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UniProtKB/Swiss-Prot entry Q9UJ41


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RABX5_HUMAN
Primary accession number Q9UJ41
Secondary accession numbers Q3HKR2 Q3HKR3 Q53FG0
Integrated into Swiss-Prot on July 5, 2004
Sequence was last modified on July 5, 2004 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 59)
Name and origin of the protein
Protein name Rab5 GDP/GTP exchange factor
Synonyms Rabex-5
Rabaptin-5-associated exchange factor for Rab5
RAP1
Gene name
Name: RABGEF1
Synonyms: RABEX5
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1016/S0304-3835(00)00553-X; PubMed=11098082 [NCBI, ExPASy, EBI, Israel, Japan]
Nimmrich I., Erdmann S., Melchers U., Finke U., Hentsch S., Moyer M.P., Hoffmann I., Mueller O.;
"Seven genes that are differentially transcribed in colorectal tumor cell lines.";
Cancer Lett. 160:37-43(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Cervix carcinoma;
Barbieri M.A., Hunker C.M.;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND INTERACTION WITH RABEP1.
DOI=10.1016/S0092-8674(00)80380-3; PubMed=9323142 [NCBI, ExPASy, EBI, Israel, Japan]
Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P., Stenmark H., Rybin V., Wilm M., Ashman K., Mann M., Zerial M.;
"A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function.";
Cell 90:1149-1159(1997).
[9]
FUNCTION, AND INTERACTION WITH RABEP1.
PubMed=11452015 [NCBI, ExPASy, EBI, Israel, Japan]
Lippe R., Miaczynska M., Rybin V., Runge A., Zerial M.;
"Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex.";
Mol. Biol. Cell 12:2219-2228(2001).
[10]
INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/cdg015; PubMed=12505986 [NCBI, ExPASy, EBI, Israel, Japan]
Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S.;
"Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex.";
EMBO J. 22:78-88(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 310-611, FUNCTION, INTERACTION WITH RAB5; RAB21 AND RAB22, AND MUTAGENESIS OF ASP-530; PRO-534; TYR-571 AND THR-574.
DOI=10.1016/j.cell.2004.08.009; PubMed=15339665 [NCBI, ExPASy, EBI, Israel, Japan]
Delprato A., Merithew E., Lambright D.G.;
"Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5.";
Cell 118:607-617(2004).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 139-252 IN COMPLEX WITH UBIQUITIN, UBIQUITINATION, AND MUTAGENESIS OF ALA-196.
DOI=10.1016/j.cell.2006.02.020; PubMed=16499958 [NCBI, ExPASy, EBI, Israel, Japan]
Penengo L., Mapelli M., Murachelli A.G., Confalonieri S., Magri L., Musacchio A., Di Fiore P.P., Polo S., Schneider T.R.;
"Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin.";
Cell 124:1183-1195(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ250042; CAB57359.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ230533; ABA64473.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ230534; ABA64474.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007107; AAP35771.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK127790; BAC87138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC027644; AAQ93362.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223329; BAD97049.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015330; AAH15330.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_055319.1; -.
UniGene Hs.530053
3D structure databases
PDB
1TXU; X-ray; 2.35 A; A=310-611.[ExPASy / RCSB / EBI]
2C7M; X-ray; 2.40 A; A=139-252.[ExPASy / RCSB / EBI]
2C7N; X-ray; 2.10 A; A/C/E/G/I/K=139-252.[ExPASy / RCSB / EBI]
2OT3; X-ray; 2.10 A; A=310-614.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1TXU; -.
2C7M; -.
2C7N; -.
2OT3; -.
SMR Q9UJ41; 152-211.
ModBase Q9UJ41.
Protein-protein interaction databases
IntAct Q9UJ41; -.
PTM databases
PhosphoSite Q9UJ41; -.
Organism-specific databases
H-InvDB HIX0006724; -.
HGNC HGNC:17676; RABGEF1.
GenAtlas RABGEF1.
MIM 609700; gene. [NCBI / EBI]
PharmGKB PA134946532; -.
GeneCards Q9UJ41.
Gene expression databases
ArrayExpress Q9UJ41; -.
CleanEx HS_RABGEF1; -.
GermOnline ENSG00000154710; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR003123; VPS9.
IPR013995; VPS9_sub.
IPR002653; Znf_A20.
Graphical view of domain structure.
Pfam PF02204; VPS9; 1.
PF01754; zf-A20; 1.
Pfam graphical view of domain structure.
SMART SM00167; VPS9; 1.
SM00259; ZnF_A20; 1.
SMART graphical view of domain structure.
PROSITE PS51205; VPS9; 1.
PS51036; ZF_A20; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9UJ41.
Genome annotation databases
Ensembl ENSG00000154710; Homo sapiens. [Contig view]
GeneID 27342; -.
KEGG hsa:27342; -.
Phylogenomic databases
HOGENOM Q9UJ41; -.
HOVERGEN Q9UJ41; -.
Other
LinkHub Q9UJ41; -.
SOURCE RABGEF1; Homo sapiens.
ProtoNet Q9UJ41.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Endocytosis; Endosome; Metal-binding; Phosphoprotein; Protein transport; Transport; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   708  708     Rab5 GDP/GTP exchange factor. PRO_0000191315
DOMAIN   449   592  144     VPS9. 
ZN_FING   151   185  35     A20-type. 
REGION   139   252  114     Interaction with ubiquitinated proteins. 
COILED   624   665  42     Potential. 
MOD_RES   310   310        Phosphoserine. 
VAR_SEQ   1   138        Missing (in isoform 2 and isoform 3). VSP_010690
VAR_SEQ   199   238        Missing (in isoform 2). VSP_010691
VAR_SEQ   377   415        Missing (in isoform 2 and isoform 3). VSP_010692
MUTAGEN   196   196        A->G: Reduces affinity for ubiquitin 3-fold. 
MUTAGEN   530   530        D->A: Strongly reduced activity. 
MUTAGEN   534   534        P->A: Strongly reduced activity. 
MUTAGEN   571   571        Y->A: Strongly reduced activity. 
MUTAGEN   574   574        T->A: Strongly reduced activity. 
CONFLICT   199   199        V -> A (in Ref. 2; ABA64474). 
CONFLICT   203   203        C -> Y (in Ref. 2; ABA64474). 
CONFLICT   476   476        E -> D (in Ref. 4; BAC87138). 
CONFLICT   487   487        K -> R (in Ref. 5; BAD97049). 
STRAND   162   164  3      
HELIX   167   169  3      
HELIX   174   198  25      
HELIX   313   325  13      
HELIX   328   347  20      
TURN   348   350  3      
HELIX   353   374  22      
TURN   418   420  3      
HELIX   421   440  20      
HELIX   448   460  13      
TURN   461   464  4      
TURN   467   471  5      
HELIX   479   494  16      
HELIX   495   497  3      
HELIX   501   523  23      
HELIX   529   531  3      
HELIX   532   543  12      
HELIX   548   558  11      
HELIX   561   563  3      
STRAND   565   567  3      
HELIX   568   584  17      
HELIX   589   591  3      
HELIX   595   603  9      
Sequence information
Length: 708 AA [This is the length of the unprocessed precursor] Molecular weight: 79371 Da [This is the MW of the unprocessed precursor] CRC64: 007E404F13AC91D8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVVVTGREPD SRRQDGAMSS SDAEDDFLEP ATPTATQAGH ALPLLPQERC AEFPALRGPP 

        70         80         90        100        110        120 
TQGACSSCVQ RGPVLCHRAP PGAAGEHAAT EGREGAPSVS GTHALLQRPL GADCGDRPAA 

       130        140        150        160        170        180 
CGPAEGPLCQ AQVVSRKKMS LKSERRGIHV DQSDLLCKKG CGYYGNPAWQ GFCSKCWREE 

       190        200        210        220        230        240 
YHKARQKQIQ EDWELAERVL LCCPGWSAMV QFQLTATSAS WAQVILLLQP PKWLGLQKLQ 

       250        260        270        280        290        300 
REEEEAFASS QSSQGAQSLT FSKFEEKKTN EKTRKVTTVK KFFSASSRVG SKKEIQEAKA 

       310        320        330        340        350        360 
PSPSINRQTS IETDRVSKEF IEFLKTFHKT GQEIYKQTKL FLEGMHYKRD LSIEEQSECA 

       370        380        390        400        410        420 
QDFYHNVAER MQTRGKERRF HHVGQAGLEL LTSGDPPASA SQSAGNTGVE PPHPAVPPER 

       430        440        450        460        470        480 
VEKIMDQIEK YIMTRLYKYV FCPETTDDEK KDLAIQKRIR ALRWVTPQML CVPVNEDIPE 

       490        500        510        520        530        540 
VSDMVVKAIT DIIEMDSKRV PRDKLACITK CSKHIFNAIK ITKNEPASAD DFLPTLIYIV 

       550        560        570        580        590        600 
LKGNPPRLQS NIQYITRFCN PSRLMTGEDG YYFTNLCCAV AFIEKLDAQS LNLSQEDFDR 

       610        620        630        640        650        660 
YMSGQTSPRK QEAESWSPDA CLGVKQMYKN LDLLSQLNER QERIMNEAKK LEKDLIDWTD 

       670        680        690        700 
GIAREVQDIV EKYPLEIKPP NQPLAAIDSE NVENDKLPPP LQPQVYAG 

Q9UJ41 in FASTA format

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