P30685 (1B35_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
HLA class I histocompatibility antigen, B-35 alpha chain

Alternative name(s):
MHC class I antigen B*35

Gene names

Name:	HLA-B
Synonyms:	HLAB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the presentation of foreign antigens to the immune system.
Subunit structure	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.
Post-translational modification	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*35:01, B*35:02, B*35:03, B*35:04, B*35:05 (B35-G), B*35:06 (B35-K), B*35:07, B*35:08, B*35:25, B*35:28, B*35:29 (B*KG), B*35:30, B*35:32 (B*TMUL) and B*35:36. The sequence shown is that of B*35:01.
Sequence similarities	Belongs to the MHC class I family. Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Host-virus interaction Immunity
Cellular component	MHC I Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Traceable author statement. Source: Reactome interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome regulation of immune response Traceable author statement. Source: Reactome type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ER to Golgi transport vesicle membrane Traceable author statement. Source: Reactome Golgi membrane Traceable author statement. Source: Reactome MHC class I protein complex Inferred from electronic annotation. Source: UniProtKB-KW early endosome membrane Traceable author statement. Source: Reactome integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome phagocytic vesicle membrane Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Chain

25 – 362

338

HLA class I histocompatibility antigen, B-35 alpha chain

PRO_0000018840

Regions

Topological domain

25 – 308

284

Extracellular Potential

Transmembrane

309 – 332

24

Helical; Potential

Topological domain

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

Amino acid modifications

Glycosylation

110

1

N-linked (GlcNAc...) By similarity

Disulfide bond

125 ↔ 188

Disulfide bond

227 ↔ 283

Natural variations

Natural variant

40

1

G → V in allele B*35:07.

VAR_016393

Natural variant

48

1

A → S in allele B*35:25.

VAR_016394

Natural variant

69

1

T → E in allele B*35:25; requires 2 nucleotide substitutions.

VAR_016395

Natural variant

87

1

N → E in allele B*35:28; requires 2 nucleotide substitutions.

VAR_016396

Natural variant

91

1

F → S in allele B*35:28.

VAR_016397

Natural variant

98

1

Y → D in allele B*35:29.

VAR_016398

Natural variant

107

1

G → D in allele B*35:36.

VAR_016399

Natural variant

118 – 119

2

II → TL in allele B*35:05 and allele B*35:32.

VAR_016400

Natural variant

121

1

R → S in allele B*35:05 and allele B*35:30.

VAR_016401

Natural variant

127

1

L → V in allele B*35:32.

VAR_016402

Natural variant

133

1

L → F in allele B*35:02.

VAR_016403

Natural variant

138

1

D → N in allele B*35:02, allele B*35:04 and allele B*35:06.

VAR_016404

Natural variant

140

1

S → F in allele B*35:06 and allele B*35:36.

VAR_016405

Natural variant

140

1

S → Y in allele B*35:02, allele B*35:03 and allele B*35:04.

VAR_016406

Natural variant

180

1

L → R in allele B*35:08.

VAR_016407

Secondary structure

1

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362

Helix Strand Turn

Details...

Beta strand

27 – 36

10

Beta strand

41 – 43

3

Beta strand

45 – 52

8

Beta strand

55 – 61

7

Beta strand

64 – 66

3

Beta strand

69 – 71

3

Helix

74 – 76

3

Helix

81 – 108

28

Beta strand

113 – 115

3

Beta strand

118 – 127

10

Beta strand

133 – 142

10

Beta strand

145 – 150

6

Beta strand

157 – 161

5

Helix

162 – 173

12

Helix

176 – 185

10

Helix

187 – 198

12

Helix

200 – 203

4

Beta strand

210 – 217

8

Beta strand

219 – 235

17

Beta strand

238 – 243

6

Helix

249 – 251

3

Beta strand

252 – 254

3

Beta strand

261 – 263

3

Beta strand

265 – 274

10

Helix

278 – 280

3

Beta strand

281 – 286

6

Beta strand

290 – 292

3

Beta strand

294 – 296

3

Sequences

	Sequence		Length	Mass (Da)
	P30685 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 52906854FC43E7A6	FASTA	362	40,455
	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

References

[1]	"The structure of HLA-B35 suggests that it is derived from HLA-Bw58 by two genetic mechanisms." Ooba T., Hayashi H., Karaki S., Tanabe M., Kano K., Takiguchi M. Immunogenetics 30:76-80(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*35:01).
[2]	"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." Chertkoff L.P., Herrera M., Fainboim L., Satz M.L. Hum. Immunol. 31:153-158(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*35:02).
[3]	"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." Zemmour J., Little A.-M., Schendel D.J., Parham P. J. Immunol. 148:1941-1948(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*35:03).
[4]	"Polymorphism of human minor histocompatibility antigens: T cell recognition of human minor histocompatibility peptides presented by HLA-B35 subtype molecules." Beck Y., Satz L., Takamiya Y., Nakayama S., Ling L., Ishikawa Y., Nagao T., Uchida H., Tokunaga K., Mueller C., Juji T., Takiguchi M. J. Exp. Med. 181:2037-2048(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ALLELE B*35:03). Tissue: Blood.
[5]	"Unusual HLA-B alleles in two tribes of Brazilian Indians." Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., Williams R.C., Luz R., Petzl-Erler M.L., Parham P. Nature 357:326-329(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ALLELES B*35:05 AND B*35:06).
[6]	"Isolation and characterization of two new functional subtypes of HLA-B35." Theiler G., Pando M., Delfino J.M., Takiguchi M., Satz M.L. Tissue Antigens 41:143-147(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*35:07 AND B*35:08).
[7]	"Microheterogeneity in HLA-B35 alleles influences peptide-dependent allorecognition by cytotoxic T cells but not binding of a peptide-restricted monoclonal antibody." Steinle A., Reinhardt C., Noessner E., Uchanska-Ziegler B., Ziegler A., Schendel D.J. Hum. Immunol. 38:261-269(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*35:08).
[8]	"New recombinant HLA-B alleles in a tribe of South American Amerindians indicate rapid evolution of MHC class I loci." 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. Nature 357:329-333(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 9-362 (ALLELE B*35:04).
[9]	"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." 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. Tissue Antigens 55:266-270(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*35:29 AND B*35:32).
[10]	"Twenty-nine new HLA-B alleles associated with antigens in the 5C CREG." 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. Tissue Antigens 57:481-485(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES B*35:25; B*35:28; B*35:29; B*35:30 AND B*35:36).
[11]	"An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501." Smith K.J., Reid S.W., Stuart D.I., McMichael A.J., Jones E.Y., Bell J.I. Immunity 4:203-214(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-300.
[12]	"Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C-terminus." Menssen R., Orth P., Ziegler A., Saenger W. J. Mol. Biol. 285:645-653(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M28115 , M28109, M28110, M28111, M28112, M28113, M28114 Genomic DNA. Translation: AAA59617.1.
M63454 Genomic DNA. Translation: AAA59682.1.
M81798 mRNA. Translation: AAA59684.1.
D50299 mRNA. Translation: BAA08828.1.
M84385 mRNA. Translation: AAA59635.1.
M84381 mRNA. Translation: AAA59631.1.
L04695 mRNA. Translation: AAA59694.1.
L04696 mRNA. Translation: AAA52674.1.
Z22651 mRNA. Translation: CAA80366.1.
M86403 mRNA. No translation available.
AH007565 Genomic DNA. Translation: AAD23460.1.
AH007706 Genomic DNA. Translation: AAD30277.1.
AH006372 Genomic DNA. Translation: AAC32570.1.
AH007604 Genomic DNA. Translation: AAD27538.1.
AH008126 Genomic DNA. Translation: AAD51745.1.
AH007584 Genomic DNA. Translation: AAD26151.1.
AH009759 Genomic DNA. Translation: AAG01819.1.

IPI

IPI00646083.

PIR

A45880.
I54298.
I56133.
I61904.
I61907.
I81233.

UniGene

Hs.654404.
Hs.77961.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A1N	X-ray	2.00	A	25-300	[»]
1A9B	X-ray	3.20	A/D	25-301	[»]
1A9E	X-ray	2.50	A	25-301	[»]
1CG9	X-ray	2.70	A	25-301	[»]
1XH3	X-ray	1.48	A	25-300	[»]
1ZHK	X-ray	1.60	A	25-300	[»]
1ZHL	X-ray	1.50	A	25-300	[»]
1ZSD	X-ray	1.70	A	25-300	[»]
2AK4	X-ray	2.50	A/F/K/Q	25-300	[»]
2AXF	X-ray	1.80	A	25-300	[»]
2AXG	X-ray	2.00	A	25-300	[»]
2CIK	X-ray	1.75	A	25-300	[»]
2FYY	X-ray	1.50	A	25-300	[»]
2FZ3	X-ray	1.90	A	25-300	[»]
2H6P	X-ray	1.90	A	25-300	[»]
2NW3	X-ray	1.70	A	25-300	[»]
2NX5	X-ray	2.70	A/F/K/Q	25-300	[»]
3BW9	X-ray	1.75	A	25-300	[»]
3BWA	X-ray	1.30	A	25-300	[»]
3KWW	X-ray	2.18	A	25-300	[»]
3KXF	X-ray	3.10	A/C/I/K	25-300	[»]
3LKN	X-ray	2.00	A	25-300	[»]
3LKO	X-ray	1.80	A	25-300	[»]
3LKP	X-ray	1.80	A	25-300	[»]
3LKQ	X-ray	1.80	A	25-300	[»]
3LKR	X-ray	2.00	A	25-300	[»]
3LKS	X-ray	1.90	A	25-300	[»]
3MV7	X-ray	2.00	A	25-300	[»]
3MV8	X-ray	2.10	A	25-300	[»]
3MV9	X-ray	2.70	A	25-300	[»]
3VFS	X-ray	1.85	A	25-300	[»]
3VFT	X-ray	1.95	A	25-300	[»]
3VFU	X-ray	1.65	A	25-300	[»]
3VFV	X-ray	1.55	A	25-300	[»]
3VFW	X-ray	2.30	A	25-300	[»]

ProteinModelPortal

P30685.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30685. 1 interaction.

Polymorphism databases

DMDM

231390.

Proteomic databases

PRIDE

P30685.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359635; ENSP00000352656; ENSG00000206450.

Organism-specific databases

GeneCards

GC06M031321.

H-InvDB

HIX0167180.

HGNC

HGNC:4932. HLA-B.

MIM

142830. gene.

neXtProt

NX_P30685.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG016709.

InParanoid

P30685.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P30685.

CleanEx

HS_HLA-B.

Genevestigator

P30685.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
3.30.500.10. 1 hit.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR001039. MHC_I_a_a1/a2.
IPR010579. MHC_I_a_C.
[Graphical view]

Pfam

PF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view]

PRINTS

PR01638. MHCCLASSI.

SMART

SM00407. IGc1. 1 hit.
[Graphical view]

SUPFAM

SSF54452. MHC_I/II-like_Ag-recog. 1 hit.

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HLA-B. human.

EvolutionaryTrace

P30685.

SOURCE

Search...

Entry information

Entry name

1B35_HUMAN

Accession

Primary (citable) accession number: P30685
Secondary accession number(s): O62919 , P30468, P30469, P30470, P30471, P30472, P30473, P30474, Q9GJM7, Q9TPV2, Q9TQH3, Q9TQH9, Q9TQN4, Q9TQN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.