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Protein

Ras-related protein Rab-40A

Gene

RAB40A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 288GTPBy similarity
Nucleotide bindingi69 – 735GTPBy similarity
Nucleotide bindingi126 – 1294GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-40A
Alternative name(s):
SOCS box-containing protein RAR2A
Short name:
Protein Rar-2
Gene namesi
Name:RAB40A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:18283. RAB40A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34137.

Polymorphism and mutation databases

BioMutaiRAB40A.
DMDMi83287759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Ras-related protein Rab-40APRO_0000121257Add
BLAST
Propeptidei275 – 2773Removed in mature formSequence analysisPRO_0000370830

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi269 – 2691S-palmitoyl cysteineSequence analysis
Modified residuei274 – 2741Cysteine methyl esterSequence analysis
Lipidationi274 – 2741S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Palmitate, Prenylation

Proteomic databases

PaxDbiQ8WXH6.
PRIDEiQ8WXH6.

PTM databases

iPTMnetiQ8WXH6.
PhosphoSiteiQ8WXH6.

Expressioni

Gene expression databases

BgeeiQ8WXH6.
CleanExiHS_RAB40A.
GenevisibleiQ8WXH6. HS.

Interactioni

Protein-protein interaction databases

BioGridi126773. 12 interactions.
IntActiQ8WXH6. 2 interactions.
MINTiMINT-6941746.
STRINGi9606.ENSP00000305648.

Structurei

3D structure databases

ProteinModelPortaliQ8WXH6.
SMRiQ8WXH6. Positions 12-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini175 – 22854SOCS boxPROSITE-ProRule annotationAdd
BLAST

Domaini

The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes.By similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated
Contains 1 SOCS box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0078. Eukaryota.
ENOG410XPUI. LUCA.
GeneTreeiENSGT00840000129698.
HOGENOMiHOG000233967.
HOVERGENiHBG009351.
InParanoidiQ8WXH6.
KOiK07928.
OMAiLRHRMNW.
OrthoDBiEOG7XSTF5.
PhylomeDBiQ8WXH6.
TreeFamiTF323230.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR001496. SOCS_box.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
PF07525. SOCS_box. 1 hit.
[Graphical view]
SMARTiSM00253. SOCS. 1 hit.
SM00969. SOCS_box. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8WXH6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAPGSPDQA YDFLLKFLLV GDRDVGKSEI LESLQDGAAE SPYSHLGGID
60 70 80 90 100
YKTTTILLDG QRVKLKLWDT SGQGRFCTIF RSYSRGAQGV ILVYDIANRW
110 120 130 140 150
SFEGMDRWIK KIEEHAPGVP KILVGNRLHL AFKRQVPREQ AQAYAERLGV
160 170 180 190 200
TFFEVSPLCN FNIIESFTEL ARIVLLRHRM NWLGRPSKVL SLQDLCCRTI
210 220 230 240 250
VSCTPVHLVD KLPLPSTLRS HLKSFSMAKG LNARMMRGLS YSLTTSSTHK
260 270
SSLCKVEIVC PPQSPPKNCT RNSCKIS
Length:277
Mass (Da):31,076
Last modified:September 13, 2005 - v2
Checksum:iEB00BFF4E56A8577
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501K → KR in AAL60514 (Ref. 2) Curated
Sequence conflicti257 – 2571E → K in AAL60514 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451H → L.
Corresponds to variant rs1180895 [ dbSNP | Ensembl ].
VAR_034435

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132748 mRNA. Translation: AAL75949.1.
AF422143 mRNA. Translation: AAL60514.1.
AB232637 mRNA. Translation: BAF02899.1.
Z69733 Genomic DNA. Translation: CAI41993.1.
BC074854 mRNA. Translation: AAH74854.1.
BC074855 mRNA. Translation: AAH74855.1.
BC113501 mRNA. Translation: AAI13502.1.
BC117232 mRNA. Translation: AAI17233.1.
CCDSiCCDS35357.1.
RefSeqiNP_543155.2. NM_080879.2.
XP_005262140.1. XM_005262083.3.
XP_011529174.1. XM_011530872.1.
UniGeneiHs.706904.

Genome annotation databases

EnsembliENST00000304236; ENSP00000305648; ENSG00000172476.
ENST00000372633; ENSP00000361716; ENSG00000172476.
GeneIDi142684.
KEGGihsa:142684.
UCSCiuc004ekk.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132748 mRNA. Translation: AAL75949.1.
AF422143 mRNA. Translation: AAL60514.1.
AB232637 mRNA. Translation: BAF02899.1.
Z69733 Genomic DNA. Translation: CAI41993.1.
BC074854 mRNA. Translation: AAH74854.1.
BC074855 mRNA. Translation: AAH74855.1.
BC113501 mRNA. Translation: AAI13502.1.
BC117232 mRNA. Translation: AAI17233.1.
CCDSiCCDS35357.1.
RefSeqiNP_543155.2. NM_080879.2.
XP_005262140.1. XM_005262083.3.
XP_011529174.1. XM_011530872.1.
UniGeneiHs.706904.

3D structure databases

ProteinModelPortaliQ8WXH6.
SMRiQ8WXH6. Positions 12-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126773. 12 interactions.
IntActiQ8WXH6. 2 interactions.
MINTiMINT-6941746.
STRINGi9606.ENSP00000305648.

PTM databases

iPTMnetiQ8WXH6.
PhosphoSiteiQ8WXH6.

Polymorphism and mutation databases

BioMutaiRAB40A.
DMDMi83287759.

Proteomic databases

PaxDbiQ8WXH6.
PRIDEiQ8WXH6.

Protocols and materials databases

DNASUi142684.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304236; ENSP00000305648; ENSG00000172476.
ENST00000372633; ENSP00000361716; ENSG00000172476.
GeneIDi142684.
KEGGihsa:142684.
UCSCiuc004ekk.4. human.

Organism-specific databases

CTDi142684.
GeneCardsiRAB40A.
HGNCiHGNC:18283. RAB40A.
neXtProtiNX_Q8WXH6.
PharmGKBiPA34137.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0078. Eukaryota.
ENOG410XPUI. LUCA.
GeneTreeiENSGT00840000129698.
HOGENOMiHOG000233967.
HOVERGENiHBG009351.
InParanoidiQ8WXH6.
KOiK07928.
OMAiLRHRMNW.
OrthoDBiEOG7XSTF5.
PhylomeDBiQ8WXH6.
TreeFamiTF323230.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GeneWikiiRAB40A.
GenomeRNAii142684.
PROiQ8WXH6.

Gene expression databases

BgeeiQ8WXH6.
CleanExiHS_RAB40A.
GenevisibleiQ8WXH6. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR001496. SOCS_box.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
PF07525. SOCS_box. 1 hit.
[Graphical view]
SMARTiSM00253. SOCS. 1 hit.
SM00969. SOCS_box. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a new human cDNA homologous to Homo sapiens Rar protein."
    Zhou Y., Yu L., Zhao S.Y.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Kile B.T., Hilton D.J., Nicola N.A.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing proteins based on their Rab-binding activity."
    Itoh T., Satoh M., Kanno E., Fukuda M.
    Genes Cells 11:1023-1037(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain and Lung.

Entry informationi

Entry nameiRB40A_HUMAN
AccessioniPrimary (citable) accession number: Q8WXH6
Secondary accession number(s): O00407
, Q17RQ5, Q6DK06, Q8TF06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: September 13, 2005
Last modified: June 8, 2016
This is version 135 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.