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P34056 (AP2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor AP-2-alpha

Short name=AP2-alpha
Alternative name(s):
AP-2 transcription factor
Activating enhancer-binding protein 2-alpha
Activator protein 2
Short name=AP-2
Gene names
Name:Tfap2a
Synonyms:Ap2tf, Tcfap2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region. Ref.7

Subunit structure

Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with WWOX. Interacts with UBE2I. Interacts with RALBP1 in a complex also containing EPN1 and NUMB during interphase and mitosis By similarity. Interacts with CITED4. Interacts with KCTD1; this interaction represses transcription activation. Interacts (via C-terminus) with CITED2 (via C-terminus); the interaction stimulates TFAP2A-transcriptional activation. Interacts (via N-terminus) with EP300 (via N-terminus); the interaction requires CITED2 By similarity. Interacts with KCTD15; this interaction inhibits TFAP2A transcriptional activation By similarity. Ref.6

Subcellular location

Nucleus.

Developmental stage

Expressed in the embryonic heart. Expressed from embryo day 9.5 to birth. At day 12.5, expressed in the midbrain, hindbrain, spinal cord, sensory ganglia, epidermis, nephric system and limbs. At mid-embryogenesis, isoform 3 is the most abundant form in the nervous system and total embryo, but the least abundant form in the epidermis. In adults, AP-2A is expressed in the eye, skin, kidney, prostate, thymus, skeletal muscle and very weakly, in the brain. Highest expression found in skin and eye. Ref.7

Induction

All isoforms are induced during retinoic acid-mediated differentiation and by cAMP stimulation of primary astrocytes. Isoform 3 is most strongly induced in the former case, isoform 1 in the latter case.

Domain

The WW-binding motif mediates interaction with WWOX By similarity.

Post-translational modification

Sumoylated on Lys-10; which inhibits transcriptional activity By similarity.

Sequence similarities

Belongs to the AP-2 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior neuropore closure

Inferred from mutant phenotype PubMed 8622765. Source: MGI

basement membrane organization

Inferred from mutant phenotype PubMed 16186342. Source: MGI

bone morphogenesis

Inferred from mutant phenotype PubMed 8622766. Source: UniProtKB

cellular response to iron ion

Inferred from sequence or structural similarity. Source: UniProtKB

cornea development in camera-type eye

Inferred from mutant phenotype PubMed 16186342. Source: MGI

embryonic body morphogenesis

Inferred from mutant phenotype PubMed 15013802. Source: MGI

embryonic camera-type eye morphogenesis

Inferred from mutant phenotype PubMed 9811866. Source: MGI

embryonic cranial skeleton morphogenesis

Inferred from mutant phenotype PubMed 8622766. Source: UniProtKB

embryonic forelimb morphogenesis

Inferred from mutant phenotype PubMed 9811866. Source: UniProtKB

embryonic pattern specification

Inferred from mutant phenotype PubMed 17984226. Source: MGI

epidermis morphogenesis

Inferred from mutant phenotype PubMed 16449191. Source: MGI

eyelid development in camera-type eye

Inferred from mutant phenotype PubMed 9811866. Source: UniProtKB

face morphogenesis

Inferred from mutant phenotype PubMed 9811866. Source: MGI

forebrain neuron development

Inferred from mutant phenotype PubMed 10803593. Source: MGI

forelimb morphogenesis

Inferred from mutant phenotype PubMed 9811866. Source: MGI

inner ear morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

keratinocyte development

Inferred from genetic interaction PubMed 18824566. Source: MGI

kidney development

Inferred from sequence or structural similarity. Source: UniProtKB

lens induction in camera-type eye

Inferred from mutant phenotype PubMed 10571739. Source: MGI

lens morphogenesis in camera-type eye

Inferred from mutant phenotype PubMed 18224708PubMed 9918694. Source: MGI

metanephric nephron development

Inferred from expression pattern PubMed 7555706. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 16449191. Source: MGI

negative regulation of epidermal growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 16449191. Source: MGI

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 21539825. Source: MGI

negative regulation of reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription by competitive promoter binding

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21829553. Source: UniProtKB

nervous system development

Inferred from expression pattern PubMed 7555706. Source: UniProtKB

neural crest cell development

Inferred from mutant phenotype PubMed 8622766. Source: MGI

neural tube closure

Inferred from mutant phenotype PubMed 8622766PubMed 9811866. Source: MGI

oculomotor nerve formation

Inferred from mutant phenotype PubMed 8622766. Source: UniProtKB

optic cup structural organization

Inferred from mutant phenotype PubMed 20150232. Source: UniProtKB

optic vesicle morphogenesis

Inferred from mutant phenotype PubMed 20150232. Source: UniProtKB

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 11744375. Source: MGI

palate development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of bone mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype PubMed 19463168. Source: MGI

positive regulation of gene expression

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of tooth mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19750005. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of neuron differentiation

Inferred from mutant phenotype PubMed 10842061. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11522791. Source: MGI

retina layer formation

Inferred from electronic annotation. Source: Ensembl

sensory organ development

Inferred from expression pattern PubMed 7555706. Source: UniProtKB

sensory perception of sound

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 8622765. Source: MGI

skin development

Inferred from expression pattern PubMed 7555706. Source: UniProtKB

sympathetic nervous system development

Inferred from genetic interaction PubMed 21539825. Source: MGI

trigeminal nerve development

Inferred from mutant phenotype PubMed 8622766. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 10842061PubMed 16449191PubMed 18224708PubMed 18723448PubMed 18824566. Source: MGI

transcription factor complex

Traceable author statement PubMed 11522791. Source: MGI

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 19750005. Source: UniProtKB

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 17670746. Source: MGI

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 10068641. Source: MGI

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 9858544. Source: NTNU_SB

RNA polymerase II transcription coactivator activity

Inferred from direct assay PubMed 21829553. Source: UniProtKB

RNA polymerase II transcription corepressor activity

Inferred from direct assay PubMed 21829553. Source: UniProtKB

RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 9858544. Source: NTNU_SB

chromatin binding

Inferred from direct assay Ref.7. Source: UniProtKB

core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 19943855. Source: MGI

protein binding

Inferred from physical interaction PubMed 11522791. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11522791Ref.7. Source: MGI

transcription coactivator activity

Inferred from direct assay PubMed 7555706. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P34056-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P34056-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-160: Missing.
Isoform 3 (identifier: P34056-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MLWKLTDNIKYEDCE → MLVHSFSAM
Isoform 4 (identifier: P34056-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MLWKLTDNIKYEDCE → MNSVVVDTPYFGGLPTLGLWNGFSRVVEALRLISSSPSRLAFFQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Transcription factor AP-2-alpha
PRO_0000184797

Regions

Region280 – 410131H-S-H (helix-span-helix), dimerization
Motif57 – 626WW-binding
Compositional bias29 – 11789Gln/Pro-rich (transactivation domain)

Amino acid modifications

Modified residue2391Phosphoserine; by PKA By similarity
Cross-link10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 1515MLWKL…YEDCE → MLVHSFSAM in isoform 3.
VSP_006402
Alternative sequence1 – 1515MLWKL…YEDCE → MNSVVVDTPYFGGLPTLGLW NGFSRVVEALRLISSSPSRL AFFQ in isoform 4.
VSP_006403
Alternative sequence16 – 160145Missing in isoform 2.
VSP_006404

Experimental info

Sequence conflict381P → S in AAH07471. Ref.2
Sequence conflict1391A → G Ref.2
Sequence conflict1391A → G Ref.3
Sequence conflict158 – 1592DV → RL Ref.4
Sequence conflict3901Missing Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 901F456EE07AE69C

FASTA43747,971
        10         20         30         40         50         60 
MLWKLTDNIK YEDCEDRHDG TSNGTARLPQ LGTVGQSPYT SAPPLSHTPN ADFQPPYFPP 

        70         80         90        100        110        120 
PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR QSQESGLLHT HRGLPHQLSG 

       130        140        150        160        170        180 
LDPRRDYRRH EDLLHGPHAL GSGLGDLPIH SLPHAIEDVP HVEDPGINIP DQTVIKKGPV 

       190        200        210        220        230        240 
SLSKSNSNAV SAIPINKDNL FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP 

       250        260        270        280        290        300 
PECLNASLLG GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGEAVHL 

       310        320        330        340        350        360 
ARDFGYVCET EFPAKAVAEF LNRQHSDPNE QVARKNMLLA TKQICKEFTD LLAQDRSPLG 

       370        380        390        400        410        420 
NSRPNPILEP GIQSCLTHFN LISHGFGSPA VCAAVTALQN YLTEALKAMD KMYLSNNPNS 

       430 
HTDNSAKSSD KEEKHRK 

« Hide

Isoform 2 [UniParc].

Checksum: 6E9B01E97186E4E1
Show »

FASTA29231,960
Isoform 3 [UniParc].

Checksum: 7CA39A800983538C
Show »

FASTA43147,092
Isoform 4 [UniParc].

Checksum: 49A69CBE5826B8BB
Show »

FASTA46650,900

References

« Hide 'large scale' references
[1]"The complete murine cDNA sequence of the transcription factor AP-2."
Moser M., Pscherer A., Bauer R., Imhof A., Seegers S., Kerscher M., Buettner R.
Nucleic Acids Res. 21:4844-4844(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NIH Swiss.
[2]"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].
[3]"Alternative mRNAs encode multiple isoforms of transcription factor AP-2 during murine embryogenesis."
Meier P., Koedood M., Philipp J., Fontana A., Mitchell P.J.
Dev. Biol. 169:1-14(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-279, ALTERNATIVE SPLICING.
Strain: 129/4 and ICR.
Tissue: Embryo.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-437.
Strain: C57BL/6J.
Tissue: Embryonic head.
[5]"Transcription factor AP-2 is expressed in neural crest cell lineages during mouse embryogenesis."
Mitchell P.J., Timmons P.M., Hebert J.M., Rigby P.W.J., Tjian R.
Genes Dev. 5:105-119(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 259-437.
[6]"Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding transcriptional coactivators: induced expression in mammary epithelial cells."
Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T., Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S., Shioda T.
Genomics 80:601-613(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CITED4.
[7]"Cited2 controls left-right patterning and heart development through a Nodal-Pitx2c pathway."
Bamforth S.D., Braganca J., Farthing C.R., Schneider J.E., Broadbent C., Michell A.C., Clarke K., Neubauer S., Norris D., Brown N.A., Anderson R.H., Bhattacharya S.
Nat. Genet. 36:1189-1196(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH CHROMATIN, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74216 mRNA. Translation: CAA52292.1.
BC018226 mRNA. Translation: AAH18226.1.
BC007471 mRNA. Translation: AAH07471.1.
U17285 mRNA. Translation: AAA85681.1.
U17291, U17289 Genomic DNA. Translation: AAA85678.1.
U17286 mRNA. Translation: AAA85682.1.
U17287 mRNA. Translation: AAA85683.1.
U17291, U17290 Genomic DNA. Translation: AAA85679.1.
U17288 mRNA. Translation: AAA85684.1.
U17291 Genomic DNA. Translation: AAA85680.1.
AK013900 mRNA. Translation: BAB29047.1.
X57012 mRNA. Translation: CAA40331.1.
CCDSCCDS26467.1. [P34056-1]
CCDS49243.1. [P34056-3]
PIRS42111.
RefSeqNP_035677.2. NM_011547.3.
UniGeneMm.85544.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204011. 7 interactions.

PTM databases

PhosphoSiteP34056.

Proteomic databases

MaxQBP34056.
PRIDEP34056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000110193; ENSMUSP00000105822; ENSMUSG00000021359.
GeneID21418.
KEGGmmu:21418.
UCSCuc007qei.1. mouse. [P34056-4]
uc011yyq.1. mouse. [P34056-2]

Organism-specific databases

CTD7020.
MGIMGI:104671. Tfap2a.

Phylogenomic databases

eggNOGNOG300693.
GeneTreeENSGT00550000074577.
HOVERGENHBG002455.
InParanoidP34056.
KOK09176.
OrthoDBEOG7HHWS1.
PhylomeDBP34056.
TreeFamTF313718.

Gene expression databases

BgeeP34056.
CleanExMM_TCFAP2A.
GenevestigatorP34056.

Family and domain databases

InterProIPR004979. TF_AP2.
IPR008121. TF_AP2_alpha_N.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERPTHR10812. PTHR10812. 1 hit.
PfamPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSPR01749. AP2ATNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNetSearch...

Other

NextBio300724.
PROP34056.
SOURCESearch...

Entry information

Entry nameAP2A_MOUSE
AccessionPrimary (citable) accession number: P34056
Secondary accession number(s): Q60740 expand/collapse secondary AC list , Q60741, Q60742, Q60743, Q62067, Q62068, Q62069, Q91VX0, Q9CRY4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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