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Protein

Ras-related protein Rab-43

Gene

RAB43

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. The low intrinsic GTPase activity of RAB43 is activated by USP6NL. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for the structural integrity of the Golgi complex. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi25 – 328GTP
Nucleotide bindingi73 – 775GTPBy similarity
Nucleotide bindingi131 – 1344GTP
Nucleotide bindingi163 – 1642GTP

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • Golgi organization Source: UniProtKB
  • intracellular protein transport Source: GO_Central
  • metabolic process Source: GOC
  • phagosome maturation Source: UniProtKB
  • Rab protein signal transduction Source: GO_Central
  • retrograde transport, plasma membrane to Golgi Source: UniProtKB
  • virion assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-43
Alternative name(s):
Ras-related protein Rab-41
Gene namesi
Name:RAB43
Synonyms:RAB41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:19983. RAB43.

Subcellular locationi

GO - Cellular componenti

  • endosome Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • phagocytic vesicle Source: UniProtKB
  • phagocytic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321T → N: Abolishes activity. Disrupts Golgi structure. 2 Publications

Organism-specific databases

PharmGKBiPA134968262.

Polymorphism and mutation databases

BioMutaiRAB43.
DMDMi74727944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Ras-related protein Rab-43PRO_0000244615Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei193 – 1931Phosphoserine2 Publications
Lipidationi210 – 2101S-geranylgeranyl cysteineBy similarity
Modified residuei212 – 2121Cysteine methyl esterBy similarity
Lipidationi212 – 2121S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ86YS6.
PaxDbiQ86YS6.
PRIDEiQ86YS6.

PTM databases

PhosphoSiteiQ86YS6.

Expressioni

Tissue specificityi

Widely expressed in brain, testis, lung, heart, ovary, colon, kidney, uterus and spleen but not in liver.1 Publication

Gene expression databases

BgeeiQ86YS6.
CleanExiHS_RAB41.
HS_RAB43.
ExpressionAtlasiQ86YS6. baseline.
GenevisibleiQ86YS6. HS.

Organism-specific databases

HPAiHPA046840.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPB1P047922EBI-4401730,EBI-352682

Protein-protein interaction databases

BioGridi130830. 2 interactions.
IntActiQ86YS6. 1 interaction.
STRINGi9606.ENSP00000319781.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 259Combined sources
Helixi31 – 4010Combined sources
Beta strandi55 – 628Combined sources
Beta strandi65 – 728Combined sources
Helixi78 – 803Combined sources
Helixi81 – 888Combined sources
Beta strandi92 – 998Combined sources
Helixi103 – 1075Combined sources
Helixi109 – 11911Combined sources
Beta strandi125 – 1317Combined sources
Helixi136 – 1383Combined sources
Helixi143 – 15210Combined sources
Beta strandi156 – 1605Combined sources
Turni163 – 1664Combined sources
Helixi169 – 18315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUPX-ray2.05A/B9-190[»]
ProteinModelPortaliQ86YS6.
SMRiQ86YS6. Positions 15-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86YS6.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi47 – 559Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ86YS6.
KOiK07930.
OMAiYRSANRA.
OrthoDBiEOG7NGQCK.
PhylomeDBiQ86YS6.
TreeFamiTF300097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86YS6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGPGPGPGD PDEQYDFLFK LVLVGDASVG KTCVVQRFKT GAFSERQGST
60 70 80 90 100
IGVDFTMKTL EIQGKRVKLQ IWDTAGQERF RTITQSYYRS ANGAILAYDI
110 120 130 140 150
TKRSSFLSVP HWIEDVRKYA GSNIVQLLIG NKSDLSELRE VSLAEAQSLA
160 170 180 190 200
EHYDILCAIE TSAKDSSNVE EAFLRVATEL IMRHGGPLFS EKSPDHIQLN
210
SKDIGEGWGC GC
Length:212
Mass (Da):23,339
Last modified:June 1, 2003 - v1
Checksum:i087EE3802B7159C9
GO
Isoform 2 (identifier: Q9ULR0-1) [UniParc]FASTAAdd to basket

Also known as: ISY1-RAB43

The sequence of this isoform can be found in the external entry Q9ULR0.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Based on a readthrough transcript which may produce a ISY1-RAB43 fusion protein. No experimental confirmation available.
Length:331
Mass (Da):37,567
GO
Isoform 3 (identifier: Q86YS6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     130-155: GNKSDLSELREVSLAEAQSLAEHYDI → EMQSCYVAQADLELLASSNPPASTSK
     156-212: Missing.

Note: Gene prediction based on EST data. No experimental confirmation available.
Show »
Length:155
Mass (Da):17,074
Checksum:iCC4EA3C8FD5E005D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei130 – 15526GNKSD…EHYDI → EMQSCYVAQADLELLASSNP PASTSK in isoform 3. CuratedVSP_054030Add
BLAST
Alternative sequencei156 – 21257Missing in isoform 3. CuratedVSP_054031Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY166852 mRNA. Translation: AAO17291.1.
AK291014 mRNA. Translation: BAF83703.1.
AC108673 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79283.1.
BC062319 mRNA. Translation: AAH62319.1.
CCDSiCCDS33850.1. [Q86YS6-1]
CCDS56275.1. [Q86YS6-2]
RefSeqiNP_001191812.1. NM_001204883.1. [Q86YS6-1]
NP_001191813.1. NM_001204884.1. [Q86YS6-1]
NP_001191814.1. NM_001204885.1. [Q86YS6-1]
NP_001191815.1. NM_001204886.1. [Q86YS6-1]
NP_001191816.1. NM_001204887.1. [Q86YS6-2]
NP_940892.1. NM_198490.2. [Q86YS6-1]
UniGeneiHs.381132.
Hs.512661.
Hs.546542.

Genome annotation databases

EnsembliENST00000315150; ENSP00000319781; ENSG00000172780. [Q86YS6-1]
ENST00000393304; ENSP00000376981; ENSG00000172780. [Q86YS6-1]
ENST00000393305; ENSP00000376982; ENSG00000172780. [Q86YS6-1]
ENST00000393307; ENSP00000376984; ENSG00000172780. [Q86YS6-1]
ENST00000393308; ENSP00000376985; ENSG00000172780. [Q86YS6-1]
ENST00000476465; ENSP00000427632; ENSG00000172780. [Q86YS6-2]
ENST00000615093; ENSP00000481399; ENSG00000172780. [Q86YS6-2]
GeneIDi339122.
KEGGihsa:339122.
UCSCiuc003eln.2. human. [Q86YS6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY166852 mRNA. Translation: AAO17291.1.
AK291014 mRNA. Translation: BAF83703.1.
AC108673 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79283.1.
BC062319 mRNA. Translation: AAH62319.1.
CCDSiCCDS33850.1. [Q86YS6-1]
CCDS56275.1. [Q86YS6-2]
RefSeqiNP_001191812.1. NM_001204883.1. [Q86YS6-1]
NP_001191813.1. NM_001204884.1. [Q86YS6-1]
NP_001191814.1. NM_001204885.1. [Q86YS6-1]
NP_001191815.1. NM_001204886.1. [Q86YS6-1]
NP_001191816.1. NM_001204887.1. [Q86YS6-2]
NP_940892.1. NM_198490.2. [Q86YS6-1]
UniGeneiHs.381132.
Hs.512661.
Hs.546542.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUPX-ray2.05A/B9-190[»]
ProteinModelPortaliQ86YS6.
SMRiQ86YS6. Positions 15-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130830. 2 interactions.
IntActiQ86YS6. 1 interaction.
STRINGi9606.ENSP00000319781.

PTM databases

PhosphoSiteiQ86YS6.

Polymorphism and mutation databases

BioMutaiRAB43.
DMDMi74727944.

Proteomic databases

MaxQBiQ86YS6.
PaxDbiQ86YS6.
PRIDEiQ86YS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315150; ENSP00000319781; ENSG00000172780. [Q86YS6-1]
ENST00000393304; ENSP00000376981; ENSG00000172780. [Q86YS6-1]
ENST00000393305; ENSP00000376982; ENSG00000172780. [Q86YS6-1]
ENST00000393307; ENSP00000376984; ENSG00000172780. [Q86YS6-1]
ENST00000393308; ENSP00000376985; ENSG00000172780. [Q86YS6-1]
ENST00000476465; ENSP00000427632; ENSG00000172780. [Q86YS6-2]
ENST00000615093; ENSP00000481399; ENSG00000172780. [Q86YS6-2]
GeneIDi339122.
KEGGihsa:339122.
UCSCiuc003eln.2. human. [Q86YS6-1]

Organism-specific databases

CTDi339122.
GeneCardsiGC03M128806.
HGNCiHGNC:19983. RAB43.
HPAiHPA046840.
neXtProtiNX_Q86YS6.
PharmGKBiPA134968262.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118841.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ86YS6.
KOiK07930.
OMAiYRSANRA.
OrthoDBiEOG7NGQCK.
PhylomeDBiQ86YS6.
TreeFamiTF300097.

Miscellaneous databases

EvolutionaryTraceiQ86YS6.
GenomeRNAii339122.
NextBioi97235.
PROiQ86YS6.

Gene expression databases

BgeeiQ86YS6.
CleanExiHS_RAB41.
HS_RAB43.
ExpressionAtlasiQ86YS6. baseline.
GenevisibleiQ86YS6. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 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. "Isolation, expression pattern of a novel human RAB gene RAB41 and characterization of its intronless homolog RAB41P."
    Guo J.H., Chen L., Chen S., Liu X., Saiyin H., Deng Q., Zhuang Y., Wan B., Yu L., Zhao S.Y.
    DNA Seq. 14:431-435(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Eye.
  6. "Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways."
    Fuchs E., Haas A.K., Spooner R.A., Yoshimura S., Lord J.M., Barr F.A.
    J. Cell Biol. 177:1133-1143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells."
    Haas A.K., Yoshimura S., Stephens D.J., Preisinger C., Fuchs E., Barr F.A.
    J. Cell Sci. 120:2997-3010(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF THR-32.
  8. Cited for: FUNCTION, MUTAGENESIS OF THR-32, SUBCELLULAR LOCATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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.
  13. "Crystal structure of human RAB43 in complex with GDP."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-190 IN COMPLEX WITH GDP.

Entry informationi

Entry nameiRAB43_HUMAN
AccessioniPrimary (citable) accession number: Q86YS6
Secondary accession number(s): A8K4P9, E9PBQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.