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P20338

- RAB4A_HUMAN

UniProt

P20338 - RAB4A_HUMAN

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Protein

Ras-related protein Rab-4A

Gene

RAB4A

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

Functioni

Protein transport. Probably involved in vesicular traffic By similarity.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289GTP1 Publication
Nucleotide bindingi68 – 725GTP1 Publication
Nucleotide bindingi126 – 1294GTP1 Publication
Nucleotide bindingi156 – 1583GTP1 Publication

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB
  4. protein transporter activity Source: Ensembl

GO - Biological processi

  1. antigen processing and presentation Source: UniProtKB
  2. GTP catabolic process Source: UniProtKB
  3. membrane organization Source: Reactome
  4. regulation of endocytosis Source: Ensembl
  5. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
SignaLinkiP20338.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-4A
Gene namesi
Name:RAB4A
Synonyms:RAB4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9781. RAB4A.

Subcellular locationi

Membrane; Peripheral membrane protein. Cytoplasm
Note: Generally associated with membranes. Cytoplasmic when phosphorylated by CDK1.

GO - Cellular componenti

  1. endosome Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB-KW
  4. perinuclear region of cytoplasm Source: UniProtKB
  5. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511G → A: 10-fold decrease in ZFYVE20 binding affinity. 1 Publication
Mutagenesisi51 – 511G → L: 10-fold decrease in ZFYVE20 binding affinity. 1 Publication

Organism-specific databases

PharmGKBiPA34141.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Ras-related protein Rab-4APRO_0000121093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041Phosphoserine; by CDK11 Publication
Lipidationi216 – 2161S-geranylgeranyl cysteineBy similarity
Modified residuei218 – 2181Cysteine methyl esterBy similarity
Lipidationi218 – 2181S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

Phosphorylated by CDK1 kinase during mitosis.2 Publications

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP20338.
PaxDbiP20338.
PRIDEiP20338.

PTM databases

PhosphoSiteiP20338.

Expressioni

Gene expression databases

BgeeiP20338.
CleanExiHS_RAB4A.
GenevestigatoriP20338.

Organism-specific databases

HPAiCAB004990.

Interactioni

Subunit structurei

Interacts with SGSM1, SGSM2 and SGSM3 By similarity. Interacts with RAB11FIP1, RABEP1, ZFYVE20 and RUFY1. Interacts (membrane-bound form) with NDRG1; the interaction involves NDRG1 in vesicular recycling of E-cadherin.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GDI1P311502EBI-722284,EBI-946999
GDI2P503952EBI-722284,EBI-1049143

Protein-protein interaction databases

BioGridi111805. 33 interactions.
DIPiDIP-372N.
IntActiP20338. 14 interactions.
MINTiMINT-1376149.
STRINGi9606.ENSP00000355651.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 2111
Helixi26 – 3510
Beta strandi46 – 5712
Beta strandi60 – 6910
Helixi73 – 753
Helixi76 – 805
Beta strandi87 – 948
Helixi98 – 1025
Helixi104 – 11411
Beta strandi120 – 1267
Helixi128 – 1336
Helixi138 – 14710
Beta strandi151 – 1544
Turni157 – 1593
Helixi163 – 17917

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YU9X-ray2.07A7-177[»]
1Z0KX-ray1.92A/C7-177[»]
2BMDX-ray1.80A6-189[»]
2BMEX-ray1.57A/B/C/D6-189[»]
ProteinModelPortaliP20338.
SMRiP20338. Positions 7-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20338.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 509Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118841.
HOVERGENiHBG009351.
InParanoidiP20338.
KOiK07879.
OMAiDESNHTI.
OrthoDBiEOG7QK0CV.
PhylomeDBiP20338.
TreeFamiTF300032.

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]

Sequencei

Sequence statusi: Complete.

P20338-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQTAMSETY DFLFKFLVIG NAGTGKSCLL HQFIEKKFKD DSNHTIGVEF
60 70 80 90 100
GSKIINVGGK YVKLQIWDTA GQERFRSVTR SYYRGAAGAL LVYDITSRET
110 120 130 140 150
YNALTNWLTD ARMLASQNIV IILCGNKKDL DADREVTFLE ASRFAQENEL
160 170 180 190 200
MFLETSALTG ENVEEAFVQC ARKILNKIES GELDPERMGS GIQYGDAALR
210
QLRSPRRAQA PNAQECGC
Length:218
Mass (Da):24,390
Last modified:March 6, 2013 - v3
Checksum:i983D65E1162741B0
GO

Sequence cautioni

The sequence AAA60244.1 differs from that shown. Reason: Frameshift at position 6.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621N → D in AAA60244. (PubMed:2501306)Curated
Sequence conflicti208 – 2081A → T in AAA60244. (PubMed:2501306)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28211 mRNA. Translation: AAA60244.1. Frameshift.
AY585832 mRNA. Translation: AAT91347.1.
AF498934 mRNA. Translation: AAM21082.1.
AK313807 mRNA. Translation: BAG36543.1.
AL162595, AL117350 Genomic DNA. Translation: CAI19037.1.
AL117350, AL162595 Genomic DNA. Translation: CAI22870.1.
CH471098 Genomic DNA. Translation: EAW69890.1.
BC002438 mRNA. Translation: AAH02438.1.
BC004309 mRNA. Translation: AAH04309.1.
CCDSiCCDS31050.1.
PIRiE34323.
RefSeqiNP_001258927.1. NM_001271998.1.
NP_004569.2. NM_004578.3.
UniGeneiHs.296169.

Genome annotation databases

EnsembliENST00000366690; ENSP00000355651; ENSG00000168118.
GeneIDi5867.
KEGGihsa:5867.
UCSCiuc001hth.4. human.

Polymorphism databases

DMDMi460018296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28211 mRNA. Translation: AAA60244.1 . Frameshift.
AY585832 mRNA. Translation: AAT91347.1 .
AF498934 mRNA. Translation: AAM21082.1 .
AK313807 mRNA. Translation: BAG36543.1 .
AL162595 , AL117350 Genomic DNA. Translation: CAI19037.1 .
AL117350 , AL162595 Genomic DNA. Translation: CAI22870.1 .
CH471098 Genomic DNA. Translation: EAW69890.1 .
BC002438 mRNA. Translation: AAH02438.1 .
BC004309 mRNA. Translation: AAH04309.1 .
CCDSi CCDS31050.1.
PIRi E34323.
RefSeqi NP_001258927.1. NM_001271998.1.
NP_004569.2. NM_004578.3.
UniGenei Hs.296169.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YU9 X-ray 2.07 A 7-177 [» ]
1Z0K X-ray 1.92 A/C 7-177 [» ]
2BMD X-ray 1.80 A 6-189 [» ]
2BME X-ray 1.57 A/B/C/D 6-189 [» ]
ProteinModelPortali P20338.
SMRi P20338. Positions 7-182.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111805. 33 interactions.
DIPi DIP-372N.
IntActi P20338. 14 interactions.
MINTi MINT-1376149.
STRINGi 9606.ENSP00000355651.

PTM databases

PhosphoSitei P20338.

Polymorphism databases

DMDMi 460018296.

Proteomic databases

MaxQBi P20338.
PaxDbi P20338.
PRIDEi P20338.

Protocols and materials databases

DNASUi 5867.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366690 ; ENSP00000355651 ; ENSG00000168118 .
GeneIDi 5867.
KEGGi hsa:5867.
UCSCi uc001hth.4. human.

Organism-specific databases

CTDi 5867.
GeneCardsi GC01P229406.
HGNCi HGNC:9781. RAB4A.
HPAi CAB004990.
MIMi 179511. gene.
neXtProti NX_P20338.
PharmGKBi PA34141.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118841.
HOVERGENi HBG009351.
InParanoidi P20338.
KOi K07879.
OMAi DESNHTI.
OrthoDBi EOG7QK0CV.
PhylomeDBi P20338.
TreeFami TF300032.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
SignaLinki P20338.

Miscellaneous databases

EvolutionaryTracei P20338.
GeneWikii RAB4A.
GenomeRNAii 5867.
NextBioi 22786.
PROi P20338.
SOURCEi Search...

Gene expression databases

Bgeei P20338.
CleanExi HS_RAB4A.
Genevestigatori P20338.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion."
    Zahraoui A., Touchot N., Chardin P., Tavitian A.
    J. Biol. Chem. 264:12394-12401(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Regulation of CD4 expression via recycling by HRES-1/RAB4 controls susceptibility to HIV infection."
    Nagy G., Ward J., Mosser D.D., Koncz A., Gergely P. Jr., Stancato C., Qian Y., Fernandez D., Niland B., Grossman C.E., Telarico T., Banki K., Perl A.
    J. Biol. Chem. 281:34574-34591(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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 (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  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.
    , 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].
    Tissue: Caudate nucleus.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 and Uterus.
  8. "Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2."
    Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M.
    Nature 350:715-718(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK1.
  9. "Reversible phosphorylation-dephosphorylation determines the localization of rab4 during the cell cycle."
    van der Sluijs P., Hull M., Huber L.A., Male P., Goud B., Mellman I.
    EMBO J. 11:4379-4389(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-204 BY CDK1.
  10. "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles."
    Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K., van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P.
    Biochem. J. 346:593-601(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABEP1.
  11. Cited for: INTERACTION WITH RAB11FIP1.
    Tissue: Cervix carcinoma.
  12. "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes."
    de Renzis S., Soennichsen B., Zerial M.
    Nat. Cell Biol. 4:124-133(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFYVE20.
  13. "Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis."
    Lindsay A.J., McCaffrey M.W.
    FEBS Lett. 571:86-92(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB11FIP1.
  14. Cited for: INTERACTION WITH RUFY1.
  15. "The N-Myc down regulated Gene1 (NDRG1) is a Rab4a effector involved in vesicular recycling of E-cadherin."
    Kachhap S.K., Faith D., Qian D.Z., Shabbeer S., Galloway N.L., Pili R., Denmeade S.R., DeMarzo A.M., Carducci M.A.
    PLoS ONE 2:E844-E844(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDRG1.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "High resolution crystal structures of human Rab4a in its active and inactive conformations."
    Huber S.K., Scheidig A.J.
    FEBS Lett. 579:2821-2829(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 6-189 IN COMPLEX WITH GTP ANALOG AND GDP.
  18. "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
    Eathiraj S., Pan X., Ritacco C., Lambright D.G.
    Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 7-177 IN COMPLEX WITH GTP, INTERACTION WITH ZFYVE20, MUTAGENESIS OF GLY-51.

Entry informationi

Entry nameiRAB4A_HUMAN
AccessioniPrimary (citable) accession number: P20338
Secondary accession number(s): Q5T7P7, Q9BQ44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 6, 2013
Last modified: October 29, 2014
This is version 161 of the entry and version 3 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

Caution

It is uncertain whether Met-1 or Met-6 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3