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P57729 (RAB38_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-38
Alternative name(s):
Melanoma antigen NY-MEL-1
Gene names
Name:RAB38
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in melanosomal transport and docking. Involved in the proper sorting of TYRP1. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Ref.9

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Melanosome. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.5 Ref.6 Ref.9

Tissue specificity

Expressed in melanocytes.

Post-translational modification

Although at least one in vitro system can process and methylate the prenylated C-terminal, in an in vitro system that normally express Rab-38 and in vivo the prenylated C-terminal is not proteolytically processed and not methylated.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Ras-related protein Rab-38
PRO_0000121251

Regions

Nucleotide binding16 – 238GTP By similarity
Nucleotide binding65 – 695GTP By similarity
Nucleotide binding127 – 1304GTP By similarity
Motif38 – 469Effector region By similarity

Sites

Site2081Not methylated

Amino acid modifications

Lipidation2051S-palmitoyl cysteine Potential
Lipidation2081S-geranylgeranyl cysteine Probable

Natural variations

Natural variant1111K → T in a colorectal cancer sample; somatic mutation. Ref.10
VAR_036415

Sequences

Sequence LengthMass (Da)Tools
P57729 [UniParc].

Last modified January 11, 2001. Version 1.
Checksum: 0D16B42A1B237539

FASTA21123,712
        10         20         30         40         50         60 
MQAPHKEHLY KLLVIGDLGV GKTSIIKRYV HQNFSSHYRA TIGVDFALKV LHWDPETVVR 

        70         80         90        100        110        120 
LQLWDIAGQE RFGNMTRVYY REAMGAFIVF DVTRPATFEA VAKWKNDLDS KLSLPNGKPV 

       130        140        150        160        170        180 
SVVLLANKCD QGKDVLMNNG LKMDQFCKEH GFVGWFETSA KENINIDEAS RCLVKHILAN 

       190        200        210 
ECDLMESIEP DVVKPHLTST KVASCSGCAK S 

« Hide

References

« Hide 'large scale' references
[1]"Serological cloning of a melanocyte rab guanosine 5'-triphosphate-binding protein and a chromosome condensation protein from a melanoma complementary DNA library."
Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A., Old L.J., Chen Y.-T.
Cancer Res. 60:3584-3591(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]SeattleSNPs variation discovery resource
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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: Skin.
[5]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[6]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[7]"Rab GTPases containing a CAAX motif are processed post-geranylgeranylation by proteolysis and methylation."
Leung K.F., Baron R., Ali B.R., Magee A.I., Seabra M.C.
J. Biol. Chem. 282:1487-1497(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-208.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
Seto S., Tsujimura K., Koide Y.
Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-111.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF235022 mRNA. Translation: AAG30731.1.
BT009842 mRNA. Translation: AAP88844.1.
DQ178619 Genomic DNA. Translation: ABA03166.1.
BC015808 mRNA. Translation: AAH15808.1.
RefSeqNP_071732.1. NM_022337.2.
UniGeneHs.591975.

3D structure databases

ProteinModelPortalP57729.
SMRP57729. Positions 7-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117198. 2 interactions.
DIPDIP-60520N.
STRING9606.ENSP00000243662.

PTM databases

PhosphoSiteP57729.

Polymorphism databases

DMDM12230516.

Proteomic databases

PaxDbP57729.
PRIDEP57729.

Protocols and materials databases

DNASU23682.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243662; ENSP00000243662; ENSG00000123892.
GeneID23682.
KEGGhsa:23682.
UCSCuc001pcj.2. human.

Organism-specific databases

CTD23682.
GeneCardsGC11M087846.
HGNCHGNC:9776. RAB38.
MIM606281. gene.
neXtProtNX_P57729.
PharmGKBPA34129.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP57729.
KOK07923.
OMAPNYRATI.
OrthoDBEOG78M02X.
PhylomeDBP57729.
TreeFamTF324491.

Gene expression databases

BgeeP57729.
CleanExHS_RAB38.
GenevestigatorP57729.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAB38.
GenomeRNAi23682.
NextBio46557.
PROP57729.
SOURCESearch...

Entry information

Entry nameRAB38_HUMAN
AccessionPrimary (citable) accession number: P57729
Secondary accession number(s): Q53XK7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM