Q9NXR8 (ING3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibitor of growth protein 3

Alternative name(s):
p47ING3

Gene names

Name:	ING3
ORF Names:	HSPC301

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	418 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Ref.1 Ref.10
Subunit structure	Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Nucleus.
Tissue specificity	Expressed in brain, heart, kidney, liver, lung, ovaries, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus.
Domain	The PHD-type zinc finger mediates the binding to H3K4me3. Ref.12 Ref.13
Involvement in disease	Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.15
Sequence similarities	Belongs to the ING family. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence AAF28979.1 differs from that shown. Reason: Frameshift at position 90. The sequence AAH73865.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Growth regulation Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	histone H2A acetylation Inferred from direct assay Ref.10Ref.11. Source: UniProtKB histone H4 acetylation Inferred from direct assay Ref.10Ref.11. Source: UniProtKB positive regulation of apoptotic process Inferred from direct assay Ref.11. Source: UniProtKB regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Piccolo NuA4 histone acetyltransferase complex Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	methylated histone residue binding Inferred from direct assay Ref.12Ref.13. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NXR8-1)

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: Q9NXR8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     90-92: VDR → QHF
     93-418: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 3 (identifier: Q9NXR8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     90-93: VDRH → DLWN
     94-418: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 418

418

Inhibitor of growth protein 3

PRO_0000212665

Regions

Zinc finger

360 – 409

50

PHD-type

Compositional bias

313 – 329

17

Poly-Ser

Sites

Binding site

362

1

Histone H3K4me3 By similarity

Binding site

373

1

Histone H3K4me3 By similarity

Binding site

377

1

Histone H3K4me3 By similarity

Binding site

385

1

Histone H3K4me3 By similarity

Amino acid modifications

Modified residue

264

1

N6-acetyllysine Ref.14

Natural variations

Alternative sequence

90 – 93

4

VDRH → DLWN in isoform 3.

VSP_012887

Alternative sequence

90 – 92

3

VDR → QHF in isoform 2.

VSP_012885

Alternative sequence

93 – 418

326

Missing in isoform 2.

VSP_012886

Alternative sequence

94 – 418

325

Missing in isoform 3.

VSP_012888

Natural variant

20

1

D → G in HNSCC. Ref.15

VAR_021263

Experimental info

Sequence conflict

325

1

C → S Ref.2

Sequence conflict

325

1

C → S Ref.3

Sequence conflict

367

1

Q → QV in CAC48260. Ref.5

Sequence conflict

380

1

Missing in CAC48260. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

418

Helix Strand Turn

Details...

Beta strand

371 – 374

4

Helix

388 – 391

4

Helix

404 – 414

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: AA127416912D87F5	FASTA	418	46,743
	10 20 30 40 50 60 MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA KKNKPEWREE 70 80 90 100 110 120 QMASIKKDYY KALEDADEKV QLANQIYDLV DRHLRKLDQE LAKFKMELEA DNAGITEILE 130 140 150 160 170 180 RRSLELDTPS QPVNNHHAHS HTPVEKRKYN PTSHHTTTDH IPEKKFKSEA LLSTLTSDAS 190 200 210 220 230 240 KENTLGCRNN NSTASSNNAY NVNSSQPLGS YNIGSLSSGT GAGAITMAAA QAVQATAQMK 250 260 270 280 290 300 EGRRTSSLKA SYEAFKNNDF QLGKEFSMAR ETVGYSSSSA LMTTLTQNAS SSAADSRSGR 310 320 330 340 350 360 KSKNNNKSSS QQSSSSSSSS SLSSCSSSST VVQEISQQTT VVPESDSNSQ VDWTYDPNEP 370 380 390 400 410 RYCICNQVSY GEMVGCDNQD CPIEWFHYGC VGLTEAPKGK WYCPQCTAAM KRRGSRHK
	Isoform 2 [UniParc]. Checksum: EC143EFFA9888741	FASTA	92	11,333
	10 20 30 40 50 60 MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA KKNKPEWREE 70 80 90 QMASIKKDYY KALEDADEKV QLANQIYDLQ HF
	Isoform 3 [UniParc]. Checksum: 0966A2E28FA98887	FASTA	93	11,449
	10 20 30 40 50 60 MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA KKNKPEWREE 70 80 90 QMASIKKDYY KALEDADEKV QLANQIYDLD LWN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel PHD-finger motif protein, p47ING3, modulates p53-mediated transcription, cell cycle control, and apoptosis." Nagashima M., Shiseki M., Pedeux R.M., Okamura S., Kitahama-Shiseki M., Miura K., Yokota J., Harris C.C. Oncogene 22:343-350(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ROLE IN P53 MEDIATED GROWTH SUPPRESSION.
[2]	"Cloning and characterization of p47ING3, a new member of the p33ING1 family of p53 regulators." Zenklusen J.C., Green E.D. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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 AND 3). Tissue: Skeletal muscle.
[4]	"Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Umbilical cord blood.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 2 AND 3). Tissue: Blood, Liver, Lung, Pancreas and Urinary bladder.
[8]	"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex." Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W. J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 80-92, IDENTIFICATION IN NUA4 COMPLEX, MASS SPECTROMETRY.
[9]	"The highly conserved and multifunctional NuA4 HAT complex." Doyon Y., Cote J. Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON NUA4 COMPLEX.
[10]	"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans." Doyon Y., Selleck W., Lane W.S., Tan S., Cote J. Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX.
[11]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN NUA4 COMPLEX.
[12]	"ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression." Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., Carney D., Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., Davrazou F., Saha A., Cairns B.R., Ayer D.E., Kutateladze T.G., Shi Y. , Cote J., Chua K.F., Gozani O. Nature 442:96-99(2006) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN PHD-TYPE ZINC FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
[13]	"Arabidopsis ING and Alfin1-like protein families localize to the nucleus and bind to H3K4me3/2 via plant homeodomain fingers." Lee W.Y., Lee D., Chung W.I., Kwon C.S. Plant J. 58:511-524(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN PHD-TYPE ZINC FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, MASS SPECTROMETRY.
[15]	"Allelic loss and reduced expression of the ING3, a candidate tumor suppressor gene at 7q31, in human head and neck cancers." Gunduz M., Ouchida M., Fukushima K., Ito S., Jitsumori Y., Nakashima T., Nagai N., Nishizaki K., Shimizu K. Oncogene 21:4462-4470(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HNSCC GLY-20.
[16]	"Solution structure of PHD domain in inhibitor of growth protein 3 (ING3) antigen 7." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 362-418.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF074968 mRNA. Translation: AAG12172.1.
AY007790 mRNA. Translation: AAG23285.1.
AK000096 mRNA. Translation: BAA90942.1.
AK291905 mRNA. Translation: BAF84594.1.
AF161419 mRNA. Translation: AAF28979.1. Frameshift.
AL603623 Transcribed RNA. Translation: CAC48260.2.
AC004537 Genomic DNA. Translation: AAQ93373.1.
BC009777 mRNA. Translation: AAH09777.1.
BC009777 mRNA. Translation: AAQ93374.1.
BC010851 mRNA. Translation: AAH10851.1.
BC062634 mRNA. Translation: AAH09776.1.
BC062634 mRNA. Translation: AAH62634.1.
BC073865 mRNA. Translation: AAH73865.1. Sequence problems.
BC093091 mRNA. Translation: AAH93091.1.
BC093689 mRNA. Translation: AAH93689.1.
BC101609 mRNA. Translation: AAI01610.1.

IPI

IPI00387159.
IPI00413787.
IPI00478624.

RefSeq

NP_061944.2. NM_019071.2.
NP_938008.1. NM_198267.1.

UniGene

Hs.489811.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X4I	NMR	-	A	362-418	[»]

ProteinModelPortal

Q9NXR8.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NXR8. 4 interactions.

PTM databases

PhosphoSite

Q9NXR8.

Polymorphism databases

DMDM

59798432.

Proteomic databases

PaxDb

Q9NXR8.

PRIDE

Q9NXR8.

Protocols and materials databases

DNASU

54556.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000315870; ENSP00000320566; ENSG00000071243.
ENST00000339121; ENSP00000341697; ENSG00000071243.
ENST00000427726; ENSP00000410406; ENSG00000071243.
ENST00000445699; ENSP00000395719; ENSG00000071243.

GeneID

54556.

KEGG

hsa:54556.

UCSC

uc003vjm.1. human.
uc003vjn.3. human.

Organism-specific databases

CTD

54556.

GeneCards

GC07P120590.

HGNC

HGNC:14587. ING3.

MIM

275355. phenotype.
607493. gene.

neXtProt

NX_Q9NXR8.

Orphanet

67037. Squamous cell carcinoma of head and neck.

PharmGKB

PA29875.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5034.

HOVERGEN

HBG006607.

InParanoid

Q9NXR8.

KO

K11319.

OMA

NNQVDWT.

OrthoDB

EOG4H19WB.

PhylomeDB

Q9NXR8.

Gene expression databases

ArrayExpress

Q9NXR8.

Bgee

Q9NXR8.

CleanEx

HS_ING3.

Genevestigator

Q9NXR8.

GermOnline

ENSG00000071243. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR024610. ING_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]

SMART

SM00249. PHD. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ING3. human.

EvolutionaryTrace

Q9NXR8.

GenomeRNAi

54556.

NextBio

57036.

SOURCE

Search...

Entry information

Entry name

ING3_HUMAN

Accession

Primary (citable) accession number: Q9NXR8
Secondary accession number(s): A8K790 , O60394, Q567P3, Q6GMT3, Q7Z762, Q969G0, Q96DT4, Q9HC99, Q9P081

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 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.