P78317 (RNF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF4
EC=6.3.2.-

Alternative name(s):
RING finger protein 4
Small nuclear ring finger protein
Short name=Protein SNURF

Gene names

Name:	RNF4
Synonyms:	SNURF
ORF Names:	RES4-26

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

General annotation (Comments)

Function	E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation. Ref.7 Ref.9 Ref.12 Ref.14 Ref.15 Ref.16
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Homodimer (via RING-type zinc finger domain). Interacts with GSC2 By similarity. Interacts with AR/the androgen receptor and TBP By similarity. Interacts with TCF20 By similarity. Interacts with PATZ1. Interacts with TRPS1; negatively regulates TRPS1 transcriptional repressor activity. Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent. Interacts with PARP1. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6). Ref.6 Ref.7 Ref.8 Ref.11 Ref.15 Ref.17
Subcellular location	Cytoplasm. Nucleus. Nucleus › PML body. Nucleus › nucleoplasm Ref.7 Ref.8 Ref.15.
Tissue specificity	Widely expressed at low levels in many tissues; highly expressed in testis. Ref.2
Domain	The RING-type zinc finger domain is required for the ubiquitination of polysumoylated substrates By similarity.
Post-translational modification	Sumoylated; conjugated by one or two SUMO1 moieties By similarity. Autoubiquitinated By similarity.
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.7. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.9Ref.14Ref.15. Source: UniProtKB protein K11-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K48-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K6-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K63-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein autoubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of kinetochore assembly Inferred from mutant phenotype Ref.14. Source: UniProtKB regulation of spindle assembly Inferred from mutant phenotype Ref.14. Source: UniProtKB response to arsenic-containing substance Inferred from direct assay Ref.15. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB SUMO polymer binding Inferred from sequence or structural similarity. Source: UniProtKB androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB nucleosome binding Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 9710597. Source: ProtInc transcription coactivator activity Non-traceable author statement PubMed 15572661. Source: UniProtKB ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Traceable author statement PubMed 9710597. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P78317-1)

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: P78317-2)

The sequence of this isoform differs from the canonical sequence as follows:
     72-113: ERRRPRRNAR...RDVYVTTHTP → GPQVLSVVPS...SSVASASVIP
     114-190: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 190

190

E3 ubiquitin-protein ligase RNF4

PRO_0000056043

Regions

Zinc finger

132 – 177

46

RING-type

Region

1 – 16

16

Required for ubiquitination activity By similarity

Region

4 – 61

58

Mediates interaction with TRPS1 By similarity

Motif

36 – 39

4

SUMO interaction motif 1; mediates the binding to polysumoylated substrates

Motif

46 – 49

4

SUMO interaction motif 2; mediates the binding to polysumoylated substrates

Motif

57 – 59

3

SUMO interaction motif 3; mediates the binding to polysumoylated substrates

Motif

67 – 70

4

SUMO interaction motif 4; mediates the binding to polysumoylated substrates

Amino acid modifications

Modified residue

94

1

Phosphoserine Ref.10 Ref.13

Modified residue

95

1

Phosphoserine Ref.10 Ref.13

Natural variations

Alternative sequence

72 – 113

42

ERRRP…TTHTP → GPQVLSVVPSAWTDTQRSCR MDVSSFPQNAAMSSVASASV IP in isoform 2.

VSP_045789

Alternative sequence

114 – 190

77

Missing in isoform 2.

VSP_045790

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

190

Helix Strand Turn

Details...

Turn

133 – 135

3

Helix

139 – 144

6

Beta strand

149 – 152

4

Beta strand

153 – 155

3

Beta strand

157 – 159

3

Helix

160 – 169

10

Turn

174 – 176

3

Turn

181 – 183

3

Beta strand

185 – 187

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: E5E3AE4A9B28CF9D	FASTA	190	21,319
	10 20 30 40 50 60 MSTRKRRGGA INSRQAQKRT REATSTPEIS LEAEPIELVE TAGDEIVDLT CESLEPVVVD 70 80 90 100 110 120 LTHNDSVVIV DERRRPRRNA RRLPQDHADS CVVSSDDEEL SRDRDVYVTT HTPRNARDEG 130 140 150 160 170 180 ATGLRPSGTV SCPICMDGYS EIVQNGRLIV STECGHVFCS QCLRDSLKNA NTCPTCRKKI 190 NHKRYHPIYI
	Isoform 2 [UniParc]. Checksum: C65BF8B284670597	FASTA	113	12,126
	10 20 30 40 50 60 MSTRKRRGGA INSRQAQKRT REATSTPEIS LEAEPIELVE TAGDEIVDLT CESLEPVVVD 70 80 90 100 110 LTHNDSVVIV DGPQVLSVVP SAWTDTQRSC RMDVSSFPQN AAMSSVASAS VIP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure and genomic organization of five novel transcripts located close to the Huntington's disease gene on human chromosome 4p16.3." Hadano S., Ishida Y., Ikeda J.-E. DNA Res. 5:177-186(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Identification and characterization of a novel RING-finger gene (RNF4) mapping at 4p16.3." Chiariotti L., Benvenuto G., Fedele M., Santoro M., Simeone A., Fusco A., Bruni C.B. Genomics 47:258-265(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Brain.
[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 2). Tissue: Hair follicle dermal papilla, Testis and Tongue.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Testis.
[6]	"A novel member of the BTB/POZ family, PATZ, associates with the RNF4 RING finger protein and acts as a transcriptional repressor." Fedele M., Benvenuto G., Pero R., Majello B., Battista S., Lembo F., Vollono E., Day P.M., Santoro M., Lania L., Bruni C.B., Fusco A., Chiatiotti L. J. Biol. Chem. 275:7894-7901(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PATZ1.
[7]	"The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor." Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J. J. Biol. Chem. 278:38780-38785(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRPS1, SUBCELLULAR LOCATION.
[8]	"SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies." Haekli M., Karvonen U., Jaenne O.A., Palvimo J.J. Exp. Cell Res. 304:224-233(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PML, SUBCELLULAR LOCATION.
[9]	"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation." Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T. Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-95, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"PARP-1 transcriptional activity is regulated by sumoylation upon heat shock." Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., Bischof O., Seeler J.S., Dejean A. EMBO J. 28:3534-3548(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARP1.
[12]	"Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3." Guo B., Sharrocks A.D. Mol. Cell. Biol. 29:3204-3218(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-95, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"The SUMO protease SENP6 is essential for inner kinetochore assembly." Mukhopadhyay D., Arnaoutov A., Dasso M. J. Cell Biol. 188:681-692(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies." Geoffroy M.C., Jaffray E.G., Walker K.J., Hay R.T. Mol. Biol. Cell 21:4227-4239(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SUMOYLATED PML, SUBCELLULAR LOCATION.
[16]	"RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2alpha." van Hagen M., Overmeer R.M., Abolvardi S.S., Vertegaal A.C. Nucleic Acids Res. 38:1922-1931(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms." Maroui M.A., Kheddache-Atmane S., El Asmi F., Dianoux L., Aubry M., Chelbi-Alix M.K. PLoS ONE 7:E44949-E44949(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PML.
[18]	"Solution structure of the RING domain of the human RING finger protein 4." RIKEN structural genomics initiative (RSGI) Submitted (JUL-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 122-183.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB000468 mRNA. Translation: BAA19122.1.
U95140 mRNA. Translation: AAC52022.1.
AK128038 mRNA. Translation: BAG54620.1.
AK309509 mRNA. No translation available.
AK312534 mRNA. Translation: BAG35433.1.
AL110117 Genomic DNA. No translation available.
AL645924 Genomic DNA. No translation available.
BX322586 Genomic DNA. No translation available.
CR450722 Genomic DNA. No translation available.
CR545473 Genomic DNA. No translation available.
BC031935 mRNA. Translation: AAH31935.1.

IPI

IPI00297694.
IPI00965645.

RefSeq

NP_001171938.1. NM_001185009.2.
NP_001171939.1. NM_001185010.2.
NP_002929.1. NM_002938.4.

UniGene

Hs.740360.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EA6	NMR	-	A	122-183	[»]
2XEU	X-ray	1.50	A	130-190	[»]

ProteinModelPortal

P78317.

ModBase

Search...

Protein-protein interaction databases

IntAct

P78317. 14 interactions.

MINT

MINT-271054.

STRING

9606.ENSP00000315212.

PTM databases

PhosphoSite

P78317.

Polymorphism databases

DMDM

18202358.

Proteomic databases

PaxDb

P78317.

PRIDE

P78317.

Protocols and materials databases

DNASU

6047.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314289; ENSP00000315212; ENSG00000063978.
ENST00000506706; ENSP00000424076; ENSG00000063978.
ENST00000511600; ENSP00000426503; ENSG00000063978.
ENST00000511859; ENSP00000426615; ENSG00000063978.

GeneID

6047.

KEGG

hsa:6047.

UCSC

uc003gfb.3. human.

Organism-specific databases

CTD

6047.

GeneCards

GC04P002463.

HGNC

HGNC:10067. RNF4.

HPA

HPA049356.

MIM

602850. gene.

neXtProt

NX_P78317.

PharmGKB

PA34439.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG327779.

HOGENOM

HOG000059548.

HOVERGEN

HBG018577.

InParanoid

P78317.

OMA

THRQYHP.

OrthoDB

EOG4S4PHN.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P78317.

Bgee

P78317.

CleanEx

HS_RNF4.

Genevestigator

P78317.

GermOnline

ENSG00000063978. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF13639. zf-RING_2. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RNF4. human.

EvolutionaryTrace

P78317.

GenomeRNAi

6047.

NextBio

23561.

SOURCE

Search...

Entry information

Entry name

RNF4_HUMAN

Accession

Primary (citable) accession number: P78317
Secondary accession number(s): B2R6D6, D6RF58, Q49AR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 120 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.