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Q9ULC3 (RAB23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-23
Gene names
Name:RAB23
ORF Names:HSPC137
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes. Ref.14 Ref.15

Subunit structure

Interacts with SUFU. Ref.15

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Cell membrane. Cytoplasm. Cytoplasmic vesicleautophagosome. Endosome membrane By similarity. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Recruited to phagosomes containing S.aureus or M.tuberculosis. Ref.13 Ref.15

Involvement in disease

Carpenter syndrome 1 (CRPT1) [MIM:201000]: A rare autosomal recessive disorder characterized by acrocephaly with variable synostosis of the sagittal, lambdoid, and coronal sutures; peculiar facies; brachydactyly of the hands with syndactyly; preaxial polydactyly and syndactyly of the feet; congenital heart defects; growth retardation; mental retardation; hypogenitalism; and obesity. In addition, cerebral malformations, oral and dental abnormalities, coxa valga, genu valgum, hydronephrosis, precocious puberty, and hearing loss may be observed.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Endosome
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCraniosynostosis
Disease mutation
   LigandGTP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
   PTMLipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.15. Source: UniProtKB

autophagic vacuole assembly

Inferred from mutant phenotype Ref.14. Source: UniProtKB

cellular defense response

Inferred from mutant phenotype Ref.14. Source: UniProtKB

craniofacial suture morphogenesis

Inferred from mutant phenotype Ref.16. Source: UniProtKB

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription factor import into nucleus

Inferred from mutant phenotype Ref.15. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

spinal cord dorsal/ventral patterning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentautophagic vacuole

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic vesicle

Inferred from direct assay Ref.13. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay Ref.15. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 234234Ras-related protein Rab-23
PRO_0000121211
Propeptide235 – 2373Removed in mature form Potential
PRO_0000370771

Regions

Nucleotide binding16 – 238GTP By similarity
Nucleotide binding64 – 685GTP By similarity
Nucleotide binding121 – 1244GTP By similarity
Motif38 – 469Effector region By similarity

Amino acid modifications

Modified residue2341Cysteine methyl ester Potential
Lipidation2341S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant121M → K in CRPT1. Ref.17
VAR_065294
Natural variant131Missing. Ref.16
VAR_034900
Natural variant401K → R. Ref.16
Corresponds to variant rs45442500 [ dbSNP | Ensembl ].
VAR_034901
Natural variant791Missing in CRPT1. Ref.17
VAR_065295
Natural variant851C → R in CRPT1. Ref.16
VAR_034902
Natural variant1011S → A. Ref.16
Corresponds to variant rs45479896 [ dbSNP | Ensembl ].
VAR_034903
Natural variant2071G → S. Ref.4 Ref.5
Corresponds to variant rs1040461 [ dbSNP | Ensembl ].
VAR_017159

Experimental info

Sequence conflict951E → G in AAF29101. Ref.3
Sequence conflict1441K → R in AAF29101. Ref.3
Sequence conflict2251K → N in AAF29101. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9ULC3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B9CB96E94DDF6036

FASTA23726,659
        10         20         30         40         50         60 
MLEEDMEVAI KMVVVGNGAV GKSSMIQRYC KGIFTKDYKK TIGVDFLERQ IQVNDEDVRL 

        70         80         90        100        110        120 
MLWDTAGQEE FDAITKAYYR GAQACVLVFS TTDRESFEAV SSWREKVVAE VGDIPTVLVQ 

       130        140        150        160        170        180 
NKIDLLDDSC IKNEEAEALA KRLKLRFYRT SVKEDLNVNE VFKYLAEKYL QKLKQQIAED 

       190        200        210        220        230 
PELTHSSSNK IGVFNTSGGS HSGQNSGTLN GGDVINLRPN KQRTKKNRNP FSSCSIP 

« Hide

References

« Hide 'large scale' references
[1]"Human mRNA for RAB23 protein."
Seki N., Yoshikawa T., Azuma T., Saito T., Muramatsu M.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"Expression of RAB-23 in human hair follicle."
Ikeda A., Yamashita M.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hair follicle.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-207.
[5]"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 (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-207.
Tissue: Brain.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon carcinoma.
[7]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Uterus.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: SUBCELLULAR LOCATION.
[14]"The small GTPases Rab9A and Rab23 function at distinct steps in autophagy during group A Streptococcus infection."
Nozawa T., Aikawa C., Goda A., Maruyama F., Hamada S., Nakagawa I.
Cell. Microbiol. 14:1149-1165(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Rab23 negatively regulates Gli1 transcriptional factor in a Su(Fu)-dependent manner."
Chi S., Xie G., Liu H., Chen K., Zhang X., Li C., Xie J.
Cell. Signal. 24:1222-1228(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUFU, FUNCTION, GTPASE ACTIVITY, SUBCELLULAR LOCATION.
[16]"RAB23 mutations in Carpenter syndrome imply an unexpected role for hedgehog signaling in cranial-suture development and obesity."
Jenkins D., Seelow D., Jehee F.S., Perlyn C.A., Alonso L.G., Bueno D.F., Donnai D., Josifiova D., Mathijssen I.M.J., Morton J.E.V., Orstavik K.H., Sweeney E., Wall S.A., Marsh J.L., Nuernberg P., Passos-Bueno M.R., Wilkie A.O.M.
Am. J. Hum. Genet. 80:1162-1170(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-13 DEL; ARG-40 AND ALA-101, VARIANT CRPT1 ARG-85.
[17]"Carpenter syndrome: extended RAB23 mutation spectrum and analysis of nonsense-mediated mRNA decay."
Jenkins D., Baynam G., De Catte L., Elcioglu N., Gabbett M.T., Hudgins L., Hurst J.A., Jehee F.S., Oley C., Wilkie A.O.
Hum. Mutat. 32:E2069-E2078(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRPT1 LYS-12 AND TYR-79 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB034244 mRNA. Translation: BAA87324.1.
AB025427 mRNA. Translation: BAB40309.1.
AF161486 mRNA. Translation: AAF29101.1.
AF498951 mRNA. Translation: AAM21099.1.
AK313796 mRNA. Translation: BAG36532.1.
AY585189 mRNA. Translation: AAT79492.1.
CR749371 mRNA. Translation: CAH18224.1.
AL031321 Genomic DNA. Translation: CAI21564.1.
CH471081 Genomic DNA. Translation: EAX04476.1.
BC015021 mRNA. Translation: AAH15021.1.
CCDSCCDS4962.1.
RefSeqNP_001265595.1. NM_001278666.1.
NP_001265596.1. NM_001278667.1.
NP_001265597.1. NM_001278668.1.
NP_057361.3. NM_016277.4.
NP_899050.1. NM_183227.2.
UniGeneHs.555016.

3D structure databases

ProteinModelPortalQ9ULC3.
SMRQ9ULC3. Positions 8-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119694. 3 interactions.
IntActQ9ULC3. 3 interactions.
MINTMINT-6783510.
STRING9606.ENSP00000320413.

PTM databases

PhosphoSiteQ9ULC3.

Polymorphism databases

DMDM12643897.

Proteomic databases

MaxQBQ9ULC3.
PaxDbQ9ULC3.
PRIDEQ9ULC3.

Protocols and materials databases

DNASU51715.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317483; ENSP00000320413; ENSG00000112210.
ENST00000468148; ENSP00000417610; ENSG00000112210.
GeneID51715.
KEGGhsa:51715.
UCSCuc003pds.3. human.

Organism-specific databases

CTD51715.
GeneCardsGC06M057100.
HGNCHGNC:14263. RAB23.
HPAHPA029135.
HPA029136.
MIM201000. phenotype.
606144. gene.
neXtProtNX_Q9ULC3.
Orphanet65759. Carpenter syndrome.
PharmGKBPA34113.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG100144.
InParanoidQ9ULC3.
KOK06234.
OMAVTEVFKY.
OrthoDBEOG72C51B.
PhylomeDBQ9ULC3.
TreeFamTF317494.

Enzyme and pathway databases

SignaLinkQ9ULC3.

Gene expression databases

BgeeQ9ULC3.
CleanExHS_RAB23.
GenevestigatorQ9ULC3.

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

GeneWikiRAB23.
GenomeRNAi51715.
NextBio55759.
PROQ9ULC3.
SOURCESearch...

Entry information

Entry nameRAB23_HUMAN
AccessionPrimary (citable) accession number: Q9ULC3
Secondary accession number(s): B2R9I5 expand/collapse secondary AC list , Q68DJ6, Q8NI06, Q9P023
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 136 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 6

Human chromosome 6: entries, gene names and cross-references to MIM