P01901 (HA1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
H-2 class I histocompatibility antigen, K-B alpha chain
Short name=H-2K(B)

Gene names

Name:	H2-K1
Synonyms:	H2-K

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	369 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).
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the MHC class I family. Contains 1 Ig-like C1-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Immunity
Cellular component	MHC I Membrane
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent Inferred from direct assay PubMed 1538753. Source: MGI antigen processing and presentation of exogenous peptide antigen via MHC class I Inferred from direct assay PubMed 16461341. Source: MGI defense response to bacterium Inferred from direct assay PubMed 16461341. Source: MGI immune response Inferred from electronic annotation. Source: InterPro inner ear development Inferred from direct assay PubMed 21795542. Source: MGI positive regulation of T cell mediated cytotoxicity Inferred from direct assay PubMed 1538753PubMed 16461341. Source: MGI
Cellular_component	MHC class I protein complex Inferred from electronic annotation. Source: UniProtKB-KW external side of plasma membrane Inferred from direct assay PubMed 11754812PubMed 12902470PubMed 14990792PubMed 15314074PubMed 1538753PubMed 9133426. Source: MGI integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome phagocytic vesicle membrane Traceable author statement. Source: Reactome
Molecular_function	peptide antigen binding Inferred from direct assay PubMed 16461341. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fes	P16879	3	EBI-1265227,EBI-771815

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Ref.4

Chain

22 – 369

348

H-2 class I histocompatibility antigen, K-B alpha chain Ref.4

PRO_0000018928

Regions

Topological domain

22 – 305

284

Extracellular Potential

Transmembrane

306 – 328

23

Helical; Potential

Topological domain

329 – 369

41

Cytoplasmic Potential

Domain

206 – 294

89

Ig-like C1-type

Region

22 – 111

90

Alpha-1

Region

112 – 203

92

Alpha-2

Region

204 – 295

92

Alpha-3

Region

296 – 305

10

Connecting peptide

Amino acid modifications

Glycosylation

107

1

N-linked (GlcNAc...) Ref.4 Ref.5

Glycosylation

197

1

N-linked (GlcNAc...) Ref.4

Disulfide bond

122 ↔ 185

Disulfide bond

224 ↔ 280

Experimental info

Sequence conflict

217

1

E → D AA sequence Ref.4

Sequence conflict

289

1

E → Q AA sequence Ref.4

Sequence conflict

334

1

N → A AA sequence Ref.4

Sequence conflict

364

1

D → P AA sequence Ref.4

Secondary structure

1

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369

Helix Strand Turn

Details...

Beta strand

24 – 33

10

Beta strand

38 – 40

3

Beta strand

42 – 49

8

Beta strand

52 – 58

7

Beta strand

61 – 63

3

Beta strand

67 – 70

4

Helix

71 – 75

5

Helix

78 – 105

28

Beta strand

110 – 112

3

Beta strand

115 – 124

10

Beta strand

126 – 128

3

Beta strand

130 – 139

10

Beta strand

142 – 147

6

Turn

149 – 152

4

Beta strand

154 – 158

5

Helix

159 – 171

13

Helix

173 – 182

10

Helix

184 – 195

12

Helix

197 – 200

4

Beta strand

207 – 214

8

Beta strand

216 – 232

17

Beta strand

235 – 240

6

Beta strand

243 – 245

3

Turn

246 – 248

3

Beta strand

249 – 251

3

Beta strand

258 – 260

3

Beta strand

262 – 271

10

Helix

275 – 277

3

Beta strand

278 – 283

6

Beta strand

287 – 289

3

Beta strand

291 – 293

3

Sequences

	Sequence		Length	Mass (Da)
	P01901 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 3D2F125318193443	FASTA	369	41,302
	10 20 30 40 50 60 MVPCTLLLLL AAALAPTQTR AGPHSLRYFV TAVSRPGLGE PRYMEVGYVD DTEFVRFDSD 70 80 90 100 110 120 AENPRYEPRA RWMEQEGPEY WERETQKAKG NEQSFRVDLR TLLGYYNQSK GGSHTIQVIS 130 140 150 160 170 180 GCEVGSDGRL LRGYQQYAYD GCDYIALNED LKTWTAADMA ALITKHKWEQ AGEAERLRAY 190 200 210 220 230 240 LEGTCVEWLR RYLKNGNATL LRTDSPKAHV THHSRPEDKV TLRCWALGFY PADITLTWQL 250 260 270 280 290 300 NGEELIQDME LVETRPAGDG TFQKWASVVV PLGKEQYYTC HVYHQGLPEP LTLRWEPPPS 310 320 330 340 350 360 TVSNMATVAV LVVLGAAIVT GAVVAFVMKM RRRNTGGKGG DYALAPGSQT SDLSLPDCKV MVHDPHSLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence of the H-2K(b) gene: evidence for gene conversion as a mechanism for the generation of polymorphism in histocompatibility antigens." Weiss E., Golden L., Zakut R., Mellor A., Fahrner K., Kvist S., Flavell R.A. EMBO J. 2:453-462(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Nucleotide sequences of three H-2K and three H-2D complementary DNA clones coding mouse class I MHC heavy chain proteins." Wang M., Stepkowski S.M., Hebert J.S., Tian L., Yu J., Kahan B.D. Ann. Transplant. 1:26-31(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/10.
[3]	"Isolation of a cDNA clone for the murine transplantation antigen H-2Kb." Reyes A.A., Schold M., Itakura K., Wallace R.B. Proc. Natl. Acad. Sci. U.S.A. 79:3270-3274(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-369.
[4]	"Amino acid sequence of the carboxyl-terminal hydrophilic region of the H-2Kb MHC alloantigen. Completion of the entire primary structure of the H-2Kb molecule." Uehara H., Coligan J.E., Nathenson S.G. Biochemistry 20:5940-5945(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-367, GLYCOSYLATION AT ASN-107 AND ASN-197.
[5]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107, MASS SPECTROMETRY.
[6]	"Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb." Fremont D.H., Matsumura M., Stura E.A., Peterson P.A., Wilson I.A. Science 257:919-927(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-295.
[7]	"Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-2Kb." Kern P.S., Teng M.K., Smolyar A., Liu J.H., Liu J., Hussey R.E., Spoerl R., Chang H.-C., Reinherz E.L., Wang J.-H. Immunity 9:519-530(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-295 IN COMPLEX WITH CD8A.
[8]	"Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL." Speir J.A., Abdel-Motal U.M., Jondal M., Wilson I.A. Immunity 10:51-61(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-295.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00400 mRNA. Translation: AAA39648.1.
U47328 mRNA. Translation: AAB17606.1.
V00746, V00747 Genomic DNA. Translation: CAA24119.2.

IPI

IPI00874741.

PIR

HLMSKB. A90980.

RefSeq

NP_001001892.2. NM_001001892.2.

UniGene

Mm.422886.
Mm.439675.
Mm.440940.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BQH	X-ray	2.80	A/D	22-295	[»]
1FO0	X-ray	2.50	H	22-296	[»]
1FZJ	X-ray	1.90	A	22-295	[»]
1FZK	X-ray	1.70	A	22-295	[»]
1FZM	X-ray	1.80	A	22-295	[»]
1FZO	X-ray	1.80	A	22-295	[»]
1G6R	X-ray	2.80	H/I	22-295	[»]
1G7P	X-ray	1.50	A	22-295	[»]
1G7Q	X-ray	1.60	A	22-295	[»]
1KBG	X-ray	2.20	H	22-295	[»]
1KJ2	X-ray	2.71	H/I	22-298	[»]
1KJ3	X-ray	2.30	H/I	22-299	[»]
1KPU	X-ray	1.50	A	22-295	[»]
1KPV	X-ray	1.71	A	22-295	[»]
1LEG	X-ray	1.75	A	22-295	[»]
1LEK	X-ray	2.15	A	22-295	[»]
1LK2	X-ray	1.35	A	22-295	[»]
1MWA	X-ray	2.40	H/I	22-295	[»]
1N59	X-ray	2.95	A/C	22-297	[»]
1NAM	X-ray	2.70	H	22-296	[»]
1NAN	X-ray	2.30	H/L	22-299	[»]
1OSZ	X-ray	2.10	A	22-295	[»]
1P1Z	X-ray	3.26	A	22-295	[»]
1P4L	X-ray	2.90	A	22-295	[»]
1RJY	X-ray	1.90	A/D	22-301	[»]
1RJZ	X-ray	2.60	A/D	22-301	[»]
1RK0	X-ray	2.61	A	22-295	[»]
1RK1	X-ray	2.10	A	22-295	[»]
1S7Q	X-ray	1.99	A	22-369	[»]
1S7R	X-ray	2.95	A/D	22-369	[»]
1S7S	X-ray	1.99	A	22-369	[»]
1S7T	X-ray	2.30	A/D	22-369	[»]
1T0M	X-ray	2.00	A/D	22-299	[»]
1T0N	X-ray	1.80	A/D	22-299	[»]
1VAC	X-ray	2.50	A	22-295	[»]
1VAD	X-ray	2.50	A	22-295	[»]
1WBZ	X-ray	2.00	A/C	22-296	[»]
2CKB	X-ray	3.00	H/I	22-295	[»]
2CLV	X-ray	1.90	A/H	22-300	[»]
2CLZ	X-ray	1.90	A/H	22-300	[»]
2FO4	X-ray	2.70	A	22-295	[»]
2MHA	X-ray	2.50	A/C	22-291	[»]
2OL3	X-ray	2.90	H	22-300	[»]
2QRI	X-ray	2.00	A/B	22-301	[»]
2QRS	X-ray	2.00	A/B	22-301	[»]
2QRT	X-ray	1.80	A/B	22-301	[»]
2VAA	X-ray	2.30	A	22-295	[»]
2VAB	X-ray	2.50	A	22-295	[»]
2ZSV	X-ray	1.80	A/C	22-299	[»]
2ZSW	X-ray	2.80	A/C/E/G	22-299	[»]
3C8K	X-ray	2.90	A	22-295	[»]
3CVH	X-ray	2.90	A/M	22-295	[»]
3P4M	X-ray	2.50	A/D	22-298	[»]
3P4N	X-ray	2.50	A/D	22-298	[»]
3P4O	X-ray	2.30	A/D	22-298	[»]
3P9L	X-ray	2.00	A/D	22-299	[»]
3P9M	X-ray	2.00	A/D	22-298	[»]
3PAB	X-ray	2.20	A/D	22-299	[»]
3RGV	X-ray	2.90	C	22-296	[»]
3ROL	X-ray	2.60	A/C	22-296	[»]
3ROO	X-ray	2.00	A/C	22-296	[»]
3TID	X-ray	1.65	A	22-297	[»]
3TIE	X-ray	2.25	A/D	22-297	[»]
4HKJ	X-ray	3.00	A/E/I/M	22-301	[»]

ProteinModelPortal

P01901.

SMR

P01901. Positions 22-295.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6189N.

IntAct

P01901. 2 interactions.

MINT

MINT-241080.

Proteomic databases

PaxDb

P01901.

PRIDE

P01901.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000025181; ENSMUSP00000025181; ENSMUSG00000061232.

GeneID

14972.

KEGG

mmu:14972.

Organism-specific databases

CTD

14972.

MGI

MGI:95904. H2-K1.

Phylogenomic databases

eggNOG

NOG42056.

HOVERGEN

HBG016709.

InParanoid

P01901.

KO

K06751.

OMA

ERNTHIC.

Enzyme and pathway databases

Reactome

REACT_102124. Immune System.
REACT_107772. Immune System.

Gene expression databases

ArrayExpress

P01901.

Bgee

P01901.

CleanEx

MM_H2-K1.

Genevestigator

P01901.

GermOnline

ENSMUSG00000061232. Mus musculus.

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

H2-K1. mouse.

EvolutionaryTrace

P01901.

NextBio

287336.

SOURCE

Search...

Entry information

Entry name

HA1B_MOUSE

Accession

Primary (citable) accession number: P01901

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program