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P14434 (HA2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
H-2 class II histocompatibility antigen, A-B alpha chain

Short name=IAalpha
Gene names
Name:H2-Aa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Sequence similarities

Belongs to the MHC class II family.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 256233H-2 class II histocompatibility antigen, A-B alpha chain
PRO_0000018975

Regions

Topological domain24 – 218195Extracellular Potential
Transmembrane219 – 24426Helical; Potential
Topological domain245 – 25612Cytoplasmic Potential
Domain114 – 20693Ig-like C1-type
Region24 – 11188Alpha-1
Region112 – 20594Alpha-2
Region206 – 21813Connecting peptide

Amino acid modifications

Glycosylation1451N-linked (GlcNAc...) Ref.5
Disulfide bond134 ↔ 190 Ref.5

Secondary structure

.................................. 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14434 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: C9DD084F6179B41F

FASTA25628,093
        10         20         30         40         50         60 
MPRSRALILG VLALTTMLSL CGGEDDIEAD HVGTYGISVY QSPGDIGQYT FEFDGDELFY 

        70         80         90        100        110        120 
VDLDKKETVW MLPEFGQLAS FDPQGGLQNI AVVKHNLGVL TKRSNSTPAT NEAPQATVFP 

       130        140        150        160        170        180 
KSPVLLGQPN TLICFVDNIF PPVINITWLR NSKSVADGVY ETSFFVNRDY SFHKLSYLTF 

       190        200        210        220        230        240 
IPSDDDIYDC KVEHWGLEEP VLKHWEPEIP APMSELTETV VCALGLSVGL VGIVVGTIFI 

       250 
IQGLRSGGTS RHPGPL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the mouse major histocompatibility locus class II region."
Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., Mahairas G., Hood L.E.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Sequence of the mouse major histocompatibility class II region."
Rowen L., Qin S., Loretz C., Mix L., Lasky S., Madan A., Hood L.E.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"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].
Strain: C57BL/6J.
Tissue: Mammary gland.
[4]"Regions of allelic hypervariability in the murine A alpha immune response gene."
Benoist C.O., Mathis D.J., Kanter M.R., Williams V.E., McDevitt H.O.
Cell 34:169-177(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-256.
[5]"Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif."
Zhu Y., Rudensky A.Y., Corper A.L., Teyton L., Wilson I.A.
J. Mol. Biol. 326:1157-1174(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 24-205 IN COMPLEX WITH HUMAN CLIP PEPTIDE, GLYCOSYLATION AT ASN-145, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027865 Genomic DNA. Translation: AAB81529.1.
AF050157 Genomic DNA. Translation: AAC05285.1.
BC019721 mRNA. Translation: AAH19721.1.
BC031711 mRNA. Translation: AAH31711.1.
K01922 mRNA. Translation: AAA39614.1.
IPIIPI00126346.
RefSeqNP_034508.2. NM_010378.2.
UniGeneMm.235338.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNUX-ray2.50A/C/E/G27-208[»]
1MUJX-ray2.15A24-205[»]
3C5ZX-ray2.55C/G27-208[»]
3C60X-ray3.05C/G27-208[»]
3C6LX-ray3.40C/G27-208[»]
3RDTX-ray2.70C27-208[»]
ProteinModelPortalP14434.
SMRP14434. Positions 26-205.
ModBaseSearch...

Protein-protein interaction databases

IntActP14434. 1 interaction.
MINTMINT-257614.

Proteomic databases

PaxDbP14434.
PRIDEP14434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040655; ENSMUSP00000046105; ENSMUSG00000036594.
GeneID14960.
KEGGmmu:14960.

Organism-specific databases

CTD14960.
MGIMGI:95895. H2-Aa.

Phylogenomic databases

eggNOGNOG26577.
GeneTreeENSGT00560000076735.
HOGENOMHOG000112076.
HOVERGENHBG006862.
InParanoidP14434.
KOK06752.
OMATVFSKFP.
OrthoDBEOG4KWJTP.

Gene expression databases

ArrayExpressP14434.
BgeeP14434.
CleanExMM_H2-AA.
GenevestigatorP14434.
GermOnlineENSMUSG00000036594. Mus musculus.

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.
IPR001003. MHC_II_a_N.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
PF00993. MHC_II_alpha. 1 hit.
[Graphical view]
SMARTSM00407. IGc1. 1 hit.
SM00920. MHC_II_alpha. 1 hit.
[Graphical view]
SUPFAMSSF54452. MHC_I/II-like_Ag-recog. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14434.
NextBio287306.
SOURCESearch...

Entry information

Entry nameHA2B_MOUSE
AccessionPrimary (citable) accession number: P14434
Secondary accession number(s): O78195
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 30, 2000
Last modified: April 3, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families