Reviewed, UniProtKB/Swiss-Prot Q9UJ41 (RABX5_HUMAN)

Names and origin

Protein names

Recommended name:
    Rab5 GDP/GTP exchange factor
Alternative name(s):
    Rabex-5
    Rabaptin-5-associated exchange factor for Rab5
    RAP1

Gene names

Name:	RABGEF1
Synonyms:	RABEX5

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	708 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase By similarity. Ref.8 Ref.9 Ref.16
Subunit structure	Heterodimer with RABEP1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Interacts with RAB21, and with 100-fold lower affinity also with RAB22. Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2. Interacts with ubiquitinated EGFR. Ref.8 Ref.9 Ref.16 Ref.10
Subcellular location	Cytoplasm. Early endosome. Recycling endosome Ref.10.
Post-translational modification	Monoubiquitinated.
Sequence similarities	Contains 1 A20-type zinc finger. Contains 1 VPS9 domain.

Ontologies

Keywords
Biological process	Endocytosis Protein transport Transport Ubl conjugation pathway
Cellular component	Cytoplasm Endosome
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro protein binding Ref.17 Ref.18 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C19orf50	Q9BQD3	1	EBI-913954,EBI-739657
EGFR	P00533	2	EBI-913954,EBI-297353
RPS27A	P62988	2	EBI-913954,EBI-413034
RPS27A	P62990	2	EBI-913954,EBI-413053	From a different organism.
YWHAB	P31946	1	EBI-913954,EBI-359815
YWHAG	P61981	1	EBI-913954,EBI-359832

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UJ41-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q9UJ41-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
     199-238: Missing.
     377-415: Missing.

Isoform 3 (identifier: Q9UJ41-3)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
     377-415: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 708

708

Rab5 GDP/GTP exchange factor

PRO_0000191315

Regions

Domain

449 – 592

144

VPS9

Zinc finger

151 – 185

35

A20-type

Region

139 – 252

114

Interaction with ubiquitinated proteins

Coiled coil

624 – 665

42

Potential

Amino acid modifications

Modified residue

302

1

Phosphoserine Ref.12 Ref.13

Modified residue

310

1

Phosphoserine Ref.11

Modified residue

329

1

N6-acetyllysine Ref.15

Modified residue

348

1

N6-acetyllysine Ref.15

Modified residue

617

1

Phosphoserine Ref.14

Natural variations

Alternative sequence

1 – 138

138

Missing in isoform 2 and isoform 3.

VSP_010690

Alternative sequence

199 – 238

40

Missing in isoform 2.

VSP_010691

Alternative sequence

377 – 415

39

Missing in isoform 2 and isoform 3.

VSP_010692

Experimental info

Mutagenesis

196

1

A → G: Reduces affinity for ubiquitin 3-fold. Ref.17

Mutagenesis

530

1

D → A: Strongly reduced activity. Ref.16

Mutagenesis

534

1

P → A: Strongly reduced activity. Ref.16

Mutagenesis

571

1

Y → A: Strongly reduced activity. Ref.16

Mutagenesis

574

1

T → A: Strongly reduced activity. Ref.16

Sequence conflict

199

1

V → A in ABA64474. Ref.2

Sequence conflict

203

1

C → Y in ABA64474. Ref.2

Sequence conflict

476

1

E → D in BAC87138. Ref.3

Sequence conflict

487

1

K → R in BAD97049. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

708

Helix Strand Turn

Details...

Beta 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

Beta strand

565 – 567

3

Helix

568 – 584

17

Helix

589 – 591

3

Helix

595 – 603

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 2. Checksum: 007E404F13AC91D8	FASTA	708	79,371
	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
	Isoform 2. Checksum: 49ACABA276E65E91	FASTA	491	56,891
	10 20 30 40 50 60 MSLKSERRGI HVDQSDLLCK KGCGYYGNPA WQGFCSKCWR EEYHKARQKQ IQEDWELAER 70 80 90 100 110 120 LQREEEEAFA SSQSSQGAQS LTFSKFEEKK TNEKTRKVTT VKKFFSASSR VGSKKEIQEA 130 140 150 160 170 180 KAPSPSINRQ TSIETDRVSK EFIEFLKTFH KTGQEIYKQT KLFLEGMHYK RDLSIEEQSE 190 200 210 220 230 240 CAQDFYHNVA ERMQTRGKVP PERVEKIMDQ IEKYIMTRLY KYVFCPETTD DEKKDLAIQK 250 260 270 280 290 300 RIRALRWVTP QMLCVPVNED IPEVSDMVVK AITDIIEMDS KRVPRDKLAC ITKCSKHIFN 310 320 330 340 350 360 AIKITKNEPA SADDFLPTLI YIVLKGNPPR LQSNIQYITR FCNPSRLMTG EDGYYFTNLC 370 380 390 400 410 420 CAVAFIEKLD AQSLNLSQED FDRYMSGQTS PRKQEAESWS PDACLGVKQM YKNLDLLSQL 430 440 450 460 470 480 NERQERIMNE AKKLEKDLID WTDGIAREVQ DIVEKYPLEI KPPNQPLAAI DSENVENDKL 490 PPPLQPQVYA G
	Isoform 3 (Long). Checksum: 3C21934AA5ABBF9A	FASTA	531	61,300
	10 20 30 40 50 60 MSLKSERRGI HVDQSDLLCK KGCGYYGNPA WQGFCSKCWR EEYHKARQKQ IQEDWELAER 70 80 90 100 110 120 VLLCCPGWSA MVQFQLTATS ASWAQVILLL QPPKWLGLQK LQREEEEAFA SSQSSQGAQS 130 140 150 160 170 180 LTFSKFEEKK TNEKTRKVTT VKKFFSASSR VGSKKEIQEA KAPSPSINRQ TSIETDRVSK 190 200 210 220 230 240 EFIEFLKTFH KTGQEIYKQT KLFLEGMHYK RDLSIEEQSE CAQDFYHNVA ERMQTRGKVP 250 260 270 280 290 300 PERVEKIMDQ IEKYIMTRLY KYVFCPETTD DEKKDLAIQK RIRALRWVTP QMLCVPVNED 310 320 330 340 350 360 IPEVSDMVVK AITDIIEMDS KRVPRDKLAC ITKCSKHIFN AIKITKNEPA SADDFLPTLI 370 380 390 400 410 420 YIVLKGNPPR LQSNIQYITR FCNPSRLMTG EDGYYFTNLC CAVAFIEKLD AQSLNLSQED 430 440 450 460 470 480 FDRYMSGQTS PRKQEAESWS PDACLGVKQM YKNLDLLSQL NERQERIMNE AKKLEKDLID 490 500 510 520 530 WTDGIAREVQ DIVEKYPLEI KPPNQPLAAI DSENVENDKL PPPLQPQVYA G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Seven genes that are differentially transcribed in colorectal tumor cell lines." Nimmrich I., Erdmann S., Melchers U., Finke U., Hentsch S., Moyer M.P., Hoffmann I., Mueller O. Cancer Lett. 160:37-43(2000) [PubMed: 11098082] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	Barbieri M.A., Hunker C.M. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). Tissue: Cervix carcinoma.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[6]	"The DNA sequence of human chromosome 7." 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. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lymph.
[8]	"A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function." Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P., Stenmark H., Rybin V., Wilm M., Ashman K., Mann M., Zerial M. Cell 90:1149-1159(1997) [PubMed: 9323142] [Abstract] Cited for: FUNCTION, INTERACTION WITH RABEP1.
[9]	"Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex." Lippe R., Miaczynska M., Rybin V., Runge A., Zerial M. Mol. Biol. Cell 12:2219-2228(2001) [PubMed: 11452015] [Abstract] Cited for: FUNCTION, INTERACTION WITH RABEP1.
[10]	"Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex." Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S. EMBO J. 22:78-88(2003) [PubMed: 12505986] [Abstract] Cited for: INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, SUBCELLULAR LOCATION.
[11]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY. Tissue: Platelet.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, MASS SPECTROMETRY.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, MASS SPECTROMETRY.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, MASS SPECTROMETRY.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-329 AND LYS-348, MASS SPECTROMETRY.
[16]	"Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5." Delprato A., Merithew E., Lambright D.G. Cell 118:607-617(2004) [PubMed: 15339665] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 310-611, FUNCTION, INTERACTION WITH RAB5; RAB21 AND RAB22, MUTAGENESIS OF ASP-530; PRO-534; TYR-571 AND THR-574.
[17]	"Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin." Penengo L., Mapelli M., Murachelli A.G., Confalonieri S., Magri L., Musacchio A., Di Fiore P.P., Polo S., Schneider T.R. Cell 124:1183-1195(2006) [PubMed: 16499958] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 139-252 IN COMPLEX WITH UBIQUITIN, UBIQUITINATION, MUTAGENESIS OF ALA-196.
[18]	"Structural basis for Rab GTPase activation by VPS9 domain exchange factors." Delprato A., Lambright D.G. Nat. Struct. Mol. Biol. 14:406-412(2007) [PubMed: 17450153] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 310-614 IN COMPLEX WITH RAB21.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ250042 mRNA. Translation: CAB57359.1.
DQ230533 mRNA. Translation: ABA64473.1.
DQ230534 mRNA. Translation: ABA64474.1.
AK127790 mRNA. Translation: BAC87138.1.
BT007107 mRNA. Translation: AAP35771.1.
AK223329 mRNA. Translation: BAD97049.1.
AC027644 Genomic DNA. Translation: AAQ93362.1.
BC015330 mRNA. Translation: AAH15330.1.

IPI

IPI00418213.
IPI00816003.
IPI00924641.

RefSeq

NP_055319.1.

UniGene

Hs.530053

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TXU	X-ray	2.35	A	310-611	[»]
2C7M	X-ray	2.40	A	139-252	[»]
2C7N	X-ray	2.10	A/C/E/G/I/K	139-252	[»]
2OT3	X-ray	2.10	A	310-614	[»]

SMR

Q9UJ41. Positions 155-252.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29348N.

IntAct

Q9UJ41. 7 interactions.

STRING

Q9UJ41.

PTM databases

PhosphoSite

Q9UJ41.

Proteomic databases

PRIDE

Q9UJ41.

Genome annotation databases

Ensembl

ENST00000451741; ENSP00000398177; ENSG00000154710; Homo sapiens. [Genome view]

GeneID

27342.

KEGG

hsa:27342.

UCSC

uc003tvf.1. human.

Organism-specific databases

CTD

27342.

GeneCards

GC07P065843.

H-InvDB

HIX0006724.

HGNC

HGNC:17676. RABGEF1.

MIM

609700. gene.

PharmGKB

PA134946532.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG717649.

HOVERGEN

Q9UJ41.

Gene expression databases

ArrayExpress

Q9UJ41.

Bgee

Q9UJ41.

CleanEx

HS_RABGEF1.

Genevestigator

Q9UJ41.

GermOnline

ENSG00000154710. Homo sapiens.

Family and domain databases

InterPro

IPR003123. VPS9.
IPR013995. VPS9_sub.
IPR002653. Znf_A20.
[Graphical view]

Pfam

PF02204. VPS9. 1 hit.
PF01754. zf-A20. 1 hit.
[Graphical view]

SMART

SM00167. VPS9. 1 hit.
SM00259. ZnF_A20. 1 hit.
[Graphical view]

PROSITE

PS51205. VPS9. 1 hit.
PS51036. ZF_A20. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

50418.

SOURCE

Search...

Entry information

Entry name

RABX5_HUMAN

Accession

Primary (citable) accession number: Q9UJ41
Secondary accession number(s): Q3HKR2, Q3HKR3, Q53FG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.