Q5JT25 (RAB41_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-41

Gene names

Name:

RAB41

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	222 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Sequence similarities	Belongs to the small GTPase superfamily. Rab family.
Sequence caution	The sequence CAI41489.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein 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
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5JT25-1)

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.

Isoform 2 (identifier: Q5JT25-2)

The sequence of this isoform differs from the canonical sequence as follows:
     42-42: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 222	222	Ras-related protein Rab-41		PRO_0000244618
Regions
	Nucleotide binding	38 – 45	8	GTP By similarity
	Nucleotide binding	86 – 90	5	GTP By similarity
	Nucleotide binding	144 – 147	4	GTP By similarity
	Motif	60 – 68	9	Effector region By similarity
Amino acid modifications
	Lipidation	222	1	S-geranylgeranyl cysteine By similarity
Natural variations
	Alternative sequence	42	1	Missing in isoform 2.		VSP_037051

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 91F90E1749A7C39E	FASTA	222	25,038
	10 20 30 40 50 60 MSAFGHDEAW MEAGGFGLEA AERTEYQSLC KSKLLFLGEQ SVGKTSIISR FMYNSFGCAC 70 80 90 100 110 120 QATVGIDFLS KTMYLEDQIV QLQLWDTAGQ ERFHSLIPSY IRDSTIAVVV YDITNINSFK 130 140 150 160 170 180 ETDKWVEHVR AERGDDVVIM LLGNKIDLDN KRQVTAEQGE EKSRNLNVMF IETSAKTGYN 190 200 210 220 VKKLFRRVAS ALLSTRTSPP PKEGTVEIEL ESFEESGNRS YC
	Isoform 2 [UniParc]. Checksum: 4D569A9FAD1586ED	FASTA	221	24,939
	10 20 30 40 50 60 MSAFGHDEAW MEAGGFGLEA AERTEYQSLC KSKLLFLGEQ SGKTSIISRF MYNSFGCACQ 70 80 90 100 110 120 ATVGIDFLSK TMYLEDQIVQ LQLWDTAGQE RFHSLIPSYI RDSTIAVVVY DITNINSFKE 130 140 150 160 170 180 TDKWVEHVRA ERGDDVVIML LGNKIDLDNK RQVTAEQGEE KSRNLNVMFI ETSAKTGYNV 190 200 210 220 KKLFRRVASA LLSTRTSPPP KEGTVEIELE SFEESGNRSY C

References

[1]

"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].

[2]

"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] (ISOFORM 2).

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL357752 Genomic DNA. Translation: CAI41489.1. Different initiation. BC117239 mRNA. Translation: AAI17240.1.
IPI	IPI00232898. IPI00929731.
RefSeq	NP_001027898.2. NM_001032726.2.
UniGene	Hs.276327.
3D structure databases
ProteinModelPortal	Q5JT25.
SMR	Q5JT25. Positions 33-193.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5JT25.
PTM databases
PhosphoSite	Q5JT25.
Polymorphism databases
DMDM	229462781.
Proteomic databases
PRIDE	Q5JT25.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374473; ENSP00000363597; ENSG00000147127.
GeneID	347517.
KEGG	hsa:347517.
UCSC	uc004dyc.1. human.
Organism-specific databases
CTD	347517.
GeneCards	GC0XP069502.
HGNC	HGNC:18293. RAB41.
HPA	HPA001510.
neXtProt	NX_Q5JT25.
PharmGKB	PA34140.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19534.
GeneTree	ENSGT00600000084341.
HOGENOM	HBG745225.
HOVERGEN	HBG009351.
InParanoid	Q5JT25.
OMA	FEESGNR.
PhylomeDB	Q5JT25.
Gene expression databases
Bgee	Q5JT25.
CleanEx	HS_RAB41.
Genevestigator	Q5JT25.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
KO	K07896.
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...

Entry information

Entry name

RAB41_HUMAN

Accession

Primary (citable) accession number: Q5JT25
Secondary accession number(s): Q17RQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	May 5, 2009
Last modified:	January 25, 2012
This is version 60 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.