Q14088 (RB33A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-33A

Alternative name(s):
Small GTP-binding protein S10

Gene names

Name:	RAB33A
Synonyms:	RABS10

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
Tissue specificity	Expressed only in lymphoid cell lines.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RABAC1	Q9UI14	3	EBI-744685,EBI-712367

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 237	237	Ras-related protein Rab-33A		PRO_0000121237
Regions
	Nucleotide binding	43 – 50	8	GTP By similarity
	Nucleotide binding	91 – 95	5	GTP By similarity
	Nucleotide binding	151 – 154	4	GTP By similarity
Amino acid modifications
	Modified residue	237	1	Cysteine methyl ester By similarity
	Lipidation	235	1	S-geranylgeranyl cysteine By similarity
	Lipidation	237	1	S-geranylgeranyl cysteine By similarity
Natural variations
	Natural variant	102	1	M → T.		VAR_006849

Sequences

	Sequence		Length	Mass (Da)
	Q14088 [UniParc]. Last modified May 1, 1997. Version 2. Checksum: 2EE23B8237225F4A	FASTA	237	26,593
	10 20 30 40 50 60 MAQPILGHGS LQPASAAGLA SLELDSSLDQ YVQIRIFKII VIGDSNVGKT CLTFRFCGGT 70 80 90 100 110 120 FPDKTEATIG VDFREKTVEI EGEKIKVQVW DTAGQERFRK SMVEHYYRNV HAVVFVYDVT 130 140 150 160 170 180 KMTSFTNLKM WIQECNGHAV PPLVPKVLVG NKCDLREQIQ VPSNLALKFA DAHNMLLFET 190 200 210 220 230 SAKDPKESQN VESIFMCLAC RLKAQKSLLY RDAERQQGKV QKLEFPQEAN SKTSCPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a cDNA encoding a novel small GTP-binding protein." Koda T., Kakinuma M. FEBS Lett. 328:21-24(1993) [PubMed: 7688322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[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].
[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: 15772651] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D14889 mRNA. Translation: BAA03606.1. AF498959 mRNA. Translation: AAM21107.1. BT007038 mRNA. Translation: AAP35687.1. AL139234 Genomic DNA. Translation: CAI42781.1. BC001157 mRNA. Translation: AAH01157.1. BC009996 mRNA. Translation: AAH09996.1.
IPI	IPI00028517.
PIR	S35058.
RefSeq	NP_004785.1. NM_004794.2.
UniGene	Hs.654356.
3D structure databases
ProteinModelPortal	Q14088.
SMR	Q14088. Positions 35-199.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14088. 3 interactions.
MINT	MINT-1455156.
STRING	Q14088.
PTM databases
PhosphoSite	Q14088.
Polymorphism databases
DMDM	2500071.
Proteomic databases
PRIDE	Q14088.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000257017; ENSP00000257017; ENSG00000134594.
GeneID	9363.
KEGG	hsa:9363.
UCSC	uc004evl.1. human.
Organism-specific databases
CTD	9363.
GeneCards	GC0XP129305.
H-InvDB	HIX0017045.
HGNC	HGNC:9773. RAB33A.
MIM	300333. gene.
neXtProt	NX_Q14088.
PharmGKB	PA34124.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08982.
GeneTree	ENSGT00600000084223.
HOGENOM	HBG745225.
HOVERGEN	HBG009351.
InParanoid	Q14088.
OMA	TWIEECN.
OrthoDB	EOG4WH8MS.
PhylomeDB	Q14088.
Gene expression databases
ArrayExpress	Q14088.
Bgee	Q14088.
CleanEx	HS_RAB33A.
Genevestigator	Q14088.
GermOnline	ENSG00000134594. Homo sapiens.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
KO	K07919.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00175. RAB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35063.
SOURCE	Search...

Entry information

Entry name

RB33A_HUMAN

Accession

Primary (citable) accession number: Q14088
Secondary accession number(s): Q5JUZ6, Q92465

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.