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Q9UJ41

- RABX5_HUMAN

UniProt

Q9UJ41 - RABX5_HUMAN

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Protein

Rab5 GDP/GTP exchange factor

Gene

RABGEF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri151 – 18535A20-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. Rab GTPase binding Source: UniProtKB
  3. Rab guanyl-nucleotide exchange factor activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. positive regulation of Rab GTPase activity Source: GOC
  3. protein targeting to membrane Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Rab5 GDP/GTP exchange factor
Alternative name(s):
RAP1
Rabaptin-5-associated exchange factor for Rab5
Rabex-5
Gene namesi
Name:RABGEF1
Synonyms:RABEX5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:17676. RABGEF1.

Subcellular locationi

Cytoplasm 1 Publication. Early endosome 1 Publication. Recycling endosome 1 Publication

GO - Cellular componenti

  1. early endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961A → G: Reduces affinity for ubiquitin 3-fold. 1 Publication
Mutagenesisi530 – 5301D → A: Strongly reduced activity. 1 Publication
Mutagenesisi534 – 5341P → A: Strongly reduced activity. 1 Publication
Mutagenesisi571 – 5711Y → A: Strongly reduced activity. 1 Publication
Mutagenesisi574 – 5741T → A: Strongly reduced activity. 1 Publication

Organism-specific databases

PharmGKBiPA134946532.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 708708Rab5 GDP/GTP exchange factorPRO_0000191315Add
BLAST

Post-translational modificationi

Monoubiquitinated.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9UJ41.
PaxDbiQ9UJ41.
PRIDEiQ9UJ41.

PTM databases

PhosphoSiteiQ9UJ41.

Expressioni

Gene expression databases

CleanExiHS_RABGEF1.
ExpressionAtlasiQ9UJ41. baseline.
GenevestigatoriQ9UJ41.

Organism-specific databases

HPAiHPA001407.

Interactioni

Subunit structurei

Interacts with RGS14; the interaction is GTP-dependent By similarity. 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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005334EBI-913954,EBI-297353
KXD1Q9BQD32EBI-913954,EBI-739657
UBBP0CG476EBI-913954,EBI-413034
UBCP629902EBI-913954,EBI-413053From a different organism.

Protein-protein interaction databases

BioGridi118154. 27 interactions.
DIPiDIP-29348N.
IntActiQ9UJ41. 11 interactions.
MINTiMINT-1189235.
STRINGi9606.ENSP00000284957.

Structurei

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi161 – 1633Combined sources
Helixi167 – 1693Combined sources
Helixi174 – 19825Combined sources
Helixi239 – 24810Combined sources
Helixi318 – 3258Combined sources
Helixi328 – 34619Combined sources
Turni347 – 3504Combined sources
Helixi353 – 37220Combined sources
Helixi418 – 44023Combined sources
Helixi448 – 46114Combined sources
Turni462 – 4643Combined sources
Turni467 – 4715Combined sources
Helixi479 – 49416Combined sources
Helixi495 – 4973Combined sources
Helixi501 – 52323Combined sources
Helixi529 – 54315Combined sources
Helixi548 – 55811Combined sources
Turni561 – 5655Combined sources
Helixi568 – 58518Combined sources
Helixi589 – 5913Combined sources
Helixi595 – 6028Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXUX-ray2.35A311-611[»]
2C7MX-ray2.40A139-252[»]
2C7NX-ray2.10A/C/E/G/I/K139-252[»]
2OT3X-ray2.10A310-614[»]
4N3XX-ray2.00A/B/C/D626-672[»]
4N3YX-ray2.20A630-672[»]
4N3ZX-ray3.10A310-672[»]
4Q9UX-ray4.62A/E310-672[»]
ProteinModelPortaliQ9UJ41.
SMRiQ9UJ41. Positions 155-252, 312-604.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJ41.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini449 – 592144VPS9PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 252114Interaction with ubiquitinated proteinsAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili624 – 66542Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 A20-type zinc finger.PROSITE-ProRule annotation
Contains 1 VPS9 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri151 – 18535A20-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG301606.
GeneTreeiENSGT00530000063341.
HOGENOMiHOG000070180.
HOVERGENiHBG062584.
InParanoidiQ9UJ41.
PhylomeDBiQ9UJ41.
TreeFamiTF321331.

Family and domain databases

InterProiIPR003123. VPS9.
IPR013995. VPS9_subgr.
IPR002653. Znf_A20.
[Graphical view]
PfamiPF02204. VPS9. 1 hit.
PF01754. zf-A20. 1 hit.
[Graphical view]
SMARTiSM00167. VPS9. 1 hit.
SM00259. ZnF_A20. 1 hit.
[Graphical view]
PROSITEiPS51205. VPS9. 1 hit.
PS51036. ZF_A20. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UJ41-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVVVTGREPD SRRQDGAMSS SDAEDDFLEP ATPTATQAGH ALPLLPQERC
60 70 80 90 100
AEFPALRGPP TQGACSSCVQ RGPVLCHRAP PGAAGEHAAT EGREGAPSVS
110 120 130 140 150
GTHALLQRPL GADCGDRPAA CGPAEGPLCQ AQVVSRKKMS LKSERRGIHV
160 170 180 190 200
DQSDLLCKKG CGYYGNPAWQ GFCSKCWREE YHKARQKQIQ EDWELAERVL
210 220 230 240 250
LCCPGWSAMV QFQLTATSAS WAQVILLLQP PKWLGLQKLQ REEEEAFASS
260 270 280 290 300
QSSQGAQSLT FSKFEEKKTN EKTRKVTTVK KFFSASSRVG SKKEIQEAKA
310 320 330 340 350
PSPSINRQTS IETDRVSKEF IEFLKTFHKT GQEIYKQTKL FLEGMHYKRD
360 370 380 390 400
LSIEEQSECA QDFYHNVAER MQTRGKERRF HHVGQAGLEL LTSGDPPASA
410 420 430 440 450
SQSAGNTGVE PPHPAVPPER VEKIMDQIEK YIMTRLYKYV FCPETTDDEK
460 470 480 490 500
KDLAIQKRIR ALRWVTPQML CVPVNEDIPE VSDMVVKAIT DIIEMDSKRV
510 520 530 540 550
PRDKLACITK CSKHIFNAIK ITKNEPASAD DFLPTLIYIV LKGNPPRLQS
560 570 580 590 600
NIQYITRFCN PSRLMTGEDG YYFTNLCCAV AFIEKLDAQS LNLSQEDFDR
610 620 630 640 650
YMSGQTSPRK QEAESWSPDA CLGVKQMYKN LDLLSQLNER QERIMNEAKK
660 670 680 690 700
LEKDLIDWTD GIAREVQDIV EKYPLEIKPP NQPLAAIDSE NVENDKLPPP

LQPQVYAG

Note: No experimental confirmation available.

Length:708
Mass (Da):79,371
Last modified:July 5, 2004 - v2
Checksum:i007E404F13AC91D8
GO
Isoform 2 (identifier: Q9UJ41-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:491
Mass (Da):56,891
Checksum:i49ACABA276E65E91
GO
Isoform 3 (identifier: Q9UJ41-3) [UniParc]FASTAAdd to Basket

Also known as: Long

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

Show »
Length:531
Mass (Da):61,300
Checksum:i3C21934AA5ABBF9A
GO
Isoform 4 (identifier: Q9UJ41-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MVVVTGRE → MMASSYHE
     9-132: Missing.
     199-238: Missing.
     377-415: Missing.

Note: No experimental confirmation available.

Show »
Length:505
Mass (Da):58,526
Checksum:i655A49886ADE2891
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991V → A in ABA64474. 1 PublicationCurated
Sequence conflicti203 – 2031C → Y in ABA64474. 1 PublicationCurated
Sequence conflicti476 – 4761E → D in BAC87138. (PubMed:14702039)Curated
Sequence conflicti487 – 4871K → R in BAD97049. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 138138Missing in isoform 2 and isoform 3. 5 PublicationsVSP_010690Add
BLAST
Alternative sequencei1 – 88MVVVTGRE → MMASSYHE in isoform 4. 1 PublicationVSP_054643
Alternative sequencei9 – 132124Missing in isoform 4. 1 PublicationVSP_054644Add
BLAST
Alternative sequencei199 – 23840Missing in isoform 2 and isoform 4. 6 PublicationsVSP_010691Add
BLAST
Alternative sequencei377 – 41539Missing in isoform 2, isoform 3 and isoform 4. 6 PublicationsVSP_010692Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ250042 mRNA. Translation: CAB57359.1.
DQ230533 mRNA. Translation: ABA64473.1.
DQ230534 mRNA. Translation: ABA64474.1.
BT007107 mRNA. Translation: AAP35771.1.
AK127790 mRNA. Translation: BAC87138.1.
AK303006 mRNA. Translation: BAG64139.1.
AK223329 mRNA. Translation: BAD97049.1.
AC027644 Genomic DNA. Translation: AAQ93362.1.
AC079588 Genomic DNA. No translation available.
BC015330 mRNA. Translation: AAH15330.1.
CCDSiCCDS5535.1. [Q9UJ41-2]
CCDS69308.1. [Q9UJ41-4]
RefSeqiNP_001273989.1. NM_001287060.1.
NP_001273990.1. NM_001287061.1. [Q9UJ41-4]
NP_001273991.1. NM_001287062.1. [Q9UJ41-2]
NP_055319.1. NM_014504.2. [Q9UJ41-2]
UniGeneiHs.530053.
Hs.662268.
Hs.733181.

Genome annotation databases

EnsembliENST00000284957; ENSP00000284957; ENSG00000154710. [Q9UJ41-2]
ENST00000380828; ENSP00000370208; ENSG00000154710. [Q9UJ41-4]
ENST00000450873; ENSP00000415815; ENSG00000154710. [Q9UJ41-2]
GeneIDi27342.
KEGGihsa:27342.
UCSCiuc003tvf.3. human. [Q9UJ41-1]
uc003tvh.3. human. [Q9UJ41-2]

Polymorphism databases

DMDMi56405102.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ250042 mRNA. Translation: CAB57359.1 .
DQ230533 mRNA. Translation: ABA64473.1 .
DQ230534 mRNA. Translation: ABA64474.1 .
BT007107 mRNA. Translation: AAP35771.1 .
AK127790 mRNA. Translation: BAC87138.1 .
AK303006 mRNA. Translation: BAG64139.1 .
AK223329 mRNA. Translation: BAD97049.1 .
AC027644 Genomic DNA. Translation: AAQ93362.1 .
AC079588 Genomic DNA. No translation available.
BC015330 mRNA. Translation: AAH15330.1 .
CCDSi CCDS5535.1. [Q9UJ41-2 ]
CCDS69308.1. [Q9UJ41-4 ]
RefSeqi NP_001273989.1. NM_001287060.1.
NP_001273990.1. NM_001287061.1. [Q9UJ41-4 ]
NP_001273991.1. NM_001287062.1. [Q9UJ41-2 ]
NP_055319.1. NM_014504.2. [Q9UJ41-2 ]
UniGenei Hs.530053.
Hs.662268.
Hs.733181.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TXU X-ray 2.35 A 311-611 [» ]
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 [» ]
4N3X X-ray 2.00 A/B/C/D 626-672 [» ]
4N3Y X-ray 2.20 A 630-672 [» ]
4N3Z X-ray 3.10 A 310-672 [» ]
4Q9U X-ray 4.62 A/E 310-672 [» ]
ProteinModelPortali Q9UJ41.
SMRi Q9UJ41. Positions 155-252, 312-604.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118154. 27 interactions.
DIPi DIP-29348N.
IntActi Q9UJ41. 11 interactions.
MINTi MINT-1189235.
STRINGi 9606.ENSP00000284957.

PTM databases

PhosphoSitei Q9UJ41.

Polymorphism databases

DMDMi 56405102.

Proteomic databases

MaxQBi Q9UJ41.
PaxDbi Q9UJ41.
PRIDEi Q9UJ41.

Protocols and materials databases

DNASUi 27342.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284957 ; ENSP00000284957 ; ENSG00000154710 . [Q9UJ41-2 ]
ENST00000380828 ; ENSP00000370208 ; ENSG00000154710 . [Q9UJ41-4 ]
ENST00000450873 ; ENSP00000415815 ; ENSG00000154710 . [Q9UJ41-2 ]
GeneIDi 27342.
KEGGi hsa:27342.
UCSCi uc003tvf.3. human. [Q9UJ41-1 ]
uc003tvh.3. human. [Q9UJ41-2 ]

Organism-specific databases

CTDi 27342.
GeneCardsi GC07P066148.
HGNCi HGNC:17676. RABGEF1.
HPAi HPA001407.
MIMi 609700. gene.
neXtProti NX_Q9UJ41.
PharmGKBi PA134946532.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301606.
GeneTreei ENSGT00530000063341.
HOGENOMi HOG000070180.
HOVERGENi HBG062584.
InParanoidi Q9UJ41.
PhylomeDBi Q9UJ41.
TreeFami TF321331.

Miscellaneous databases

ChiTaRSi RABGEF1. human.
EvolutionaryTracei Q9UJ41.
GeneWikii RABGEF1.
GenomeRNAii 27342.
NextBioi 35476520.
PROi Q9UJ41.
SOURCEi Search...

Gene expression databases

CleanExi HS_RABGEF1.
ExpressionAtlasi Q9UJ41. baseline.
Genevestigatori Q9UJ41.

Family and domain databases

InterProi IPR003123. VPS9.
IPR013995. VPS9_subgr.
IPR002653. Znf_A20.
[Graphical view ]
Pfami PF02204. VPS9. 1 hit.
PF01754. zf-A20. 1 hit.
[Graphical view ]
SMARTi SM00167. VPS9. 1 hit.
SM00259. ZnF_A20. 1 hit.
[Graphical view ]
PROSITEi PS51205. VPS9. 1 hit.
PS51036. ZF_A20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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. "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).
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Brain and Testis.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, SUBCELLULAR LOCATION.
  11. "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] [Europe PMC] [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.
  12. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 139-252 IN COMPLEX WITH UBIQUITIN, UBIQUITINATION, MUTAGENESIS OF ALA-196.
  13. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 310-614 IN COMPLEX WITH RAB21.

Entry informationi

Entry nameiRABX5_HUMAN
AccessioniPrimary (citable) accession number: Q9UJ41
Secondary accession number(s): B4DZM7
, Q3HKR2, Q3HKR3, Q53FG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3