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UniProtKB/Swiss-Prot entry P30685


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 1B35_HUMAN
Primary accession number P30685
Secondary accession numbers O62919 P30468 P30469 P30470 P30471 P30472 P30473 P30474 Q9GJM7 Q9TPV2 Q9TQH3 Q9TQH9 Q9TQN4 Q9TQN6
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 88)
Name and origin of the protein
Protein name HLA class I histocompatibility antigen, B-35 alpha chain [Precursor]
Synonym MHC class I antigen B*35
Gene name
Name: HLA-B
Synonyms: HLAB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*3501).
DOI=10.1007/BF02421534; PubMed=2788131 [NCBI, ExPASy, EBI, Israel, Japan]
Ooba T., Hayashi H., Karaki S., Tanabe M., Kano K., Takiguchi M.;
"The structure of HLA-B35 suggests that it is derived from HLA-Bw58 by two genetic mechanisms.";
Immunogenetics 30:76-80(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*3502).
DOI=10.1016/0198-8859(91)90020-A; PubMed=1890016 [NCBI, ExPASy, EBI, Israel, Japan]
Chertkoff L.P., Herrera M., Fainboim L., Satz M.L.;
"Complete nucleotide sequence of a genomic clone encoding HLA-B35 isolated from a Caucasian individual of Hispanic origin. Identification of a new variant of HLA-B35.";
Hum. Immunol. 31:153-158(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3503).
PubMed=1541831 [NCBI, ExPASy, EBI, Israel, Japan]
Zemmour J., Little A.-M., Schendel D.J., Parham P.;
"The HLA-A,B 'negative' mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon.";
J. Immunol. 148:1941-1948(1992).
[4]
NUCLEOTIDE SEQUENCE (ALLELE B*3503).
TISSUE=Blood;
DOI=10.1084/jem.181.6.2037; PubMed=7759996 [NCBI, ExPASy, EBI, Israel, Japan]
Beck Y., Satz L., Takamiya Y., Nakayama S., Ling L., Ishikawa Y., Nagao T., Uchida H., Tokunaga K., Mueller C., Juji T., Takiguchi M.;
"Polymorphism of human minor histocompatibility antigens: T cell recognition of human minor histocompatibility peptides presented by HLA-B35 subtype molecules.";
J. Exp. Med. 181:2037-2048(1995).
[5]
NUCLEOTIDE SEQUENCE (ALLELES B*3505 AND B*3506).
DOI=10.1038/357326a0; PubMed=1317015 [NCBI, ExPASy, EBI, Israel, Japan]
Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., Williams R.C., Luz R., Petzl-Erler M.L., Parham P.;
"Unusual HLA-B alleles in two tribes of Brazilian Indians.";
Nature 357:326-329(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*3507 AND B*3508).
PubMed=8316945 [NCBI, ExPASy, EBI, Israel, Japan]
Theiler G., Pando M., Delfino J.M., Takiguchi M., Satz M.L.;
"Isolation and characterization of two new functional subtypes of HLA-B35.";
Tissue Antigens 41:143-147(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3508).
DOI=10.1016/0198-8859(93)90553-D; PubMed=8138421 [NCBI, ExPASy, EBI, Israel, Japan]
Steinle A., Reinhardt C., Noessner E., Uchanska-Ziegler B., Ziegler A., Schendel D.J.;
"Microheterogeneity in HLA-B35 alleles influences peptide-dependent allorecognition by cytotoxic T cells but not binding of a peptide-restricted monoclonal antibody.";
Hum. Immunol. 38:261-269(1993).
[8]
NUCLEOTIDE SEQUENCE OF 9-362 (ALLELE B*3504).
DOI=10.1038/357329a0; PubMed=1589035 [NCBI, ExPASy, EBI, Israel, Japan]
Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., Troup G.M., Hughes A.L., Letvin N.L.;
"New recombinant HLA-B alleles in a tribe of South American Amerindians indicate rapid evolution of MHC class I loci.";
Nature 357:329-333(1992).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*3529 AND B*3532).
DOI=10.1034/j.1399-0039.2000.550311.x; PubMed=10777103 [NCBI, ExPASy, EBI, Israel, Japan]
Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Greville W.D., Kennedy A., Taverniti A., Moses J.H., Clow N., Watson N., Dunckley H.;
"Routine HLA-B genotyping with PCR-sequence-specific oligonucleotides (PCR-SSO) detects eight new alleles: B*0807, B*0809, B*1551, B*3529, B*3532, B*4025, B*5304 and B*5508.";
Tissue Antigens 55:266-270(2000).
[10]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES B*3525; B*3528; B*3529; B*3530 AND B*3536).
DOI=10.1034/j.1399-0039.2001.057005481.x; PubMed=11556976 [NCBI, ExPASy, EBI, Israel, Japan]
Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., Mitton W., Ng J., Hartzman R.J., Hurley C.K.;
"Twenty-nine new HLA-B alleles associated with antigens in the 5C CREG.";
Tissue Antigens 57:481-485(2001).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-300.
DOI=10.1016/S1074-7613(00)80429-X; PubMed=8624811 [NCBI, ExPASy, EBI, Israel, Japan]
Smith K.J., Reid S.W., Stuart D.I., McMichael A.J., Jones E.Y., Bell J.I.;
"An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.";
Immunity 4:203-214(1996).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1006/jmbi.1998.2363; PubMed=9878435 [NCBI, ExPASy, EBI, Israel, Japan]
Menssen R., Orth P., Ziegler A., Saenger W.;
"Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C-terminus.";
J. Mol. Biol. 285:645-653(1999).
Comments
  • FUNCTION: Involved in the presentation of foreign antigens to the immune system.
  • SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). Interacts with human herpesvirus 8 MIR1 protein (By similarity).
  • SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
  • PTM: Polyubiquitinated in a post ER compartment by interaction with human herpesvirus 8 MIR1 protein. This targets the protein for rapid degradation via the ubiquitin system (By similarity).
  • POLYMORPHISM: The following alleles of B-35 are known: B*3501, B*3502, B*3503, B*3504, B*3505 (B35-G), B*3506 (B35-K), B*3507, B*3508, B*3525, B*3528, B*3529 (B*KG), B*3530, B*3532 (B*TMUL) and B*3536. The sequence shown is that of B*3501.
  • SIMILARITY: Belongs to the MHC class I family.
  • SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M28115; AAA59617.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28109; AAA59617.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28110; AAA59617.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28111; AAA59617.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28112; AAA59617.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28113; AAA59617.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28114; AAA59617.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63454; AAA59682.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M81798; AAA59684.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D50299; BAA08828.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M84385; AAA59635.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M84381; AAA59631.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L04695; AAA59694.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L04696; AAA52674.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22651; CAA80366.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M86403; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AF117771; AAD23460.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF117770; AAD23460.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134867; AAD30277.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134866; AAD30277.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061864; AAC32570.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061863; AAC32570.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF108429; AAD27538.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF108428; AAD27538.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF176078; AAD51745.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF176077; AAD51745.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF110505; AAD26151.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF110504; AAD26151.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF282766; AAG01819.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF282765; AAG01819.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45880; A45880.
I54298; I54298.
I56133; I56133.
I61904; I61904.
I61907; I61907.
I81233; I81233.
UniGene Hs.654404
3D structure databases
PDB
1A1N; X-ray; 2.00 A; A=25-300.[ExPASy / RCSB / EBI]
1A9B; X-ray; 3.20 A; A/D=25-301.[ExPASy / RCSB / EBI]
1A9E; X-ray; 2.50 A; A=25-301.[ExPASy / RCSB / EBI]
1CG9; X-ray; 2.70 A; A=25-301.[ExPASy / RCSB / EBI]
1XH3; X-ray; 1.48 A; A=25-300.[ExPASy / RCSB / EBI]
1ZHK; X-ray; 1.60 A; A=25-300.[ExPASy / RCSB / EBI]
1ZHL; X-ray; 1.50 A; A=25-300.[ExPASy / RCSB / EBI]
1ZSD; X-ray; 1.70 A; A=25-300.[ExPASy / RCSB / EBI]
2AK4; X-ray; 2.50 A; A/F/K/Q=25-300.[ExPASy / RCSB / EBI]
2AXF; X-ray; 1.80 A; A=25-300.[ExPASy / RCSB / EBI]
2AXG; X-ray; 2.00 A; A=25-300.[ExPASy / RCSB / EBI]
2CIK; X-ray; 1.75 A; A=25-300.[ExPASy / RCSB / EBI]
2FYY; X-ray; 1.50 A; A=25-300.[ExPASy / RCSB / EBI]
2FZ3; X-ray; 1.90 A; A=25-300.[ExPASy / RCSB / EBI]
2H6P; X-ray; 1.90 A; A=25-300.[ExPASy / RCSB / EBI]
2NW3; X-ray; 1.70 A; A=25-300.[ExPASy / RCSB / EBI]
2NX5; X-ray; 2.70 A; A/F/K/Q=25-300.[ExPASy / RCSB / EBI]
3BW9; X-ray; 1.75 A; A=25-300.[ExPASy / RCSB / EBI]
3BWA; X-ray; 1.30 A; A=25-300.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A1N; -.
1A9B; -.
1A9E; -.
1CG9; -.
1XH3; -.
1ZHK; -.
1ZHL; -.
1ZSD; -.
2AK4; -.
2AXF; -.
2AXG; -.
2CIK; -.
2FYY; -.
2FZ3; -.
2H6P; -.
2NW3; -.
2NX5; -.
3BW9; -.
3BWA; -.
ModBase P30685.
Protein-protein interaction databases
DIP DIP:6056N; -.
Enzyme and pathway databases
Reactome REACT_6900; Signaling in Immune System.
Organism-specific databases
H-InvDB HIX0005715; -.
HGNC HGNC:4932; HLA-B.
GenAtlas HLA-B.
MIM 142830; gene. [NCBI / EBI]
PharmGKB PA35056; -.
GeneCards P30685.
Gene expression databases
CleanEx HS_HLA-B; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042612; Cellular component: MHC class I protein complex (inferred from electronic annotation from InterPro).
GO:0002474; Biological process: antigen processing and presentation of peptide antigen via MHC class I (inferred from electronic annotation from UniProtKB-KW).
GO:0006955; Biological process: immune response (inferred from electronic annotation from InterPro).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003006; Ig/MHC_CS.
IPR003597; Ig_C1-set.
IPR011161; MHC_I-like_Ag-recog.
IPR001039; MHC_I_a_a1/a2.
IPR010579; MHC_I_a_C.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 1.
G3DSA:3.30.500.10; MHC_I-like_Ag-recog; 1.
Pfam PF07654; C1-set; 1.
PF00129; MHC_I; 1.
PF06623; MHC_I_C; 1.
Pfam graphical view of domain structure.
PRINTS PR01638; MHCCLASSI.
ProDom PD000050; MHC_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00407; IGc1; 1.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 1.
PS00290; IG_MHC; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P30685.
ProtoNet P30685.
Genome annotation databases
Ensembl ENSG00000206450; Homo sapiens. [Contig view]
Phylogenomic databases
HOVERGEN P30685; -.
Other
LinkHub P30685; -.
SOURCE HLA-B; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Glycoprotein; Host-virus interaction; Immune response; Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24      
CHAIN   25   362  338     HLA class I histocompatibility antigen, B-35 alpha chain. PRO_0000018840
TOPO_DOM   25   308  284     Extracellular (Potential). 
TRANSMEM   309   332  24     Potential. 
TOPO_DOM   333   362  30     Cytoplasmic (Potential). 
DOMAIN   209   295  87     Ig-like C1-type. 
REGION   25   114  90     Alpha-1. 
REGION   115   206  92     Alpha-2. 
REGION   207   298  92     Alpha-3. 
REGION   299   308  10     Connecting peptide. 
CARBOHYD   110   110        N-linked (GlcNAc...) (By similarity). 
DISULFID   125   188         
DISULFID   227   283         
VARIANT   40    40  1     G -> V (in allele B*3507). VAR_016393 [3D]
VARIANT   48    48  1     A -> S (in allele B*3525). VAR_016394 [3D]
VARIANT   69    69  1     T -> E (in allele B*3525; requires 2 nucleotide substitutions). VAR_016395 [3D]
VARIANT   87    87  1     N -> E (in allele B*3528; requires 2 nucleotide substitutions). VAR_016396 [3D]
VARIANT   91    91  1     F -> S (in allele B*3528). VAR_016397 [3D]
VARIANT   98    98  1     Y -> D (in allele B*3529). VAR_016398 [3D]
VARIANT   107   107  1     G -> D (in allele B*3536). VAR_016399 [3D]
VARIANT   118   119  2     II -> TL (in allele B*3505 and allele B*3532). VAR_016400
VARIANT   121   121  1     R -> S (in allele B*3505 and allele B*3530). VAR_016401 [3D]
VARIANT   127   127  1     L -> V (in allele B*3532). VAR_016402 [3D]
VARIANT   133   133  1     L -> F (in allele B*3502). VAR_016403 [3D]
VARIANT   138   138  1     D -> N (in allele B*3502, allele B*3504 and allele B*3506). VAR_016404 [3D]
VARIANT   140   140  1     S -> F (in allele B*3506 and allele B*3536). VAR_016405 [3D]
VARIANT   140   140  1     S -> Y (in allele B*3502, allele B*3503 and allele B*3504). VAR_016406 [3D]
VARIANT   180   180  1     L -> R (in allele B*3508). VAR_016407 [3D]
STRAND   27    36  10      
STRAND   41    43  3      
STRAND   45    52  8      
STRAND   55    61  7      
STRAND   64    66  3      
HELIX   74    76  3      
HELIX   81   108  28      
STRAND   118   127  10      
STRAND   133   142  10      
STRAND   145   150  6      
STRAND   157   161  5      
HELIX   162   173  12      
HELIX   176   185  10      
HELIX   187   198  12      
HELIX   200   203  4      
STRAND   210   217  8      
STRAND   219   235  17      
STRAND   238   243  6      
HELIX   249   251  3      
STRAND   261   263  3      
STRAND   265   274  10      
HELIX   278   280  3      
STRAND   281   286  6      
STRAND   294   296  3      
Sequence information
Length: 362 AA [This is the length of the unprocessed precursor] Molecular weight: 40455 Da [This is the MW of the unprocessed precursor] CRC64: 52906854FC43E7A6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF 

        70         80         90        100        110        120 
DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ 

       130        140        150        160        170        180 
RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL 

       190        200        210        220        230        240 
RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT 

       250        260        270        280        290        300 
WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP 

       310        320        330        340        350        360 
SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL 


TA 

P30685 in FASTA format

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View entry in raw text format (no links)
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