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P48382

- RFX5_HUMAN

UniProt

P48382 - RFX5_HUMAN

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Protein

DNA-binding protein RFX5

Gene
RFX5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi92 – 16877RFX-type winged-helixAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. protein binding Source: IntAct
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein RFX5
Alternative name(s):
Regulatory factor X 5
Gene namesi
Name:RFX5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9986. RFX5.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Bare lymphocyte syndrome 2 (BLS2) [MIM:209920]: A severe combined immunodeficiency disease with early onset. It is characterized by a profound defect in constitutive and interferon-gamma induced MHC II expression, absence of cellular and humoral T-cell response to antigen challenge, hypogammaglobulinemia and impaired antibody production. The consequence include extreme susceptibility to viral, bacterial and fungal infections.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti149 – 1491R → Q in BLS2. 1 Publication
VAR_015550

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

MIMi209920. phenotype.
Orphaneti572. Immunodeficiency by defective expression of HLA class 2.
PharmGKBiPA34356.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 616615DNA-binding protein RFX5PRO_0000215292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei185 – 1851Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP48382.
PaxDbiP48382.
PRIDEiP48382.

PTM databases

PhosphoSiteiP48382.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP48382.
BgeeiP48382.
CleanExiHS_RFX5.
GenevestigatoriP48382.

Organism-specific databases

HPAiHPA018519.

Interactioni

Subunit structurei

Homodimer. The RFX heterotetrameric complex consists of 2 molecules of RFX5 and one each of RFXAP and RFX-B/RFXANK; with each subunit representing a separate complementation group. RFX forms cooperative DNA binding complexes with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active transcriptional complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC2Q927694EBI-923266,EBI-301821

Protein-protein interaction databases

BioGridi111925. 16 interactions.
IntActiP48382. 4 interactions.
MINTiMINT-7944772.
STRINGi9606.ENSP00000290524.

Structurei

Secondary structure

1
616
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 367
Helixi40 – 5415
Helixi58 – 669
Helixi74 – 785
Beta strandi82 – 865
Beta strandi178 – 1803

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KW3NMR-A/B24-90[»]
3V30X-ray1.57B167-183[»]
ProteinModelPortaliP48382.
SMRiP48382. Positions 24-90, 94-167.

Miscellaneous databases

EvolutionaryTraceiP48382.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 9066N-terminal domainAdd
BLAST
Regioni62 – 665Leucine-rich region; critical for dimer formation and for interaction with RFXAP

Domaini

The N-terminus is required for dimer formation, association with RFXANK and RFXAP, assembly of the RFX complex, and for binding of this complex to its X box target site in the MHC-II promoter. The C-terminus mediates cooperative binding between the RFX complex and NF-Y.1 Publication

Sequence similaritiesi

Belongs to the RFX family.

Phylogenomic databases

eggNOGiNOG315073.
HOGENOMiHOG000037928.
HOVERGENiHBG014939.
InParanoidiP48382.
KOiK08061.
OMAiTCDWAER.
OrthoDBiEOG7MD4P8.
PhylomeDBiP48382.
TreeFamiTF321340.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003150. DNA-bd_RFX.
IPR029298. RFX5_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF14621. RFX5_DNA_bdg. 1 hit.
PF02257. RFX_DNA_binding. 1 hit.
[Graphical view]
PROSITEiPS51526. RFX_DBD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P48382-1) [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

MAEDEPDAKS PKTGGRAPPG GAEAGEPTTL LQRLRGTISK AVQNKVEGIL    50
QDVQKFSDND KLYLYLQLPS GPTTGDKSSE PSTLSNEEYM YAYRWIRNHL 100
EEHTDTCLPK QSVYDAYRKY CESLACCRPL STANFGKIIR EIFPDIKARR 150
LGGRGQSKYC YSGIRRKTLV SMPPLPGLDL KGSESPEMGP EVTPAPRDEL 200
VEAACALTCD WAERILKRSF SSIVEVARFL LQQHLISARS AHAHVLKAMG 250
LAEEDEHAPR ERSSKPKNGL ENPEGGAHKK PERLAQPPKD LEARTGAGPL 300
ARGERKKSVV ESSAPGANNL QVNALVARLP LLLPRAPRSL IPPIPVSPPI 350
LAPRLSSGAL KVATLPLSSR AGAPPAAVPI INMILPTVPA LPGPGPGPGR 400
APPGGLTQPR GTENREVGIG GDQGPHDKGV KRTAEVPVSE ASGQAPPAKA 450
AKQDIEDTAS DAKRKRGRPR KKSGGSGERN STPLKSAAAM ESAQSSRLPW 500
ETWGSGGEGN SAGGAERPGP MGEAEKGAVL AQGQGDGTVS KGGRGPGSQH 550
TKEAEDKIPL VPSKVSVIKG SRSQKEAFPL AKGEVDTAPQ GNKDLKEHVL 600
QSSLSQEHKD PKATPP 616
Length:616
Mass (Da):65,323
Last modified:February 1, 1996 - v1
Checksum:i5EBB33C677BB717F
GO
Isoform 2 (identifier: P48382-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-117: Missing.

Note: No experimental confirmation available.

Show »
Length:576
Mass (Da):60,513
Checksum:iF8DEC5FCB5675383
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti149 – 1491R → Q in BLS2. 1 Publication
VAR_015550
Natural varianti197 – 1971R → Q.
Corresponds to variant rs2233851 [ dbSNP | Ensembl ].
VAR_034448
Natural varianti409 – 4091P → R.
Corresponds to variant rs2233854 [ dbSNP | Ensembl ].
VAR_034449
Natural varianti499 – 4991P → S.
Corresponds to variant rs2233855 [ dbSNP | Ensembl ].
VAR_034450

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei78 – 11740Missing in isoform 2. VSP_055864Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85786 mRNA. Translation: CAA59771.1.
AK302891 mRNA. Translation: BAH13834.1.
AL391069 Genomic DNA. Translation: CAH70327.1.
CH471121 Genomic DNA. Translation: EAW53446.1.
CH471121 Genomic DNA. Translation: EAW53447.1.
CH471121 Genomic DNA. Translation: EAW53448.1.
BC017471 mRNA. Translation: AAH17471.1.
CCDSiCCDS994.1.
PIRiI38155.
RefSeqiNP_000440.1. NM_000449.3.
NP_001020774.1. NM_001025603.1.
XP_005245462.1. XM_005245405.1.
XP_005245463.1. XM_005245406.1.
UniGeneiHs.632472.

Genome annotation databases

EnsembliENST00000290524; ENSP00000290524; ENSG00000143390.
ENST00000368870; ENSP00000357864; ENSG00000143390.
ENST00000452513; ENSP00000398388; ENSG00000143390.
ENST00000452671; ENSP00000389130; ENSG00000143390.
GeneIDi5993.
KEGGihsa:5993.
UCSCiuc001exv.1. human.

Polymorphism databases

DMDMi1350587.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

RFX5base

RFX5 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85786 mRNA. Translation: CAA59771.1 .
AK302891 mRNA. Translation: BAH13834.1 .
AL391069 Genomic DNA. Translation: CAH70327.1 .
CH471121 Genomic DNA. Translation: EAW53446.1 .
CH471121 Genomic DNA. Translation: EAW53447.1 .
CH471121 Genomic DNA. Translation: EAW53448.1 .
BC017471 mRNA. Translation: AAH17471.1 .
CCDSi CCDS994.1.
PIRi I38155.
RefSeqi NP_000440.1. NM_000449.3.
NP_001020774.1. NM_001025603.1.
XP_005245462.1. XM_005245405.1.
XP_005245463.1. XM_005245406.1.
UniGenei Hs.632472.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KW3 NMR - A/B 24-90 [» ]
3V30 X-ray 1.57 B 167-183 [» ]
ProteinModelPortali P48382.
SMRi P48382. Positions 24-90, 94-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111925. 16 interactions.
IntActi P48382. 4 interactions.
MINTi MINT-7944772.
STRINGi 9606.ENSP00000290524.

PTM databases

PhosphoSitei P48382.

Polymorphism databases

DMDMi 1350587.

Proteomic databases

MaxQBi P48382.
PaxDbi P48382.
PRIDEi P48382.

Protocols and materials databases

DNASUi 5993.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290524 ; ENSP00000290524 ; ENSG00000143390 .
ENST00000368870 ; ENSP00000357864 ; ENSG00000143390 .
ENST00000452513 ; ENSP00000398388 ; ENSG00000143390 .
ENST00000452671 ; ENSP00000389130 ; ENSG00000143390 .
GeneIDi 5993.
KEGGi hsa:5993.
UCSCi uc001exv.1. human.

Organism-specific databases

CTDi 5993.
GeneCardsi GC01M151313.
HGNCi HGNC:9986. RFX5.
HPAi HPA018519.
MIMi 209920. phenotype.
601863. gene.
neXtProti NX_P48382.
Orphaneti 572. Immunodeficiency by defective expression of HLA class 2.
PharmGKBi PA34356.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315073.
HOGENOMi HOG000037928.
HOVERGENi HBG014939.
InParanoidi P48382.
KOi K08061.
OMAi TCDWAER.
OrthoDBi EOG7MD4P8.
PhylomeDBi P48382.
TreeFami TF321340.

Miscellaneous databases

EvolutionaryTracei P48382.
GeneWikii RFX5.
GenomeRNAii 5993.
NextBioi 23349.
PROi P48382.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48382.
Bgeei P48382.
CleanExi HS_RFX5.
Genevestigatori P48382.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR003150. DNA-bd_RFX.
IPR029298. RFX5_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF14621. RFX5_DNA_bdg. 1 hit.
PF02257. RFX_DNA_binding. 1 hit.
[Graphical view ]
PROSITEi PS51526. RFX_DBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel DNA-binding regulatory factor is mutated in primary MHC class II deficiency (bare lymphocyte syndrome)."
    Steimle V., Durand B., Barras E., Zufferey M., Hadam M.R., Mach B., Reith W.
    Genes Dev. 9:1021-1032(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 2).
    Tissue: Testis.
  3. "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].
  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] (ISOFORM 1).
    Tissue: Uterus.
  6. "RFX-B is the gene responsible for the most common cause of the bare lymphocyte syndrome, an MHC class II immunodeficiency."
    Nagarajan U.M., Louis-Plence P., DeSandro A., Nilsen R., Bushey A., Boss J.M.
    Immunity 10:153-162(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Lymphoblast.
  7. "A functionally essential domain of RFX5 mediates activation of major histocompatibility complex class II promoters by promoting cooperative binding between RFX and NF-Y."
    Villard J., Peretti M., Masternak K., Barras E., Caretti G., Mantovani R., Reith W.
    Mol. Cell. Biol. 20:3364-3376(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "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-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Solution structure of the heterotrimeric complex between the interaction domains of RFX5 and RFXAP from the RFX gene regulatory complex."
    Laird K.M., Briggs L.L., Boss J.M., Summers M.F., Garvie C.W.
    J. Mol. Biol. 403:40-51(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-90, SUBUNIT, DOMAIN N-TERMINAL.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 167-183 IN COMPLEX WITH RFXANK.
  12. "Mutations in the bare lymphocyte syndrome define critical steps in the assembly of the regulatory factor X complex."
    Nekrep N., Jabrane-Ferrat N., Peterlin B.M.
    Mol. Cell. Biol. 20:4455-4461(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BLS2 GLN-149.

Entry informationi

Entry nameiRFX5_HUMAN
AccessioniPrimary (citable) accession number: P48382
Secondary accession number(s): B7Z848
, D3DV19, E9PFU4, Q5VWC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 129 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, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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