMILARITY: Contains 1 GRIP domain.
CC -!- SIMILARITY: Contains 2 RanBD1 domains.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; U64675; AAB41848.2; -; mRNA.
DR EMBL; AL136868; CAB66802.1; -; mRNA.
DR EMBL; AC013271; AAY14902.1; -; Genomic_DNA.
DR EMBL; AC123886; AAY14839.1; -; Genomic_DNA.
DR EMBL; AC108938; AAY24132.1; -; Genomic_DNA.
DR EMBL; AC109815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209082; BAD92319.1; -; mRNA.
DR RefSeq; NP_001032955.1; NM_001037866.1.
DR RefSeq; NP_001116835.1; NM_001123363.3.
DR RefSeq; NP_005045.2; NM_005054.2.
DR RefSeq; NP_115636.1; NM_032260.2.
DR UniGene; Hs.469630; -.
DR UniGene; Hs.645445; -.
DR ProteinModelPortal; Q99666; -.
DR SMR; Q99666; 3-145, 649-674, 1051-1178, 1348-1464, 1663-1700.
DR IntAct; Q99666; 5.
DR MINT; MINT-2817131; -.
DR STRING; 9606.ENSP00000016946; -.
DR PhosphoSite; Q99666; -.
DR PaxDb; Q99666; -.
DR PRIDE; Q99666; -.
DR DNASU; 729540; -.
DR DNASU; 84220; -.
DR Ensembl; ENST00000016946; ENSP00000016946; ENSG00000015568.
DR Ensembl; ENST00000272454; ENSP00000272454; ENSG00000015568.
DR Ensembl; ENST00000329516; ENSP00000330842; ENSG00000183054.
DR Ensembl; ENST00000330331; ENSP00000330023; ENSG00000183054.
DR Ensembl; ENST00000393283; ENSP00000376962; ENSG00000015568.
DR GeneID; 729540; -.
DR GeneID; 84220; -.
DR KEGG; hsa:729540; -.
DR KEGG; hsa:84220; -.
DR UCSC; uc002tfe.1; human.
DR CTD; 729540; -.
DR CTD; 84220; -.
DR GeneCards; GC02M111271; -.
DR GeneCards; GC02P110550; -.
DR HGNC; HGNC:32418; RGPD5.
DR HGNC; HGNC:32419; RGPD6.
DR MIM; 612708; gene.
DR MIM; 612709; gene.
DR MIM; 612710; gene.
DR neXtProt; NX_Q99666; -.
DR PharmGKB; PA142671074; -.
DR eggNOG; COG5171; -.
DR HOGENOM; HOG000089994; -.
DR HOVERGEN; HBG108404; -.
DR InParanoid; Q53T03; -.
DR PhylomeDB; Q99666; -.
DR ChiTaRS; RGPD5; human.
DR GeneWiki; RGPD5; -.
DR NextBio; 130592; -.
DR PRO; PR:Q99666; -.
DR ArrayExpress; Q99666; -.
DR Bgee; Q99666; -.
DR CleanEx; HS_RGPD5; -.
DR CleanEx; HS_RGPD8; -.
DR Genevestigator; Q99666; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000042; P:protein targeting to Golgi; IEA:InterPro.
DR Gene3D; 1.10.220.60; -; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR000237; GRIP.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF01465; GRIP; 1.
DR Pfam; PF00638; Ran_BP1; 2.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00755; Grip; 1.
DR SMART; SM00160; RanBD; 2.
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 Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 1765 RANBP2-like and GRIP domain-containing
FT protein 5/6.
FT /FTId=PRO_0000204915.
FT REPEAT 26 59 TPR 1.
FT REPEAT 60 93 TPR 2.
FT REPEAT 648 681 TPR 3.
FT DOMAIN 1036 1172 RanBD1 1.
FT DOMAIN 1333 1469 RanBD1 2.
FT DOMAIN 1702 1752 GRIP.
FT COMPBIAS 1261 1266 Poly-Ser.
FT MOD_RES 19 19 Phosphothreonine.
FT MOD_RES 21 21 Phosphoserine.
FT VAR_SEQ 868 904 VATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGSSNT ->
FT EAAHRHFTIEKHGDSKWIIYRFTKQLCGTERARAKIS (in
FT isoform 2).
FT /FTId=VSP_038968.
FT VAR_SEQ 905 1765 Missing (in isoform 2).
FT /FTId=VSP_038969.
FT CONFLICT 174 174 L -> V (in Ref. 1; AAB41848).
FT CONFLICT 204 204 N -> H (in Ref. 1; AAB41848).
FT CONFLICT 214 214 Y -> H (in Ref. 1; AAB41848).
FT CONFLICT 229 229 Q -> R (in Ref. 1; AAB41848).
FT CONFLICT 257 257 E -> G (in Ref. 1; AAB41848).
FT CONFLICT 270 270 K -> E (in Ref. 1; AAB41848).
FT CONFLICT 451 451 L -> S (in Ref. 1; AAB41848).
FT CONFLICT 736 736 P -> S (in Ref. 1; AAB41848).
FT CONFLICT 784 784 K -> R (in Ref. 1; AAB41848).
FT CONFLICT 893 893 A -> G (in Ref. 1; AAB41848).
FT CONFLICT 905 905 E -> D (in Ref. 1; AAB41848).
FT CONFLICT 946 946 F -> L (in Ref. 1; AAB41848).
FT CONFLICT 1074 1074 R -> S (in Ref. 1; AAB41848).
FT CONFLICT 1135 1135 D -> H (in Ref. 1; AAB41848).
FT CONFLICT 1612 1612 S -> P (in Ref. 1; AAB41848).
FT CONFLICT 1682 1682 L -> P (in Ref. 1; AAB41848).
SQ SEQUENCE 1765 AA; 198924 MW; DC699DC82C67749D CRC64;
MRRSKADVER YVASVLGLTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP
KAHRFLGLLY ELEENTEKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVELYRSTKR
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWQA 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 HITFAMLDAV
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 ENDTGFQAQD ISGRKKGRGV
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 KGSGTGAAGA 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 IAVAILEETT
RERTDVIQGD DVADAASEVE VSSTSETTTK AVVSPPKFVF VSESVKRIFS SEKSKPFVFG
NSSATGSLFG FSFNAPLKSN NSETSSVAQS GSESKVEPKK CELSKNSDIE QSSDSKVKNL
SASFPTEESS INYTFKTPEK EPPLWHAEFT KEELVQKLRS TTKSADHLNG LLREIEATNA
VLMEQIKLLK SEIRRLERNQ EREKSAANLE YLKNVLLQFI FLKPGSERER LLPVINTMLQ
LSPEEKGKLA AVAQDEEENA SRSSG
//
ID RGPD5_HUMAN Reviewed; 1765 AA.
AC Q99666; Q53QN2; Q53T03; Q59GM7; Q9H0B2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=RANBP2-like and GRIP domain-containing protein 5/6;
DE AltName: Full=Ran-binding protein 2-like 1/2;
DE Short=RanBP2-like 1/2;
DE Short=RanBP2L1;
DE Short=RanBP2L2;
DE AltName: Full=Sperm membrane protein BS-63;
GN Name=RGPD5; Synonyms=RANBP2L1, RGP5, RGP7, RGPD7;
GN and
GN Name=RGPD6; Synonyms=RANBP2L2, RGP6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10101573; DOI=10.1080/014850199262904;
RA Wang L.F., Zhu H.D., Miao S.Y., Cao D.F., Wu Y.W., Zong S.D.,
RA Koide S.S.;
RT "Molecular cloning and characterization of a novel testis-specific
RT nucleoporin-related gene.";
RL Arch. Androl. 42:71-84(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1009-1765 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15710750; DOI=10.1101/gr.3266405;
RA Ciccarelli F.D., von Mering C., Suyama M., Harrington E.D.,
RA Izaurralde E., Bork P.;
RT "Complex genomic rearrangements lead to novel primate gene function.";
RL Genome Res. 15:343-351(2005).
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-21, AND MASS
RP SPECTROMETRY.
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99666-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99666-2; Sequence=VSP_038968, VSP_038969;
CC -!- TISSUE SPECIFICITY: Expressed in testis.
CC -!- MISCELLANEOUS: One of the 8 copies of RANBP2 clustered close to
CC the chromosome 2 centromere.
CC -!- SIMILARITY: Contains 1 GRIP domain.
CC -!- SIMILARITY: Contains 2 RanBD1 domains.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; U64675; AAB41848.2; -; mRNA.
DR EMBL; AL136868; CAB66802.1; -; mRNA.
DR EMBL; AC013271; AAY14902.1; -; Genomic_DNA.
DR EMBL; AC123886; AAY14839.1; -; Genomic_DNA.
DR EMBL; AC108938; AAY24132.1; -; Genomic_DNA.
DR EMBL; AC109815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209082; BAD92319.1; -; mRNA.
DR RefSeq; NP_001032955.1; NM_001037866.1.
DR RefSeq; NP_001116835.1; NM_001123363.3.
DR RefSeq; NP_005045.2; NM_005054.2.
DR RefSeq; NP_115636.1; NM_032260.2.
DR UniGene; Hs.469630; -.
DR UniGene; Hs.645445; -.
DR ProteinModelPortal; Q99666; -.
DR SMR; Q99666; 3-145, 649-674, 1051-1178, 1348-1464, 1663-1700.
DR IntAct; Q99666; 5.
DR MINT; MINT-2817131; -.
DR STRING; 9606.ENSP00000016946; -.
DR PhosphoSite; Q99666; -.
DR PaxDb; Q99666; -.
DR PRIDE; Q99666; -.
DR DNASU; 729540; -.
DR DNASU; 84220; -.
DR Ensembl; ENST00000016946; ENSP00000016946; ENSG00000015568.
DR Ensembl; ENST00000272454; ENSP00000272454; ENSG00000015568.
DR Ensembl; ENST00000329516; ENSP00000330842; ENSG00000183054.
DR Ensembl; ENST00000330331; ENSP00000330023; ENSG00000183054.
DR Ensembl; ENST00000393283; ENSP00000376962; ENSG00000015568.
DR GeneID; 729540; -.
DR GeneID; 84220; -.
DR KEGG; hsa:729540; -.
DR KEGG; hsa:84220; -.
DR UCSC; uc002tfe.1; human.
DR CTD; 729540; -.
DR CTD; 84220; -.
DR GeneCards; GC02M111271; -.
DR GeneCards; GC02P110550; -.
DR HGNC; HGNC:32418; RGPD5.
DR HGNC; HGNC:32419; RGPD6.
DR MIM; 612708; gene.
DR MIM; 612709; gene.
DR MIM; 612710; gene.
DR neXtProt; NX_Q99666; -.
DR PharmGKB; PA142671074; -.
DR eggNOG; COG5171; -.
DR HOGENOM; HOG000089994; -.
DR HOVERGEN; HBG108404; -.
DR InParanoid; Q53T03; -.
DR PhylomeDB; Q99666; -.
DR ChiTaRS; RGPD5; human.
DR GeneWiki; RGPD5; -.
DR NextBio; 130592; -.
DR PRO; PR:Q99666; -.
DR ArrayExpress; Q99666; -.
DR Bgee; Q99666; -.
DR CleanEx; HS_RGPD5; -.
DR CleanEx; HS_RGPD8; -.
DR Genevestigator; Q99666; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000042; P:protein targeting to Golgi; IEA:InterPro.
DR Gene3D; 1.10.220.60; -; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR000237; GRIP.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF01465; GRIP; 1.
DR Pfam; PF00638; Ran_BP1; 2.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00755; Grip; 1.
DR SMART; SM00160; RanBD; 2.
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 Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 1765 RANBP2-like and GRIP domain-containing
FT protein 5/6.
FT /FTId=PRO_0000204915.
FT REPEAT 26 59 TPR 1.
FT REPEAT 60 93 TPR 2.
FT REPEAT 648 681 TPR 3.
FT DOMAIN 1036 1172 RanBD1 1.
FT DOMAIN 1333 1469 RanBD1 2.
FT DOMAIN 1702 1752 GRIP.
FT COMPBIAS 1261 1266 Poly-Ser.
FT MOD_RES 19 19 Phosphothreonine.
FT MOD_RES 21 21 Phosphoserine.
FT VAR_SEQ 868 904 VATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGSSNT ->
FT EAAHRHFTIEKHGDSKWIIYRFTKQLCGTERARAKIS (in
FT isoform 2).
FT /FTId=VSP_038968.
FT VAR_SEQ 905 1765 Missing (in isoform 2).
FT /FTId=VSP_038969.
FT CONFLICT 174 174 L -> V (in Ref. 1; AAB41848).
FT CONFLICT 204 204 N -> H (in Ref. 1; AAB41848).
FT CONFLICT 214 214 Y -> H (in Ref. 1; AAB41848).
FT CONFLICT 229 229 Q -> R (in Ref. 1; AAB41848).
FT CONFLICT 257 257 E -> G (in Ref. 1; AAB41848).
FT CONFLICT 270 270 K -> E (in Ref. 1; AAB41848).
FT CONFLICT 451 451 L -> S (in Ref. 1; AAB41848).
FT CONFLICT 736 736 P -> S (in Ref. 1; AAB41848).
FT CONFLICT 784 784 K -> R (in Ref. 1; AAB41848).
FT CONFLICT 893 893 A -> G (in Ref. 1; AAB41848).
FT CONFLICT 905 905 E -> D (in Ref. 1; AAB41848).
FT CONFLICT 946 946 F -> L (in Ref. 1; AAB41848).
FT CONFLICT 1074 1074 R -> S (in Ref. 1; AAB41848).
FT CONFLICT 1135 1135 D -> H (in Ref. 1; AAB41848).
FT CONFLICT 1612 1612 S -> P (in Ref. 1; AAB41848).
FT CONFLICT 1682 1682 L -> P (in Ref. 1; AAB41848).
SQ SEQUENCE 1765 AA; 198924 MW; DC699DC82C67749D CRC64;
MRRSKADVER YVASVLGLTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP
KAHRFLGLLY ELEENTEKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVELYRSTKR
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWQA 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 HITFAMLDAV
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 ENDTGFQAQD ISGRKKGRGV
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 KGSGTGAAGA 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 IAVAILEETT
RERTDVIQGD DVADAASEVE VSSTSETTTK AVVSPPKFVF VSESVKRIFS SEKSKPFVFG
NSSATGSLFG FSFNAPLKSN NSETSSVAQS GSESKVEPKK CELSKNSDIE QSSDSKVKNL
SASFPTEESS INYTFKTPEK EPPLWHAEFT KEELVQKLRS TTKSADHLNG LLREIEATNA
VLMEQIKLLK SEIRRLERNQ EREKSAANLE YLKNVLLQFI FLKPGSERER LLPVINTMLQ
LSPEEKGKLA AVAQDEEENA SRSSG
//
MIM
612708
*RECORD*
*FIELD* NO
612708
*FIELD* TI
*612708 RANBP2-LIKE AND GRIP DOMAIN-CONTAINING PROTEIN 5; RGPD5
;;RGP5;;
BS63
*FIELD* TX
read more
CLONING
Using 5-prime RACE and nested PCR of testis total RNA, Cai et al. (2002)
cloned RGPD5, which they designated BS63. The deduced 1,765-amino acid
protein has structural characteristics of nucleoporins. Most of the
protein shares high homology with RANBP2 (601181), but it has a unique C
terminus. Cai et al. (2002) stated that Northern blot analysis detected
an 8.5-kb transcript in several human tissues and a 6-kb transcript in
testis only. Using immunoelectron microscopy of demembranated human
sperm, Cai et al. (2002) found that BS63 localized to the nuclear
membrane. In rat testis sections, Bs63 localized to nuclear pores in
spermatids.
By searching databases for intrachromosomal duplications of genes in
primates but not in other metazoans, Ciccarelli et al. (2005) identified
8 RGPD genes, including RGPD5, which they called RGP5. The RGPD genes
resulted from duplications of a region of human chromosome 2 containing
the RANBP2 and GCC2 (612711) genes. Like other RGPD proteins, the
deduced RGPD5 protein exceeds 1,700 amino acids. Most of the sequence is
homologous to regions of RANBP2, except for the C terminus, which
includes the GRIP domain from GCC2. Using primers that did not
differentiate between RGPD5 and RGPD6 (612709) for PCR analysis,
Ciccarelli et al. (2005) detected expression in testis and HeLa cell
cDNA libraries.
GENE FUNCTION
Using yeast 2-hybrid analysis of a mouse testis cDNA library, Cai et al.
(2002) found that human BS63 interacted with Ran (601179), transportin-1
(TNPO1; 602901), and Af10 (MLLT10; 602409), suggesting that BS63
functions in nuclear transport.
MAPPING
By genomic sequence analysis, Ciccarelli et al. (2005) mapped the 8 RGPD
genes to chromosome 2p11.2-q13, and they named the genes according to
their physical order. RGPD5 is 1 of 6 RGPD genes on chromosome
2q12.3-q13.
EVOLUTION
See RGPD1 (612704) for information on the evolution of the RGPD genes.
*FIELD* RF
1. Cai, Y.; Gao, Y.; Sheng, Q.; Miao, S.; Cui, X.; Wang, L.; Zong,
S.; Koide, S. S.: Characterization and potential function of a novel
testis-specific nucleoporin BS-63. Molec. Reprod. Dev. 61: 126-134,
2002. Erratum: Molec. Reprod. Dev. 61: 279 only, 2002.
2. Ciccarelli, F. D.; von Mering, C.; Suyama, M.; Harrington, E. D.;
Izaurralde E.; Bork, P.: Complex genomic rearrangements lead to novel
primate gene function. Genome Res. 15: 343-351, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2009
*FIELD* ED
carol: 04/04/2013
mgross: 4/3/2009
*RECORD*
*FIELD* NO
612708
*FIELD* TI
*612708 RANBP2-LIKE AND GRIP DOMAIN-CONTAINING PROTEIN 5; RGPD5
;;RGP5;;
BS63
*FIELD* TX
read more
CLONING
Using 5-prime RACE and nested PCR of testis total RNA, Cai et al. (2002)
cloned RGPD5, which they designated BS63. The deduced 1,765-amino acid
protein has structural characteristics of nucleoporins. Most of the
protein shares high homology with RANBP2 (601181), but it has a unique C
terminus. Cai et al. (2002) stated that Northern blot analysis detected
an 8.5-kb transcript in several human tissues and a 6-kb transcript in
testis only. Using immunoelectron microscopy of demembranated human
sperm, Cai et al. (2002) found that BS63 localized to the nuclear
membrane. In rat testis sections, Bs63 localized to nuclear pores in
spermatids.
By searching databases for intrachromosomal duplications of genes in
primates but not in other metazoans, Ciccarelli et al. (2005) identified
8 RGPD genes, including RGPD5, which they called RGP5. The RGPD genes
resulted from duplications of a region of human chromosome 2 containing
the RANBP2 and GCC2 (612711) genes. Like other RGPD proteins, the
deduced RGPD5 protein exceeds 1,700 amino acids. Most of the sequence is
homologous to regions of RANBP2, except for the C terminus, which
includes the GRIP domain from GCC2. Using primers that did not
differentiate between RGPD5 and RGPD6 (612709) for PCR analysis,
Ciccarelli et al. (2005) detected expression in testis and HeLa cell
cDNA libraries.
GENE FUNCTION
Using yeast 2-hybrid analysis of a mouse testis cDNA library, Cai et al.
(2002) found that human BS63 interacted with Ran (601179), transportin-1
(TNPO1; 602901), and Af10 (MLLT10; 602409), suggesting that BS63
functions in nuclear transport.
MAPPING
By genomic sequence analysis, Ciccarelli et al. (2005) mapped the 8 RGPD
genes to chromosome 2p11.2-q13, and they named the genes according to
their physical order. RGPD5 is 1 of 6 RGPD genes on chromosome
2q12.3-q13.
EVOLUTION
See RGPD1 (612704) for information on the evolution of the RGPD genes.
*FIELD* RF
1. Cai, Y.; Gao, Y.; Sheng, Q.; Miao, S.; Cui, X.; Wang, L.; Zong,
S.; Koide, S. S.: Characterization and potential function of a novel
testis-specific nucleoporin BS-63. Molec. Reprod. Dev. 61: 126-134,
2002. Erratum: Molec. Reprod. Dev. 61: 279 only, 2002.
2. Ciccarelli, F. D.; von Mering, C.; Suyama, M.; Harrington, E. D.;
Izaurralde E.; Bork, P.: Complex genomic rearrangements lead to novel
primate gene function. Genome Res. 15: 343-351, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2009
*FIELD* ED
carol: 04/04/2013
mgross: 4/3/2009
MIM
612709
*RECORD*
*FIELD* NO
612709
*FIELD* TI
*612709 RANBP2-LIKE AND GRIP DOMAIN-CONTAINING PROTEIN 6; RGPD6
;;RGP6
*FIELD* TX
read moreCLONING
By searching databases for intrachromosomal duplications of genes in
primates but not in other metazoans, Ciccarelli et al. (2005) identified
8 RGPD genes, including RGPD6, which they called RGP6. The RGPD genes
resulted from duplications of a region of human chromosome 2 containing
the RANBP2 (601181) and GCC2 (612711) genes. Like other RGPD proteins,
the deduced RGPD6 protein exceeds 1,700 amino acids. Most of the
sequence is homologous to regions of RANBP2, except for the C terminus,
which includes the GRIP domain from GCC2. Using primers that did not
differentiate between RGPD5 (612708) and RGPD6 for PCR analysis,
Ciccarelli et al. (2005) detected expression in testis and HeLa cell
cDNA libraries.
MAPPING
By genomic sequence analysis, Ciccarelli et al. (2005) mapped the 8 RGPD
genes to chromosome 2p11.2-q13, and they named the genes according to
their physical order. RGPD6 is 1 of 6 RGPD genes on chromosome
2q12.3-q13.
EVOLUTION
See RGPD1 (612704) for information on the evolution of the RGPD genes.
*FIELD* RF
1. Ciccarelli, F. D.; von Mering, C.; Suyama, M.; Harrington, E. D.;
Izaurralde E.; Bork, P.: Complex genomic rearrangements lead to novel
primate gene function. Genome Res. 15: 343-351, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2009
*FIELD* ED
mgross: 04/03/2009
mgross: 4/3/2009
*RECORD*
*FIELD* NO
612709
*FIELD* TI
*612709 RANBP2-LIKE AND GRIP DOMAIN-CONTAINING PROTEIN 6; RGPD6
;;RGP6
*FIELD* TX
read moreCLONING
By searching databases for intrachromosomal duplications of genes in
primates but not in other metazoans, Ciccarelli et al. (2005) identified
8 RGPD genes, including RGPD6, which they called RGP6. The RGPD genes
resulted from duplications of a region of human chromosome 2 containing
the RANBP2 (601181) and GCC2 (612711) genes. Like other RGPD proteins,
the deduced RGPD6 protein exceeds 1,700 amino acids. Most of the
sequence is homologous to regions of RANBP2, except for the C terminus,
which includes the GRIP domain from GCC2. Using primers that did not
differentiate between RGPD5 (612708) and RGPD6 for PCR analysis,
Ciccarelli et al. (2005) detected expression in testis and HeLa cell
cDNA libraries.
MAPPING
By genomic sequence analysis, Ciccarelli et al. (2005) mapped the 8 RGPD
genes to chromosome 2p11.2-q13, and they named the genes according to
their physical order. RGPD6 is 1 of 6 RGPD genes on chromosome
2q12.3-q13.
EVOLUTION
See RGPD1 (612704) for information on the evolution of the RGPD genes.
*FIELD* RF
1. Ciccarelli, F. D.; von Mering, C.; Suyama, M.; Harrington, E. D.;
Izaurralde E.; Bork, P.: Complex genomic rearrangements lead to novel
primate gene function. Genome Res. 15: 343-351, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2009
*FIELD* ED
mgross: 04/03/2009
mgross: 4/3/2009
MIM
612710
*RECORD*
*FIELD* NO
612710
*FIELD* TI
*612710 RANBP2-LIKE AND GRIP DOMAIN-CONTAINING PROTEIN 7; RGPD7
;;RGP7
*FIELD* TX
read moreCLONING
By searching databases for intrachromosomal duplications of genes in
primates but not in other metazoans, Ciccarelli et al. (2005) identified
8 RGPD genes, including RGPD7, which they called RGP7. The RGPD genes
resulted from duplications of a region of human chromosome 2 containing
the RANBP2 (601181) and GCC2 (612711) genes. Like other RGPD proteins,
the deduced RGPD7 protein exceeds 1,700 amino acids. Most of the
sequence is homologous to regions of RANBP2, except for the C terminus,
which includes the GRIP domain from GCC2. PCR analysis detected RGPD7
expression in testis and HeLa cell cDNA libraries.
MAPPING
By genomic sequence analysis, Ciccarelli et al. (2005) mapped the 8 RGPD
genes to chromosome 2p11.2-q13, and they named the genes according to
their physical order. RGPD7 is 1 of 6 RGPD genes on chromosome
2q12.3-q13.
EVOLUTION
See RGPD1 (612704) for information on the evolution of the RGPD genes.
*FIELD* RF
1. Ciccarelli, F. D.; von Mering, C.; Suyama, M.; Harrington, E. D.;
Izaurralde E.; Bork, P.: Complex genomic rearrangements lead to novel
primate gene function. Genome Res. 15: 343-351, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2009
*FIELD* ED
mgross: 04/03/2009
*RECORD*
*FIELD* NO
612710
*FIELD* TI
*612710 RANBP2-LIKE AND GRIP DOMAIN-CONTAINING PROTEIN 7; RGPD7
;;RGP7
*FIELD* TX
read moreCLONING
By searching databases for intrachromosomal duplications of genes in
primates but not in other metazoans, Ciccarelli et al. (2005) identified
8 RGPD genes, including RGPD7, which they called RGP7. The RGPD genes
resulted from duplications of a region of human chromosome 2 containing
the RANBP2 (601181) and GCC2 (612711) genes. Like other RGPD proteins,
the deduced RGPD7 protein exceeds 1,700 amino acids. Most of the
sequence is homologous to regions of RANBP2, except for the C terminus,
which includes the GRIP domain from GCC2. PCR analysis detected RGPD7
expression in testis and HeLa cell cDNA libraries.
MAPPING
By genomic sequence analysis, Ciccarelli et al. (2005) mapped the 8 RGPD
genes to chromosome 2p11.2-q13, and they named the genes according to
their physical order. RGPD7 is 1 of 6 RGPD genes on chromosome
2q12.3-q13.
EVOLUTION
See RGPD1 (612704) for information on the evolution of the RGPD genes.
*FIELD* RF
1. Ciccarelli, F. D.; von Mering, C.; Suyama, M.; Harrington, E. D.;
Izaurralde E.; Bork, P.: Complex genomic rearrangements lead to novel
primate gene function. Genome Res. 15: 343-351, 2005.
*FIELD* CD
Patricia A. Hartz: 4/2/2009
*FIELD* ED
mgross: 04/03/2009