Q9H7X0 (NAA60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-alpha-acetyltransferase 60
EC=2.3.1.48
EC=2.3.1.88

Alternative name(s):
Histone acetyltransferase type B protein 4
Short name=HAT4
N-acetyltransferase 15
NatF catalytic subunit

Gene names

Name:	NAA60
Synonyms:	HAT4, NAT15
ORF Names:	UNQ2771/PRO7155

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	242 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone acetyltransferase localized in the Golgi apparatus that mediates acetylation of free histone H4, thereby facilitating nucleosome assembly. Has a preference for free histone H4 'Lys-20'(H4K20ac), 'Lys-79'(H4K79ac) and 'Lys-91' (H4K91ac). Also displays alpha (N-terminal) acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. Ref.8 Ref.9
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA. Ref.8 Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.8
Subcellular location	Golgi apparatus membrane Ref.8.
Induction	Isoform 2 is imprinted. Promoter methylation of the paternal allele may restrict expression to the maternal allele in placenta and leukocytes. Isoform 1 is biallelically expressed. Ref.7
Post-translational modification	Acetylated: autoacetylation is required for optimal acetyltransferase activity.
Sequence similarities	Belongs to the acetyltransferase family. NAA60 subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Chromosome partition
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Molecular function	Acyltransferase Chromatin regulator Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal peptidyl-methionine acetylation Inferred from direct assay Ref.9. Source: UniProtKB cell proliferation Inferred from mutant phenotype Ref.8. Source: UniProtKB chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB nucleosome assembly Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	Golgi membrane Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	H4 histone acetyltransferase activity Inferred from direct assay Ref.8. Source: UniProtKB peptide alpha-N-acetyltransferase activity Inferred from direct assay Ref.9Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H7X0-1)

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: Q9H7X0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MTEVVPSSAL...KHLCGDWFPI → MFPRRRTERR...ASLSWEKSSR

Note: In placenta and leukocytes, expressed from the maternal allele, due to imprinting of the paternal allele.

Isoform 3 (identifier: Q9H7X0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Note: Produced by alternative splicing. No experimental confirmation available.

Isoform 4 (identifier: Q9H7X0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     113-242: GSLLLESLKD...KSGIEYSRTM → ESTARPTACS...SVFCKELPAI

Note: Produced by alternative splicing. No experimental confirmation available.

Isoform 5 (identifier: Q9H7X0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     113-242: GSLLLESLKD...KSGIEYSRTM → EPHGLHPAPG...PPAEPAFLSI

Note: Produced by alternative splicing. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 242	242	N-alpha-acetyltransferase 60		PRO_0000321566
Regions
	Domain	13 – 182	170	N-acetyltransferase
Amino acid modifications
	Modified residue	79	1	N6-acetyllysine; by autocatalysis Ref.8
	Modified residue	105	1	N6-acetyllysine; by autocatalysis Ref.8
	Modified residue	109	1	N6-acetyllysine; by autocatalysis Probable
	Modified residue	121	1	N6-acetyllysine; by autocatalysis Probable
	Modified residue	156	1	N6-acetyllysine; by autocatalysis Ref.8
Natural variations
	Alternative sequence	1 – 65	65	Missing in isoform 3.		VSP_044122
	Alternative sequence	1 – 36	36	MTEVV…DWFPI → MFPRRRTERRLGDTGTRKKI AYRKAVPGGRKCGASLSWEK SSR in isoform 2.		VSP_044123
	Alternative sequence	113 – 242	130	GSLLL…YSRTM → ESTARPTACSAASCHGRASL PRVASSTAGPCDVGWAAATR PHPSAARRARLPVHLTPSVF CKELPAI in isoform 4.		VSP_044124
	Alternative sequence	113 – 242	130	GSLLL…YSRTM → EPHGLHPAPGLCTSQPEPLL HSAQSLPPGPQPALQLPAMV GHLFQEWHRVQPDHVMSAGQ PPPGPTLRPPAEPAFLSI in isoform 5.		VSP_044125
	Natural variant	218	1	H → Q. Corresponds to variant rs34464545 [ dbSNP | Ensembl ].		VAR_060995
Experimental info
	Mutagenesis	79	1	K → R: Decreased histone acetyltransferase activity; when associated with R-105, R-109, R-121 and R-156. Ref.8
	Mutagenesis	105	1	K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-109, R-121 and R-156. Ref.8
	Mutagenesis	109	1	K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-121 and R-156. Ref.8
	Mutagenesis	111	1	G → A: Abolishes histone acetyltransferase activity. Ref.8
	Mutagenesis	121	1	K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-109 and R-156. Ref.8
	Mutagenesis	156	1	K → R: Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-109 and R-121. Ref.8
	Sequence conflict	87	1	S → T in AAQ88907. Ref.1
	Sequence conflict	242	1	M → I in CAG33605. Ref.3
Isoform 5:
	Sequence conflict	180	1	R → Q in BAG60760. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 11234F2C51DF55DE	FASTA	242	27,451
	10 20 30 40 50 60 MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR 70 80 90 100 110 120 GAIVGMIVAE IKNRTKIHKE DGDILASNFS VDTQVAYILS LGVVKEFRKH GIGSLLLESL 130 140 150 160 170 180 KDHISTTAQD HCKAIYLHVL TTNNTAINFY ENRDFKQHHY LPYYYSIRGV LKDGFTYVLY 190 200 210 220 230 240 INGGHPPWTI LDYIQHLGSA LASLSPCSIP HRVYRQAHSL LCSFLPWSGI SSKSGIEYSR TM
	Isoform 2 [UniParc]. Checksum: E049FDCDA8FD6ECC	FASTA	249	28,375
	10 20 30 40 50 60 MFPRRRTERR LGDTGTRKKI AYRKAVPGGR KCGASLSWEK SSREYPDSWY RDITSNKKFF 70 80 90 100 110 120 SLAATYRGAI VGMIVAEIKN RTKIHKEDGD ILASNFSVDT QVAYILSLGV VKEFRKHGIG 130 140 150 160 170 180 SLLLESLKDH ISTTAQDHCK AIYLHVLTTN NTAINFYENR DFKQHHYLPY YYSIRGVLKD 190 200 210 220 230 240 GFTYVLYING GHPPWTILDY IQHLGSALAS LSPCSIPHRV YRQAHSLLCS FLPWSGISSK SGIEYSRTM
	Isoform 3 [UniParc]. Checksum: 32C31E8C2E777D5D	FASTA	177	20,103
	10 20 30 40 50 60 MIVAEIKNRT KIHKEDGDIL ASNFSVDTQV AYILSLGVVK EFRKHGIGSL LLESLKDHIS 70 80 90 100 110 120 TTAQDHCKAI YLHVLTTNNT AINFYENRDF KQHHYLPYYY SIRGVLKDGF TYVLYINGGH 130 140 150 160 170 PPWTILDYIQ HLGSALASLS PCSIPHRVYR QAHSLLCSFL PWSGISSKSG IEYSRTM
	Isoform 4 [UniParc]. Checksum: 806EE0412C45F54C	FASTA	179	19,493
	10 20 30 40 50 60 MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR 70 80 90 100 110 120 GAIVGMIVAE IKNRTKIHKE DGDILASNFS VDTQVAYILS LGVVKEFRKH GIESTARPTA 130 140 150 160 170 CSAASCHGRA SLPRVASSTA GPCDVGWAAA TRPHPSAARR ARLPVHLTPS VFCKELPAI
	Isoform 5 [UniParc]. Checksum: C82D743C3A3F0776	FASTA	190	20,911
	10 20 30 40 50 60 MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR 70 80 90 100 110 120 GAIVGMIVAE IKNRTKIHKE DGDILASNFS VDTQVAYILS LGVVKEFRKH GIEPHGLHPA 130 140 150 160 170 180 PGLCTSQPEP LLHSAQSLPP GPQPALQLPA MVGHLFQEWH RVQPDHVMSA GQPPPGPTLR 190 PPAEPAFLSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5). Tissue: Fetal brain, Mesangial cell, Teratocarcinoma and Testis.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1). Tissue: Brain.
[7]	"Methylation screening of reciprocal genome-wide UPDs identifies novel human-specific imprinted genes." Nakabayashi K., Trujillo A.M., Tayama C., Camprubi C., Yoshida W., Lapunzina P., Sanchez A., Soejima H., Aburatani H., Nagae G., Ogata T., Hata K., Monk D. Hum. Mol. Genet. 20:3188-3197(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IMPRINTING, INDUCTION.
[8]	"HAT4, a Golgi apparatus-anchored B-type histone acetyltransferase, acetylates free histone H4 and facilitates chromatin assembly." Yang X., Yu W., Shi L., Sun L., Liang J., Yi X., Li Q., Zhang Y., Yang F., Han X., Zhang D., Yang J., Yao Z., Shang Y. Mol. Cell 44:39-50(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-79; LYS-105; LYS-109; LYS-121 AND LYS-156, MUTAGENESIS OF LYS-79; LYS-105; LYS-109; GLY-111; LYS-121 AND LYS-156.
[9]	"NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation." Van Damme P., Hole K., Pimenta-Marques A., Helsens K., Vandekerckhove J., Martinho R.G., Gevaert K., Arnesen T. PLoS Genet. 7:E1002169-E1002169(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY358543 mRNA. Translation: AAQ88907.1. AK024216 mRNA. Translation: BAB14853.1. AK092005 mRNA. Translation: BAG52462.1. AK297219 mRNA. Translation: BAG59702.1. AK298566 mRNA. Translation: BAG60760.1. AK302361 mRNA. Translation: BAG63686.1. CR457324 mRNA. Translation: CAG33605.1. AC004224 Genomic DNA. No translation available. AC025283 Genomic DNA. No translation available. CH471112 Genomic DNA. Translation: EAW85358.1. CH471112 Genomic DNA. Translation: EAW85359.1. CH471112 Genomic DNA. Translation: EAW85360.1. CH471112 Genomic DNA. Translation: EAW85361.1. CH471112 Genomic DNA. Translation: EAW85362.1. CH471112 Genomic DNA. Translation: EAW85363.1. CH471112 Genomic DNA. Translation: EAW85364.1. BC011267 mRNA. Translation: AAH11267.1.
IPI	IPI00155437.
RefSeq	NP_001077069.1. NM_001083600.1. NP_001077070.1. NM_001083601.1. NP_079121.1. NM_024845.2.
UniGene	Hs.513296.
3D structure databases
ProteinModelPortal	Q9H7X0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000385903.
PTM databases
PhosphoSite	Q9H7X0.
Polymorphism databases
DMDM	74733721.
Proteomic databases
PaxDb	Q9H7X0.
PRIDE	Q9H7X0.
Protocols and materials databases
DNASU	79903.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360862; ENSP00000354108; ENSG00000122390. ENST00000407558; ENSP00000385903; ENSG00000122390. ENST00000414063; ENSP00000393224; ENSG00000122390. ENST00000421765; ENSP00000405873; ENSG00000122390. ENST00000424546; ENSP00000401237; ENSG00000122390. ENST00000570819; ENSP00000460763; ENSG00000122390. ENST00000572584; ENSP00000459057; ENSG00000122390. ENST00000572942; ENSP00000461730; ENSG00000122390. ENST00000573580; ENSP00000459055; ENSG00000122390. ENST00000575076; ENSP00000458667; ENSG00000122390.
GeneID	79903.
KEGG	hsa:79903.
UCSC	uc002cvg.2. human.
Organism-specific databases
CTD	79903.
GeneCards	GC16P003495.
H-InvDB	HIX0012768. HIX0173265.
HGNC	HGNC:25875. NAA60.
HPA	HPA040916.
MIM	614246. gene.
neXtProt	NX_Q9H7X0.
PharmGKB	PA164723438.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG276305.
HOGENOM	HOG000280717.
HOVERGEN	HBG061680.
InParanoid	Q9H7X0.
OMA	PPWTILI.
OrthoDB	EOG45TCNW.
Gene expression databases
ArrayExpress	Q9H7X0.
Bgee	Q9H7X0.
CleanEx	HS_NAT15.
Genevestigator	Q9H7X0.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GNAT_dom. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NAA60. human.
GenomeRNAi	79903.
NextBio	69755.
SOURCE	Search...

Entry information

Entry name

NAA60_HUMAN

Accession

Primary (citable) accession number: Q9H7X0
Secondary accession number(s): B3KRQ0 , B4DLZ0, B4DPZ8, B4DYC4, D3DUC2, E7EQ65, Q6IA31, Q6UX26

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.