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Protein

Rab5 GDP/GTP exchange factor

Gene

RABGEF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. ubiquitin-protein transferase activity Source: Ensembl
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. negative regulation of inflammatory response Source: Ensembl
  3. negative regulation of interleukin-6 secretion Source: Ensembl
  4. negative regulation of Kit signaling pathway Source: Ensembl
  5. negative regulation of leukocyte migration Source: Ensembl
  6. negative regulation of mast cell degranulation Source: Ensembl
  7. negative regulation of protein phosphorylation Source: Ensembl
  8. negative regulation of Ras protein signal transduction Source: Ensembl
  9. negative regulation of receptor-mediated endocytosis Source: Ensembl
  10. positive regulation of GTPase activity Source: GOC
  11. protein targeting to membrane Source: UniProtKB
  12. regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:17676. RABGEF1.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Early endosome 1 Publication
  3. Recycling endosome 1 Publication

GO - Cellular componenti

  1. early endosome Source: UniProtKB
  2. recycling endosome Source: UniProtKB-SubCell
  3. vesicle Source: Ensembl
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.

Polymorphism and mutation databases

BioMutaiRABGEF1.
DMDMi56405102.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei302 – 3021Phosphoserine1 Publication
Modified residuei310 – 3101Phosphoserine1 Publication
Modified residuei329 – 3291N6-acetyllysine1 Publication
Modified residuei348 – 3481N6-acetyllysine1 Publication
Modified residuei590 – 5901Phosphoserine1 Publication
Modified residuei594 – 5941Phosphoserine1 Publication

Post-translational modificationi

Monoubiquitinated.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UJ41.
PaxDbiQ9UJ41.
PRIDEiQ9UJ41.

PTM databases

PhosphoSiteiQ9UJ41.

Expressioni

Gene expression databases

CleanExiHS_RABGEF1.
ExpressionAtlasiQ9UJ41. baseline and differential.
GenevestigatoriQ9UJ41.

Organism-specific databases

HPAiCAB037056.
HPA001407.

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
BLOC1S6Q9UL453EBI-913954,EBI-465781
CIPCQ9C0C63EBI-913954,EBI-5654244
DAZAP2Q150383EBI-913954,EBI-724310
EGFRP005334EBI-913954,EBI-297353
KXD1Q9BQD32EBI-913954,EBI-739657
TEAD4D3DUQ63EBI-913954,EBI-10176734
THOC1Q96FV93EBI-913954,EBI-1765605
TRIM15Q9C0193EBI-913954,EBI-2342111
TRIM54Q9BYV23EBI-913954,EBI-2130429
TXN2Q997573EBI-913954,EBI-2932492
UBBP0CG476EBI-913954,EBI-413034
UBCP629902EBI-913954,EBI-413053From a different organism.
UBCQ96C323EBI-913954,EBI-745483
ZC2HC1CQ53FD03EBI-913954,EBI-740767

Protein-protein interaction databases

BioGridi118154. 37 interactions.
DIPiDIP-29348N.
IntActiQ9UJ41. 21 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
Helixi626 – 6327Combined sources
Helixi634 – 66936Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 312-672.
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.
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. AlignAdd to basket

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 (Ref. 2) Curated
Sequence conflicti203 – 2031C → Y in ABA64474 (Ref. 2) Curated
Sequence conflicti476 – 4761E → D in BAC87138 (PubMed:14702039).Curated
Sequence conflicti487 – 4871K → R in BAD97049 (Ref. 5) Curated

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:
EMBLi
GenBanki
DDBJi
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]
uc011kee.2. human.

Polymorphism and mutation databases

BioMutaiRABGEF1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 312-672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118154. 37 interactions.
DIPiDIP-29348N.
IntActiQ9UJ41. 21 interactions.
MINTiMINT-1189235.
STRINGi9606.ENSP00000284957.

PTM databases

PhosphoSiteiQ9UJ41.

Polymorphism and mutation databases

BioMutaiRABGEF1.
DMDMi56405102.

Proteomic databases

MaxQBiQ9UJ41.
PaxDbiQ9UJ41.
PRIDEiQ9UJ41.

Protocols and materials databases

DNASUi27342.
Structural Biology KnowledgebaseSearch...

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]
uc011kee.2. human.

Organism-specific databases

CTDi27342.
GeneCardsiGC07P066148.
HGNCiHGNC:17676. RABGEF1.
HPAiCAB037056.
HPA001407.
MIMi609700. gene.
neXtProtiNX_Q9UJ41.
PharmGKBiPA134946532.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiRABGEF1. human.
EvolutionaryTraceiQ9UJ41.
GeneWikiiRABGEF1.
GenomeRNAii27342.
NextBioi35476520.
PROiQ9UJ41.
SOURCEiSearch...

Gene expression databases

CleanExiHS_RABGEF1.
ExpressionAtlasiQ9UJ41. baseline and differential.
GenevestigatoriQ9UJ41.

Family and domain databases

InterProiIPR003123. VPS9.
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]
ProtoNetiSearch...

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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-329 AND LYS-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590 AND SER-594, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "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.
  19. "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.
  20. "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: April 29, 2015
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.