P34056 (AP2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	437 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anterior 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 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 inner ear morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB keratinocyte development Inferred from genetic interaction PubMed 18824566. Source: MGI lens induction in camera-type eye Inferred from mutant phenotype PubMed 10571739. 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 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 neural crest cell development Inferred from mutant phenotype PubMed 8622766. 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 neuron apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of tooth mineralization Inferred from sequence or structural similarity. Source: UniProtKB regulation of neuron differentiation Inferred from mutant phenotype PubMed 10842061. Source: MGI retina layer formation Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from sequence or structural similarity. Source: UniProtKB 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_component	Golgi apparatus Inferred from electronic annotation. Source: Compara centrosome Inferred from electronic annotation. Source: Compara transcription factor complex Traceable author statement PubMed 11522791. Source: MGI
Molecular_function	RNA 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 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 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 chromatin binding Inferred from direct assay Ref.7. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 437	437	Transcription factor AP-2-alpha		PRO_0000184797
Regions
	Region	280 – 410	131	H-S-H (helix-span-helix), dimerization
	Motif	57 – 62	6	WW-binding
	Compositional bias	29 – 117	89	Gln/Pro-rich (transactivation domain)
Amino acid modifications
	Modified residue	239	1	Phosphoserine; by PKA By similarity
	Cross-link	10		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 15	15	MLWKL…YEDCE → MLVHSFSAM in isoform 3.		VSP_006402
	Alternative sequence	1 – 15	15	MLWKL…YEDCE → MNSVVVDTPYFGGLPTLGLW NGFSRVVEALRLISSSPSRL AFFQ in isoform 4.		VSP_006403
	Alternative sequence	16 – 160	145	Missing in isoform 2.		VSP_006404
Experimental info
	Sequence conflict	38	1	P → S in AAH07471. Ref.2
	Sequence conflict	139	1	A → G Ref.2
	Sequence conflict	139	1	A → G Ref.3
	Sequence conflict	158 – 159	2	DV → RL Ref.4
	Sequence conflict	390	1	Missing Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 901F456EE07AE69C	FASTA	437	47,971
	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
	Isoform 2 [UniParc]. Checksum: 6E9B01E97186E4E1	FASTA	292	31,960
	10 20 30 40 50 60 MLWKLTDNIK YEDCEHVEDP GINIPDQTVI KKGPVSLSKS NSNAVSAIPI NKDNLFGGVV 70 80 90 100 110 120 NPNEVFCSVP GRLSLLSSTS KYKVTVAEVQ RRLSPPECLN ASLLGGVLRR AKSKNGGRSL 130 140 150 160 170 180 REKLDKIGLN LPAGRRKAAN VTLLTSLVEG EAVHLARDFG YVCETEFPAK AVAEFLNRQH 190 200 210 220 230 240 SDPNEQVARK NMLLATKQIC KEFTDLLAQD RSPLGNSRPN PILEPGIQSC LTHFNLISHG 250 260 270 280 290 FGSPAVCAAV TALQNYLTEA LKAMDKMYLS NNPNSHTDNS AKSSDKEEKH RK
	Isoform 3 [UniParc]. Checksum: 7CA39A800983538C	FASTA	431	47,092
	10 20 30 40 50 60 MLVHSFSAMD RHDGTSNGTA RLPQLGTVGQ SPYTSAPPLS HTPNADFQPP YFPPPYQPIY 70 80 90 100 110 120 PQSQDPYSHV NDPYSLNPLH AQPQPQHPGW PGQRQSQESG LLHTHRGLPH QLSGLDPRRD 130 140 150 160 170 180 YRRHEDLLHG PHALGSGLGD LPIHSLPHAI EDVPHVEDPG INIPDQTVIK KGPVSLSKSN 190 200 210 220 230 240 SNAVSAIPIN KDNLFGGVVN PNEVFCSVPG RLSLLSSTSK YKVTVAEVQR RLSPPECLNA 250 260 270 280 290 300 SLLGGVLRRA KSKNGGRSLR EKLDKIGLNL PAGRRKAANV TLLTSLVEGE AVHLARDFGY 310 320 330 340 350 360 VCETEFPAKA VAEFLNRQHS DPNEQVARKN MLLATKQICK EFTDLLAQDR SPLGNSRPNP 370 380 390 400 410 420 ILEPGIQSCL THFNLISHGF GSPAVCAAVT ALQNYLTEAL KAMDKMYLSN NPNSHTDNSA 430 KSSDKEEKHR K
	Isoform 4 [UniParc]. Checksum: 49A69CBE5826B8BB	FASTA	466	50,900
	10 20 30 40 50 60 MNSVVVDTPY FGGLPTLGLW NGFSRVVEAL RLISSSPSRL AFFQDRHDGT SNGTARLPQL 70 80 90 100 110 120 GTVGQSPYTS APPLSHTPNA DFQPPYFPPP YQPIYPQSQD PYSHVNDPYS LNPLHAQPQP 130 140 150 160 170 180 QHPGWPGQRQ SQESGLLHTH RGLPHQLSGL DPRRDYRRHE DLLHGPHALG SGLGDLPIHS 190 200 210 220 230 240 LPHAIEDVPH VEDPGINIPD QTVIKKGPVS LSKSNSNAVS AIPINKDNLF GGVVNPNEVF 250 260 270 280 290 300 CSVPGRLSLL SSTSKYKVTV AEVQRRLSPP ECLNASLLGG VLRRAKSKNG GRSLREKLDK 310 320 330 340 350 360 IGLNLPAGRR KAANVTLLTS LVEGEAVHLA RDFGYVCETE FPAKAVAEFL NRQHSDPNEQ 370 380 390 400 410 420 VARKNMLLAT KQICKEFTDL LAQDRSPLGN SRPNPILEPG IQSCLTHFNL ISHGFGSPAV 430 440 450 460 CAAVTALQNY LTEALKAMDK MYLSNNPNSH TDNSAKSSDK EEKHRK

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00112753. IPI00226893. IPI00226894. IPI00226897.
PIR	S42111.
RefSeq	NP_035677.2. NM_011547.3.
UniGene	Mm.85544.
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P34056.
Proteomic databases
PRIDE	P34056.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000110193; ENSMUSP00000105822; ENSMUSG00000021359.
GeneID	21418.
KEGG	mmu:21418.
UCSC	uc007qei.1. mouse. uc011yyq.1. mouse.
Organism-specific databases
CTD	7020.
MGI	MGI:104671. Tfap2a.
Phylogenomic databases
eggNOG	NOG300693.
GeneTree	ENSGT00550000074577.
HOVERGEN	HBG002455.
InParanoid	P34056.
KO	K09176.
OrthoDB	EOG4NP73N.
Gene expression databases
ArrayExpress	P34056.
Bgee	P34056.
CleanEx	MM_TCFAP2A.
Genevestigator	P34056.
GermOnline	ENSMUSG00000021359. Mus musculus.
Family and domain databases
InterPro	IPR004979. TF_AP2. IPR008121. TF_AP2_alpha_N. IPR013854. TF_AP2_C. [Graphical view]
PANTHER	PTHR10812. PTHR10812. 1 hit.
Pfam	PF03299. TF_AP-2. 1 hit. [Graphical view]
PRINTS	PR01749. AP2ATNSCPFCT. PR01748. AP2TNSCPFCT.
ProtoNet	Search...
Other
NextBio	300724.
SOURCE	Search...

Entry information

Entry name

AP2A_MOUSE

Accession

Primary (citable) accession number: P34056
Secondary accession number(s): Q60740 , 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:	April 3, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program