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Protein

Ras-related protein Rab-38

Gene

Rab38

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium (By similarity). May be involved in melanosomal transport and docking. Involved in the proper sorting of TYRP1. Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7 (PubMed:21187289).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 238GTPBy similarity
Nucleotide bindingi65 – 695GTPBy similarity
Nucleotide bindingi127 – 1304GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-38
Gene namesi
Name:Rab38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1919683. Rab38.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Rab38 are the cause of a form of oculocutaneous albinism known as the chocolate (cht) phenotype. Mice exhibit a brown coat similar in color to mice with a mutation in tyrosinase-related protein 1 (TYRP1). The targeting of TYRP1 protein to the melanosome is impaired in Rab38(cht)/Rab38(cht) melanocytes.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781V → A: Disrupts interaction with ANKRD27; inhibits peripheral distribution of TYRP1 in melanocytes. 1 Publication

Keywords - Diseasei

Albinism, Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Ras-related protein Rab-38PRO_0000121252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi205 – 2051S-palmitoyl cysteineSequence analysis
Lipidationi208 – 2081S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Palmitate, Prenylation

Proteomic databases

EPDiQ8QZZ8.
MaxQBiQ8QZZ8.
PaxDbiQ8QZZ8.
PRIDEiQ8QZZ8.

PTM databases

iPTMnetiQ8QZZ8.
PhosphoSiteiQ8QZZ8.

Expressioni

Gene expression databases

BgeeiQ8QZZ8.
CleanExiMM_RAB38.
ExpressionAtlasiQ8QZZ8. baseline and differential.
GenevisibleiQ8QZZ8. MM.

Interactioni

Subunit structurei

Interacts with ANKRD27 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Ankrd27Q3UMR05EBI-1993463,EBI-1993429

GO - Molecular functioni

Protein-protein interaction databases

BioGridi215371. 5 interactions.
DIPiDIP-46949N.
IntActiQ8QZZ8. 62 interactions.
STRINGi10090.ENSMUSP00000102877.

Structurei

3D structure databases

ProteinModelPortaliQ8QZZ8.
SMRiQ8QZZ8. Positions 6-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 469Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG4423. Eukaryota.
ENOG410YITC. LUCA.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ8QZZ8.
KOiK07923.
OMAiKRYVHHN.
OrthoDBiEOG78M02X.
PhylomeDBiQ8QZZ8.
TreeFamiTF324491.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8QZZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTPHKEHLY KLLVIGDLGV GKTSIIKRYV HQNFSSHYRA TIGVDFALKV
60 70 80 90 100
LHWDPETVVR LQLWDIAGQE RFGNMTRVYY REAMGAFIVF DVTRPATFEA
110 120 130 140 150
VAKWKNDLDS KLTLPNGKPV SVVLLANKCD QGKDVLMNNG LKMDQFCKEH
160 170 180 190 200
GFVGWFETSA KENINIDEAS RCLVKHILAN ECDLLESIEP DIVKPHLTSP
210
KVVSCSGCAK S
Length:211
Mass (Da):23,776
Last modified:June 1, 2002 - v1
Checksum:i61F84A88CDACC486
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1502EH → DD in BAB26198 (PubMed:16141072).Curated
Sequence conflicti161 – 1622KE → QR in BAB26198 (PubMed:16141072).Curated
Sequence conflicti173 – 1753LVK → RGQ in BAB26198 (PubMed:16141072).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191G → V in cht. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY062237 mRNA. Translation: AAL38663.1.
AF448443, AF448441, AF448442 Genomic DNA. Translation: AAM12528.1.
AK009296 mRNA. Translation: BAB26198.1.
AK044783 mRNA. Translation: BAC32089.1.
AK054253 mRNA. Translation: BAC35704.1.
CCDSiCCDS21439.1.
RefSeqiNP_082514.4. NM_028238.7.
UniGeneiMm.276669.

Genome annotation databases

EnsembliENSMUST00000107256; ENSMUSP00000102877; ENSMUSG00000030559.
GeneIDi72433.
KEGGimmu:72433.
UCSCiuc009ifv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY062237 mRNA. Translation: AAL38663.1.
AF448443, AF448441, AF448442 Genomic DNA. Translation: AAM12528.1.
AK009296 mRNA. Translation: BAB26198.1.
AK044783 mRNA. Translation: BAC32089.1.
AK054253 mRNA. Translation: BAC35704.1.
CCDSiCCDS21439.1.
RefSeqiNP_082514.4. NM_028238.7.
UniGeneiMm.276669.

3D structure databases

ProteinModelPortaliQ8QZZ8.
SMRiQ8QZZ8. Positions 6-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215371. 5 interactions.
DIPiDIP-46949N.
IntActiQ8QZZ8. 62 interactions.
STRINGi10090.ENSMUSP00000102877.

PTM databases

iPTMnetiQ8QZZ8.
PhosphoSiteiQ8QZZ8.

Proteomic databases

EPDiQ8QZZ8.
MaxQBiQ8QZZ8.
PaxDbiQ8QZZ8.
PRIDEiQ8QZZ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000107256; ENSMUSP00000102877; ENSMUSG00000030559.
GeneIDi72433.
KEGGimmu:72433.
UCSCiuc009ifv.1. mouse.

Organism-specific databases

CTDi23682.
MGIiMGI:1919683. Rab38.

Phylogenomic databases

eggNOGiKOG4423. Eukaryota.
ENOG410YITC. LUCA.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ8QZZ8.
KOiK07923.
OMAiKRYVHHN.
OrthoDBiEOG78M02X.
PhylomeDBiQ8QZZ8.
TreeFamiTF324491.

Miscellaneous databases

PROiQ8QZZ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8QZZ8.
CleanExiMM_RAB38.
ExpressionAtlasiQ8QZZ8. baseline and differential.
GenevisibleiQ8QZZ8. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT CHT VAL-19.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Ovary, Retina and Tongue.
  3. "Structure-function analysis of VPS9-ankyrin-repeat protein (Varp) in the trafficking of tyrosinase-related protein 1 in melanocytes."
    Tamura K., Ohbayashi N., Ishibashi K., Fukuda M.
    J. Biol. Chem. 286:7507-7521(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ANKRD27, MUTAGENESIS OF VAL-78.

Entry informationi

Entry nameiRAB38_MOUSE
AccessioniPrimary (citable) accession number: Q8QZZ8
Secondary accession number(s): Q9D7E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.