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P01911 (2B1F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
HLA class II histocompatibility antigen, DRB1-15 beta chain
Alternative name(s):
DW2.2/DR2.2
MHC class II antigen DRB1*15
Gene names
Name:HLA-DRB1
Synonyms:HLA-DRB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.

Subunit structure

Heterodimer of an alpha and a beta subunit; also referred as MHC class II molecule. In the endoplasmic reticulum (ER) it forms a heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also known as invariant chain or HLA class II histocompatibility antigen gamma chain). In the endosomal/lysosomal system; CD74 undergoes sequential degradation by various proteases; leaving a small fragment termed CLIP on each MHC class II molecule. MHC class II molecule interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP and facilitate the binding of antigenic peptides.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Late endosome membrane; Single-pass type I membrane protein. Note: The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation. Ref.15

Post-translational modification

Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II Probable. Ref.15

Polymorphism

The following alleles of DRB1-15 are known: DRB1*15:01, DRB1*15:02, DRB1*15:03, DRB1*15:04, DRB1*15:05, DRB1*15:06, DRB1*15:07, DRB1*15:08, DRB1*15:09, DRB1*15:10, DRB1*15:11, DRB1*15:12, DRB1*15:13, DRB1*15:14, DRB1*15:15, DRB1*15:16, DRB1*15:18, DRB1*15:19, DRB1*15:20, DRB1*15:21, DRB1*15:22, DRB1*15:23, DRB1*15:24, DRB1*15:25, DRB1*15:26, DRB1*15:27, DRB1*15:28, DRB1*15:29, DRB1*15:30, DRB1*15:31 and DRB1*15:32. The sequence shown is that of DRB1*15:01.

Miscellaneous

The chain shown constituted about 70% of a pool of at least seven similar beta chains.

Sequence similarities

Belongs to the MHC class II family.

Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processImmunity
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Lysosome
Membrane
MHC II
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentER to Golgi transport vesicle membrane

Traceable author statement. Source: Reactome

Golgi membrane

Traceable author statement. Source: Reactome

MHC class II protein complex

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 12519789PubMed 20458337. Source: UniProt

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

late endosome membrane

Inferred from direct assay Ref.15. Source: UniProtKB

lysosomal membrane

Inferred from direct assay Ref.15. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

trans-Golgi network membrane

Traceable author statement. Source: Reactome

transport vesicle membrane

Traceable author statement. Source: Reactome

   Molecular_functionMHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.9 Ref.10
Chain30 – 266237HLA class II histocompatibility antigen, DRB1-15 beta chain
PRO_0000080744

Regions

Topological domain30 – 227198Extracellular Potential
Transmembrane228 – 24821Helical; Potential
Topological domain249 – 26618Cytoplasmic Potential
Domain126 – 21489Ig-like C1-type
Region30 – 12495Beta-1
Region125 – 227103Beta-2

Amino acid modifications

Glycosylation481N-linked (GlcNAc...)
Disulfide bond44 ↔ 108
Disulfide bond146 ↔ 202
Cross-link254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant51K → R.
Corresponds to variant rs9270305 [ dbSNP | Ensembl ].
VAR_050364
Natural variant551F → Y.
Corresponds to variant rs16822516 [ dbSNP | Ensembl ].
VAR_050365
Natural variant591Y → H in allele DRB1*15:03.
VAR_038162
Natural variant961I → F in allele DRB1*15:04.
Corresponds to variant rs17886918 [ dbSNP | Ensembl ].
VAR_038163
Natural variant1061T → N.
Corresponds to variant rs9269941 [ dbSNP | Ensembl ].
VAR_050366
Natural variant1151V → G in allele DRB1*15:02.
Corresponds to variant rs17885482 [ dbSNP | Ensembl ].
VAR_038164
Natural variant1641G → S.
Corresponds to variant rs1059633 [ dbSNP | Ensembl ].
VAR_050367
Natural variant1691A → T.
Corresponds to variant rs2308768 [ dbSNP | Ensembl ].
VAR_050368
Natural variant2361V → M.
Corresponds to variant rs2230816 [ dbSNP | Ensembl ].
VAR_050369
Natural variant2621T → R.
Corresponds to variant rs9269744 [ dbSNP | Ensembl ].
VAR_050370

Experimental info

Sequence conflict1191T → A in AAI08923. Ref.5
Sequence conflict1541G → A in AAA59801. Ref.8
Sequence conflict1711M → G AA sequence Ref.9
Sequence conflict179 – 1802NG → D AA sequence Ref.9

Secondary structure

..................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01911 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 3B5912820A4654BE

FASTA26629,966
        10         20         30         40         50         60 
MVCLKLPGGS CMTALTVTLM VLSSPLALSG DTRPRFLWQP KRECHFFNGT ERVRFLDRYF 

        70         80         90        100        110        120 
YNQEESVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEQA RAAVDTYCRH NYGVVESFTV 

       130        140        150        160        170        180 
QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG 

       190        200        210        220        230        240 
DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL 

       250        260 
FLGAGLFIYF RNQKGHSGLQ PTGFLS 

« Hide

References

« Hide 'large scale' references
[1]"MHC class II sequences of an HLA-DR2 narcoleptic."
Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.
Immunogenetics 27:449-455(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*15:01).
Tissue: B-cell.
[2]"Ancient haplotypes of the HLA Class II region."
Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.
Genome Res. 15:1250-1257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*15:01; DRB1*15:02 AND DRB1*15:03).
[3]"Group-specific amplification of cDNA from DRB1 genes. Complete coding sequences of partially defined alleles and identification of the new alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."
Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., de Pablo R., Garcia-Sanchez F., Vicario J.L.
Hum. Immunol. 67:1008-1016(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*15:03 AND DRB1*15:04).
Tissue: Blood.
[4]"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] (ALLELE DRB1*15:01).
[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] (ALLELES DRB1*15:01 AND DRB1*15:02).
Tissue: Leukocyte.
[6]"cDNA cloning and sequencing reveals that the electrophoretically constant DR beta 2 molecules, as well as the variable DR beta 1 molecules, from HLA-DR2 subtypes have different amino acid sequences including a hypervariable region for a functionally important epitope."
Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.
J. Immunol. 138:2953-2959(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-266 (ALLELE DRB1*15:02).
Tissue: Lymphoblast.
[7]"HLA-DR2 subtypes form an additional supertypic family of DR beta alleles."
Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.
Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01).
Tissue: Lymphoblast.
[8]"Allelic variation in the DR subregion of the human major histocompatibility complex."
Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., McDevitt H.O.
Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01).
Tissue: Lymphoblast.
[9]"Primary structure of class II human histocompatibility antigens. 1st communication. Amino acid sequence of the N-terminal 198 residues of the beta chain of a HLA-Dw2,2;DR2,2-alloantigen."
Kratzin H., Yang C.-Y., Gotz H., Pauly E., Kolbel S., Egert G., Thinnes F.P., Wernet P., Altevogt P., Hilschmann N.
Hoppe-Seyler's Z. Physiol. Chem. 362:1665-1669(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-228.
Tissue: Lymphoblast.
[10]"N-terminal amino acid sequences of the alpha and beta chains of HLA-DR1 and HLA-DR2 antigens."
Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J., Reisfeld R.A.
Biochemistry 22:185-188(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-64.
Tissue: B-cell.
[11]"Invariant chain structure and MHC class II function."
Cresswell P.
Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Presentation of antigens by MHC class II molecules: getting the most out of them."
Villadangos J.A.
Mol. Immunol. 38:329-346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Autophagy in MHC class II presentation: sampling from within."
Menendez-Benito V., Neefjes J.
Immunity 26:1-3(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"MHC class II molecules on the move for successful antigen presentation."
Rocha N., Neefjes J.
EMBO J. 27:1-5(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation."
De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., Pierre P., Gatti E.
Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY MARCH1, SUBCELLULAR LOCATION.
[16]"MHC class II transport at a glance."
Berger A.C., Roche P.A.
J. Cell Sci. 122:1-4(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[17]"CD74 in antigen presentation, inflammation, and cancers of the gastrointestinal tract."
Beswick E.J., Reyes V.E.
World J. Gastroenterol. 15:2855-2861(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[18]"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].
[19]"Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor."
Hahn M., Nicholson M.J., Pyrdol J., Wucherpfennig K.W.
Nat. Immunol. 6:490-496(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 30-227.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20430 mRNA. Translation: AAA59831.1.
AY663395 Genomic DNA. Translation: AAU87979.1.
AY663406 Genomic DNA. Translation: AAU88008.1.
AY663411 Genomic DNA. Translation: AAU88023.1.
AY663414 Genomic DNA. Translation: AAU88033.1.
AY961072 mRNA. Translation: AAX63460.1.
AY961073 mRNA. Translation: AAX63461.1.
AL713966 Genomic DNA. Translation: CAI18081.1.
BC033827 mRNA. Translation: AAH33827.1.
BC108922 mRNA. Translation: AAI08923.1.
M28584 mRNA. Translation: AAA59681.1.
M16957 mRNA. Translation: AAA36279.1.
M17378 mRNA. Translation: AAA59801.1.
PIRHLHUWB. I68734.
RefSeqNP_002115.2. NM_002124.3.
UniGeneHs.534322.
Hs.696211.
Hs.736560.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX2X-ray2.60B/E32-222[»]
1YMMX-ray3.50B30-227[»]
2WBJX-ray3.00B/F30-227[»]
ProteinModelPortalP01911.
SMRP01911. Positions 32-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109368. 15 interactions.
IntActP01911. 1 interaction.

Polymorphism databases

DMDM166214928.

Proteomic databases

PRIDEP01911.

Protocols and materials databases

DNASU3123.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360004; ENSP00000353099; ENSG00000196126.
GeneID3123.
KEGGhsa:3123.
UCSCuc003obp.4. human.

Organism-specific databases

CTD3123.
GeneCardsGC06M032546.
HGNCHGNC:4948. HLA-DRB1.
HPACAB015400.
CAB034021.
MIM142857. gene.
neXtProtNX_P01911.
PharmGKBPA35072.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG012730.
InParanoidP01911.
KOK06752.
OMAFISIHIA.
PhylomeDBP01911.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP01911.
BgeeP01911.
CleanExHS_HLA-DRB1.
GenevestigatorP01911.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.320.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011162. MHC_I/II-like_Ag-recog.
IPR014745. MHC_II_a/b_N.
IPR000353. MHC_II_b_N.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
PF00969. MHC_II_beta. 1 hit.
[Graphical view]
ProDomPD000328. MHC_II_b_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00407. IGc1. 1 hit.
SM00921. MHC_II_beta. 1 hit.
[Graphical view]
SUPFAMSSF54452. SSF54452. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHLA-DRB1. human.
EvolutionaryTraceP01911.
GeneWikiHLA-DRB1.
GenomeRNAi3123.
NextBio12394.
PROP01911.
SOURCESearch...

Entry information

Entry name2B1F_HUMAN
AccessionPrimary (citable) accession number: P01911
Secondary accession number(s): Q29790 expand/collapse secondary AC list , Q29975, Q30142, Q30166, Q32MY7, Q56FN9, Q5Y7B0, Q5Y7B9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 120 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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