Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

H2-K1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the presentation of foreign antigens to the immune system.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiR-MMU-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
H-2 class I histocompatibility antigen, K-B alpha chain
Short name:
H-2K(B)
Gene namesi
Name:H2-K1
Synonyms:H2-K
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:95904. H2-K1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 305ExtracellularSequence analysisAdd BLAST284
Transmembranei306 – 328HelicalSequence analysisAdd BLAST23
Topological domaini329 – 369CytoplasmicSequence analysisAdd BLAST41

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, MHC I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000001892822 – 369H-2 class I histocompatibility antigen, K-B alpha chainAdd BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi107N-linked (GlcNAc...)2 Publications1
Disulfide bondi122 ↔ 185
Glycosylationi197N-linked (GlcNAc...)1 Publication1
Disulfide bondi224 ↔ 280
Modified residuei354PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP01901.
PaxDbiP01901.
PeptideAtlasiP01901.
PRIDEiP01901.

PTM databases

iPTMnetiP01901.
SwissPalmiP01901.

Expressioni

Gene expression databases

BgeeiENSMUSG00000061232.
CleanExiMM_H2-K1.
ExpressionAtlasiP01901. baseline and differential.
GenevisibleiP01901. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FesP168793EBI-1265227,EBI-771815

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200155. 1 interactor.
DIPiDIP-6189N.
IntActiP01901. 3 interactors.
MINTiMINT-241080.
STRINGi10090.ENSMUSP00000025181.

Structurei

Secondary structure

1369
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 33Combined sources10
Beta strandi38 – 40Combined sources3
Beta strandi42 – 49Combined sources8
Beta strandi52 – 58Combined sources7
Beta strandi61 – 63Combined sources3
Beta strandi67 – 70Combined sources4
Helixi71 – 75Combined sources5
Helixi78 – 105Combined sources28
Beta strandi110 – 112Combined sources3
Beta strandi115 – 124Combined sources10
Beta strandi126 – 128Combined sources3
Beta strandi130 – 139Combined sources10
Beta strandi142 – 147Combined sources6
Turni149 – 152Combined sources4
Beta strandi154 – 158Combined sources5
Helixi159 – 171Combined sources13
Helixi173 – 182Combined sources10
Helixi184 – 195Combined sources12
Helixi197 – 200Combined sources4
Beta strandi207 – 214Combined sources8
Beta strandi216 – 232Combined sources17
Beta strandi235 – 240Combined sources6
Beta strandi243 – 245Combined sources3
Turni246 – 248Combined sources3
Beta strandi249 – 251Combined sources3
Beta strandi258 – 260Combined sources3
Beta strandi262 – 271Combined sources10
Helixi275 – 277Combined sources3
Beta strandi278 – 283Combined sources6
Beta strandi287 – 289Combined sources3
Beta strandi291 – 293Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQHX-ray2.80A/D22-295[»]
1FO0X-ray2.50H22-296[»]
1FZJX-ray1.90A22-295[»]
1FZKX-ray1.70A22-295[»]
1FZMX-ray1.80A22-295[»]
1FZOX-ray1.80A22-295[»]
1G6RX-ray2.80H/I22-295[»]
1G7PX-ray1.50A22-295[»]
1G7QX-ray1.60A22-295[»]
1KBGX-ray2.20H22-295[»]
1KJ2X-ray2.71H/I22-298[»]
1KJ3X-ray2.30H/I22-299[»]
1KPUX-ray1.50A22-295[»]
1KPVX-ray1.71A22-295[»]
1LEGX-ray1.75A22-295[»]
1LEKX-ray2.15A22-295[»]
1LK2X-ray1.35A22-295[»]
1MWAX-ray2.40H/I22-295[»]
1N59X-ray2.95A/C22-297[»]
1NAMX-ray2.70H22-296[»]
1NANX-ray2.30H/L22-299[»]
1OSZX-ray2.10A22-295[»]
1P1ZX-ray3.26A22-295[»]
1P4LX-ray2.90A22-295[»]
1RJYX-ray1.90A/D22-301[»]
1RJZX-ray2.60A/D22-301[»]
1RK0X-ray2.61A22-295[»]
1RK1X-ray2.10A22-295[»]
1S7QX-ray1.99A22-369[»]
1S7RX-ray2.95A/D22-369[»]
1S7SX-ray1.99A22-369[»]
1S7TX-ray2.30A/D22-369[»]
1T0MX-ray2.00A/D22-299[»]
1T0NX-ray1.80A/D22-299[»]
1VACX-ray2.50A22-295[»]
1VADX-ray2.50A22-295[»]
1WBZX-ray2.00A/C22-296[»]
2CKBX-ray3.00H/I22-295[»]
2CLVX-ray1.90A/H22-300[»]
2CLZX-ray1.90A/H22-300[»]
2FO4X-ray2.70A22-295[»]
2MHAX-ray2.50A/C22-291[»]
2OL3X-ray2.90H22-300[»]
2QRIX-ray2.00A/B22-301[»]
2QRSX-ray2.00A/B22-301[»]
2QRTX-ray1.80A/B22-301[»]
2VAAX-ray2.30A22-295[»]
2VABX-ray2.50A22-295[»]
2ZSVX-ray1.80A/C22-299[»]
2ZSWX-ray2.80A/C/E/G22-299[»]
3C8KX-ray2.90A22-295[»]
3CVHX-ray2.90A/M22-295[»]
3P4MX-ray2.50A/D22-298[»]
3P4NX-ray2.50A/D22-298[»]
3P4OX-ray2.30A/D22-298[»]
3P9LX-ray2.00A/D22-299[»]
3P9MX-ray2.00A/D22-298[»]
3PABX-ray2.20A/D22-299[»]
3RGVX-ray2.90C22-296[»]
3ROLX-ray2.60A/C22-296[»]
3ROOX-ray2.00A/C22-296[»]
3TIDX-ray1.65A22-297[»]
3TIEX-ray2.25A/D22-297[»]
4HKJX-ray3.00A/E/I/M22-301[»]
4HS3X-ray2.10A22-297[»]
4PG9X-ray2.40A22-299[»]
4PGBX-ray2.80A/D22-299[»]
4PGCX-ray2.30A/D22-299[»]
4PGDX-ray2.70A22-299[»]
4PGEX-ray2.00A22-299[»]
4PV8X-ray2.31A/C22-299[»]
4PV9X-ray2.00A/C22-299[»]
ProteinModelPortaliP01901.
SMRiP01901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01901.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini206 – 294Ig-like C1-typeAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 111Alpha-1Add BLAST90
Regioni112 – 203Alpha-2Add BLAST92
Regioni204 – 295Alpha-3Add BLAST92
Regioni296 – 305Connecting peptide10

Sequence similaritiesi

Belongs to the MHC class I family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II5V. Eukaryota.
ENOG4111K8F. LUCA.
GeneTreeiENSGT00760000118960.
HOVERGENiHBG016709.
InParanoidiP01901.
KOiK06751.
OMAiAYLEDEC.
OrthoDBiEOG091G09OH.
PhylomeDBiP01901.
TreeFamiTF336617.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProiIPR007110. 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]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view]
PRINTSiPR01638. MHCCLASSI.
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPCTLLLLL AAALAPTQTR AGPHSLRYFV TAVSRPGLGE PRYMEVGYVD
60 70 80 90 100
DTEFVRFDSD AENPRYEPRA RWMEQEGPEY WERETQKAKG NEQSFRVDLR
110 120 130 140 150
TLLGYYNQSK GGSHTIQVIS GCEVGSDGRL LRGYQQYAYD GCDYIALNED
160 170 180 190 200
LKTWTAADMA ALITKHKWEQ AGEAERLRAY LEGTCVEWLR RYLKNGNATL
210 220 230 240 250
LRTDSPKAHV THHSRPEDKV TLRCWALGFY PADITLTWQL NGEELIQDME
260 270 280 290 300
LVETRPAGDG TFQKWASVVV PLGKEQYYTC HVYHQGLPEP LTLRWEPPPS
310 320 330 340 350
TVSNMATVAV LVVLGAAIVT GAVVAFVMKM RRRNTGGKGG DYALAPGSQT
360
SDLSLPDCKV MVHDPHSLA
Length:369
Mass (Da):41,302
Last modified:July 21, 1986 - v1
Checksum:i3D2F125318193443
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti217E → D AA sequence (PubMed:7306483).Curated1
Sequence conflicti289E → Q AA sequence (PubMed:7306483).Curated1
Sequence conflicti334N → A AA sequence (PubMed:7306483).Curated1
Sequence conflicti364D → P AA sequence (PubMed:7306483).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00400 mRNA. Translation: AAA39648.1.
U47328 mRNA. Translation: AAB17606.1.
V00746, V00747 Genomic DNA. Translation: CAA24119.2.
CCDSiCCDS50069.1.
PIRiA90980. HLMSKB.
RefSeqiNP_001001892.2. NM_001001892.2.
UniGeneiMm.422886.
Mm.439675.
Mm.440940.
Mm.441651.
Mm.466882.

Genome annotation databases

EnsembliENSMUST00000025181; ENSMUSP00000025181; ENSMUSG00000061232.
GeneIDi14972.
KEGGimmu:14972.
UCSCiuc008cap.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00400 mRNA. Translation: AAA39648.1.
U47328 mRNA. Translation: AAB17606.1.
V00746, V00747 Genomic DNA. Translation: CAA24119.2.
CCDSiCCDS50069.1.
PIRiA90980. HLMSKB.
RefSeqiNP_001001892.2. NM_001001892.2.
UniGeneiMm.422886.
Mm.439675.
Mm.440940.
Mm.441651.
Mm.466882.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BQHX-ray2.80A/D22-295[»]
1FO0X-ray2.50H22-296[»]
1FZJX-ray1.90A22-295[»]
1FZKX-ray1.70A22-295[»]
1FZMX-ray1.80A22-295[»]
1FZOX-ray1.80A22-295[»]
1G6RX-ray2.80H/I22-295[»]
1G7PX-ray1.50A22-295[»]
1G7QX-ray1.60A22-295[»]
1KBGX-ray2.20H22-295[»]
1KJ2X-ray2.71H/I22-298[»]
1KJ3X-ray2.30H/I22-299[»]
1KPUX-ray1.50A22-295[»]
1KPVX-ray1.71A22-295[»]
1LEGX-ray1.75A22-295[»]
1LEKX-ray2.15A22-295[»]
1LK2X-ray1.35A22-295[»]
1MWAX-ray2.40H/I22-295[»]
1N59X-ray2.95A/C22-297[»]
1NAMX-ray2.70H22-296[»]
1NANX-ray2.30H/L22-299[»]
1OSZX-ray2.10A22-295[»]
1P1ZX-ray3.26A22-295[»]
1P4LX-ray2.90A22-295[»]
1RJYX-ray1.90A/D22-301[»]
1RJZX-ray2.60A/D22-301[»]
1RK0X-ray2.61A22-295[»]
1RK1X-ray2.10A22-295[»]
1S7QX-ray1.99A22-369[»]
1S7RX-ray2.95A/D22-369[»]
1S7SX-ray1.99A22-369[»]
1S7TX-ray2.30A/D22-369[»]
1T0MX-ray2.00A/D22-299[»]
1T0NX-ray1.80A/D22-299[»]
1VACX-ray2.50A22-295[»]
1VADX-ray2.50A22-295[»]
1WBZX-ray2.00A/C22-296[»]
2CKBX-ray3.00H/I22-295[»]
2CLVX-ray1.90A/H22-300[»]
2CLZX-ray1.90A/H22-300[»]
2FO4X-ray2.70A22-295[»]
2MHAX-ray2.50A/C22-291[»]
2OL3X-ray2.90H22-300[»]
2QRIX-ray2.00A/B22-301[»]
2QRSX-ray2.00A/B22-301[»]
2QRTX-ray1.80A/B22-301[»]
2VAAX-ray2.30A22-295[»]
2VABX-ray2.50A22-295[»]
2ZSVX-ray1.80A/C22-299[»]
2ZSWX-ray2.80A/C/E/G22-299[»]
3C8KX-ray2.90A22-295[»]
3CVHX-ray2.90A/M22-295[»]
3P4MX-ray2.50A/D22-298[»]
3P4NX-ray2.50A/D22-298[»]
3P4OX-ray2.30A/D22-298[»]
3P9LX-ray2.00A/D22-299[»]
3P9MX-ray2.00A/D22-298[»]
3PABX-ray2.20A/D22-299[»]
3RGVX-ray2.90C22-296[»]
3ROLX-ray2.60A/C22-296[»]
3ROOX-ray2.00A/C22-296[»]
3TIDX-ray1.65A22-297[»]
3TIEX-ray2.25A/D22-297[»]
4HKJX-ray3.00A/E/I/M22-301[»]
4HS3X-ray2.10A22-297[»]
4PG9X-ray2.40A22-299[»]
4PGBX-ray2.80A/D22-299[»]
4PGCX-ray2.30A/D22-299[»]
4PGDX-ray2.70A22-299[»]
4PGEX-ray2.00A22-299[»]
4PV8X-ray2.31A/C22-299[»]
4PV9X-ray2.00A/C22-299[»]
ProteinModelPortaliP01901.
SMRiP01901.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200155. 1 interactor.
DIPiDIP-6189N.
IntActiP01901. 3 interactors.
MINTiMINT-241080.
STRINGi10090.ENSMUSP00000025181.

PTM databases

iPTMnetiP01901.
SwissPalmiP01901.

Proteomic databases

EPDiP01901.
PaxDbiP01901.
PeptideAtlasiP01901.
PRIDEiP01901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025181; ENSMUSP00000025181; ENSMUSG00000061232.
GeneIDi14972.
KEGGimmu:14972.
UCSCiuc008cap.1. mouse.

Organism-specific databases

CTDi14972.
MGIiMGI:95904. H2-K1.

Phylogenomic databases

eggNOGiENOG410II5V. Eukaryota.
ENOG4111K8F. LUCA.
GeneTreeiENSGT00760000118960.
HOVERGENiHBG016709.
InParanoidiP01901.
KOiK06751.
OMAiAYLEDEC.
OrthoDBiEOG091G09OH.
PhylomeDBiP01901.
TreeFamiTF336617.

Enzyme and pathway databases

ReactomeiR-MMU-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiH2-K1. mouse.
EvolutionaryTraceiP01901.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000061232.
CleanExiMM_H2-K1.
ExpressionAtlasiP01901. baseline and differential.
GenevisibleiP01901. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProiIPR007110. 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]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
PF06623. MHC_I_C. 1 hit.
[Graphical view]
PRINTSiPR01638. MHCCLASSI.
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHA1B_MOUSE
AccessioniPrimary (citable) accession number: P01901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.