Q9UL26 (RB22A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-22A
Short name=Rab-22

Gene names

Name:	RAB22A
Synonyms:	RAB22

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	194 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Interacts directly with ZFYVE20 By similarity. Binds EEA1 By similarity.
Subcellular location	Endosome membrane; Lipid-anchor By similarity. Cell membrane; Lipid-anchor By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Endosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from direct assay. Source: UniProtKB endosome organization Inferred from expression pattern. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	early endosome Inferred from direct assay. Source: UniProtKB endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EEA1	Q15075	3	EBI-399456,EBI-298113

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 194	194	Ras-related protein Rab-22A		PRO_0000121209
Regions
	Nucleotide binding	12 – 20	9	GTP By similarity
	Nucleotide binding	60 – 64	5	GTP By similarity
	Nucleotide binding	118 – 121	4	GTP By similarity
	Nucleotide binding	148 – 150	3	GTP By similarity
	Motif	34 – 42	9	Effector region By similarity
Amino acid modifications
	Modified residue	101	1	N6-acetyllysine Ref.9
	Lipidation	193	1	S-geranylgeranyl cysteine By similarity
	Lipidation	194	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Sequence conflict	184	1	R → K in CAC10538. Ref.3
	Sequence conflict	192 – 193	2	SC → TA in AAL75941. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UL26 [UniParc]. Last modified March 1, 2001. Version 2. Checksum: EBC84711DA3F839B	FASTA	194	21,855
	10 20 30 40 50 60 MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ NELHKFLIWD 70 80 90 100 110 120 TAGQERFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV KELRQHGPPN IVVAIAGNKC 130 140 150 160 170 180 DLIDVREVME RDAKDYADSI HAIFVETSAK NAININELFI EISRRIPSTD ANLPSGGKGF 190 KLRRQPSEPK RSCC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a novel human cDNA similar to Canis familiaris mRNA for Rab22 protein." Ding J.B., Yu L., Zhao S.Y. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is an apically located GTP-binding protein in polarised intestinal epithelial cells." Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A., Fransen J.A.M. Eur. J. Cell Biol. 79:308-316(2000) [PubMed: 10887961] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon carcinoma.
[3]	"Mapping and characterization of the human RAB22A gene." Kussmann S., Hansmann I., Schlote D. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[5]	"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]. Tissue: Tongue.
[6]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: Colon and Uterus.
[9]	"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-101, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF125104 mRNA. Translation: AAL75941.1. AF091034 mRNA. Translation: AAF00047.2. AJ276210 mRNA. Translation: CAC10538.1. BT007046 mRNA. Translation: AAP35695.1. AK091180 mRNA. Translation: BAG52298.1. AL035455 Genomic DNA. Translation: CAC15020.1. CH471077 Genomic DNA. Translation: EAW75496.1. CH471077 Genomic DNA. Translation: EAW75497.1. BC015710 mRNA. Translation: AAH15710.1. BC063457 mRNA. Translation: AAH63457.1.
IPI	IPI00007756.
RefSeq	NP_065724.1. NM_020673.2.
UniGene	Hs.529044.
3D structure databases
ProteinModelPortal	Q9UL26.
SMR	Q9UL26. Positions 2-167.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UL26. 3 interactions.
MINT	MINT-5003659.
STRING	Q9UL26.
PTM databases
PhosphoSite	Q9UL26.
Polymorphism databases
DMDM	13633614.
Proteomic databases
PRIDE	Q9UL26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000244040; ENSP00000244040; ENSG00000124209.
GeneID	57403.
KEGG	hsa:57403.
UCSC	uc002xyz.1. human.
Organism-specific databases
CTD	57403.
GeneCards	GC20P056884.
H-InvDB	HIX0015948.
HGNC	HGNC:9764. RAB22A.
MIM	612966. gene.
neXtProt	NX_Q9UL26.
PharmGKB	PA34112.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12908.
GeneTree	ENSGT00550000074186.
HOGENOM	HBG745225.
HOVERGEN	HBG009351.
InParanoid	Q9UL26.
OMA	TDTNPPS.
OrthoDB	EOG4CRM14.
PhylomeDB	Q9UL26.
Gene expression databases
ArrayExpress	Q9UL26.
Bgee	Q9UL26.
CleanEx	HS_RAB22A.
Genevestigator	Q9UL26.
GermOnline	ENSG00000124209. Homo sapiens.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
KO	K07891.
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	63508.
SOURCE	Search...

Entry information

Entry name

RB22A_HUMAN

Accession

Primary (citable) accession number: Q9UL26
Secondary accession number(s): B3KR86 , E1P605, Q8TF12, Q9H4E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 101 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.