Q9NWF9 (RN216_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF216
EC=6.3.2.-

Alternative name(s):
RING finger protein 216
Triad domain-containing protein 3
Ubiquitin-conjugating enzyme 7-interacting protein 1
Zinc finger protein inhibiting NF-kappa-B

Gene names

Name:	RNF216
Synonyms:	TRIAD3, UBCE7IP1, ZIN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	866 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isoform 1 acts as an E3 ubiquitin ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Promotes degradation of TRAF3, TLR4 and TLR9. Contributes to the regulation of antiviral responses. Down-regulates activation of NF-kappa-B, IRF3 activation and IFNB production. Isoform 3/ZIN inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis. Ref.2 Ref.10
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with UBE2L3 and to some extent with UBE2L6. Interacts with TRAF3, TLR3, TLR4, TLR5 and TLR9. Isoform 3/ZIN binds RIPK1 and HIV VIF. Ref.1 Ref.2 Ref.8 Ref.10
Subcellular location	Cytoplasm.
Tissue specificity	Ubiquitous, with the highest levels of expression in testis and peripheral blood leukocytes.
Domain	The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme By similarity.
Post-translational modification	Auto-ubiquitinated.
Sequence similarities	Contains 1 IBR-type zinc finger. Contains 2 RING-type zinc fingers.
Sequence caution	The sequence BAA91422.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.10. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.10. Source: UniProtKB regulation of defense response to virus by host Inferred from direct assay Ref.10. Source: UniProtKB regulation of interferon-beta production Inferred from direct assay Ref.10. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.10. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
vif	P12504	4	EBI-723337,EBI-779991	From a different organism.

Alternative products

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

Isoform 1 (identifier: Q9NWF9-2)

Also known as: TRIAD3A;

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: Q9NWF9-1)

Also known as: TRIAD3B;

The sequence of this isoform differs from the canonical sequence as follows:
     67-67: E → ETNKPQRSRPNLIKPAAQWQDLKRLGEERPKKSRAAFESDKSSYFSVCNNPLFDSGAQ

Isoform 3 (identifier: Q9NWF9-3)

Also known as: ZIN; TRIAD3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-378: Missing.

Note: 4 different alternatively spliced mRNAs code for this protein isoform.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 866	866	E3 ubiquitin-protein ligase RNF216		PRO_0000056293
Regions
	Zinc finger	515 – 566	52	RING-type 1
	Zinc finger	583 – 648	66	IBR-type
	Zinc finger	675 – 714	40	RING-type 2
	Coiled coil	475 – 491	17	Potential
	Coiled coil	737 – 763	27	Potential
	Compositional bias	769 – 862	94	Pro-rich
Amino acid modifications
	Modified residue	35	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	1 – 378	378	Missing in isoform 3.		VSP_012443
	Alternative sequence	67	1	E → ETNKPQRSRPNLIKPAAQWQ DLKRLGEERPKKSRAAFESD KSSYFSVCNNPLFDSGAQ in isoform 2.		VSP_012444
Experimental info
	Sequence conflict	408	1	L → F in AAL38043. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TRIAD3A) [UniParc]. Last modified January 4, 2005. Version 3. Checksum: 6A46B66A6569DE74	FASTA	866	99,406
	10 20 30 40 50 60 MEEGNNNEEV IHLNNFHCHR GQEWINLRDG PITISDSSDE ERIPMLVTPA PQQHEEEDLD 70 80 90 100 110 120 DDVILTEDDS EDDYGEFLDL GPPGISEFTK PSGQTEREPK PGPSHNQAAN DIVNPRSEQK 130 140 150 160 170 180 VIILEEGSLL YTESDPLETQ NQSSEDSETE LLSNLGESAA LADDQAIEED CWLDHPYFQS 190 200 210 220 230 240 LNQQPREITN QVVPQERQPE AELGRLLFQH EFPGPAFPRP EPQQGGISGP SSPQPAHPLG 250 260 270 280 290 300 EFEDQQLASD DEEPGPAFPM QESQEPNLEN IWGQEAAEVD QELVELLVKE TEARFPDVAN 310 320 330 340 350 360 GFIEEIIHFK NYYDLNVLCN FLLENPDYPK REDRIIINPS SSLLASQDET KLPKIDFFDY 370 380 390 400 410 420 SKLTPLDQRC FIQAADLLMA DFKVLSSQDI KWALHELKGH YAITRKALSD AIKKWQELSP 430 440 450 460 470 480 ETSGKRKKRK QMNQYSYIDF KFEQGDIKIE KRMFFLENKR RHCRSYDRRA LLPAVQQEQE 490 500 510 520 530 540 FYEQKIKEMA EHEDFLLALQ MNEEQYQKDG QLIECRCCYG EFPFEELTQC ADAHLFCKEC 550 560 570 580 590 600 LIRYAQEAVF GSGKLELSCM EGSCTCSFPT SELEKVLPQT ILYKYYERKA EEEVAAAYAD 610 620 630 640 650 660 ELVRCPSCSF PALLDSDVKR FSCPNPHCRK ETCRKCQGLW KEHNGLTCEE LAEKDDIKYR 670 680 690 700 710 720 TSIEEKMTAA RIRKCHKCGT GLIKSEGCNR MSCRCGAQMC YLCRVSINGY DHFCQHPRSP 730 740 750 760 770 780 GAPCQECSRC SLWTDPTEDD EKLIEEIQKE AEEEQKRKNG ENTFKRIGPP LEKPVEKVQR 790 800 810 820 830 840 VEALPRPVPQ NLPQPQMPPY AFAHPPFPLP PVRPVFNNFP LNMGPIPAPY VPPLPNVRVN 850 860 YDFGPIHMPL EHNLPMHFGP QPRHRF
	Isoform 2 (TRIAD3B) [UniParc]. Checksum: FFAA15927AE14608	FASTA	923	105,882
	10 20 30 40 50 60 MEEGNNNEEV IHLNNFHCHR GQEWINLRDG PITISDSSDE ERIPMLVTPA PQQHEEEDLD 70 80 90 100 110 120 DDVILTETNK PQRSRPNLIK PAAQWQDLKR LGEERPKKSR AAFESDKSSY FSVCNNPLFD 130 140 150 160 170 180 SGAQDDSEDD YGEFLDLGPP GISEFTKPSG QTEREPKPGP SHNQAANDIV NPRSEQKVII 190 200 210 220 230 240 LEEGSLLYTE SDPLETQNQS SEDSETELLS NLGESAALAD DQAIEEDCWL DHPYFQSLNQ 250 260 270 280 290 300 QPREITNQVV PQERQPEAEL GRLLFQHEFP GPAFPRPEPQ QGGISGPSSP QPAHPLGEFE 310 320 330 340 350 360 DQQLASDDEE PGPAFPMQES QEPNLENIWG QEAAEVDQEL VELLVKETEA RFPDVANGFI 370 380 390 400 410 420 EEIIHFKNYY DLNVLCNFLL ENPDYPKRED RIIINPSSSL LASQDETKLP KIDFFDYSKL 430 440 450 460 470 480 TPLDQRCFIQ AADLLMADFK VLSSQDIKWA LHELKGHYAI TRKALSDAIK KWQELSPETS 490 500 510 520 530 540 GKRKKRKQMN QYSYIDFKFE QGDIKIEKRM FFLENKRRHC RSYDRRALLP AVQQEQEFYE 550 560 570 580 590 600 QKIKEMAEHE DFLLALQMNE EQYQKDGQLI ECRCCYGEFP FEELTQCADA HLFCKECLIR 610 620 630 640 650 660 YAQEAVFGSG KLELSCMEGS CTCSFPTSEL EKVLPQTILY KYYERKAEEE VAAAYADELV 670 680 690 700 710 720 RCPSCSFPAL LDSDVKRFSC PNPHCRKETC RKCQGLWKEH NGLTCEELAE KDDIKYRTSI 730 740 750 760 770 780 EEKMTAARIR KCHKCGTGLI KSEGCNRMSC RCGAQMCYLC RVSINGYDHF CQHPRSPGAP 790 800 810 820 830 840 CQECSRCSLW TDPTEDDEKL IEEIQKEAEE EQKRKNGENT FKRIGPPLEK PVEKVQRVEA 850 860 870 880 890 900 LPRPVPQNLP QPQMPPYAFA HPPFPLPPVR PVFNNFPLNM GPIPAPYVPP LPNVRVNYDF 910 920 GPIHMPLEHN LPMHFGPQPR HRF
	Isoform 3 (ZIN) (TRIAD3) [UniParc]. Checksum: 6EB1D218DE2E4E6A	FASTA	488	56,697
	10 20 30 40 50 60 MADFKVLSSQ DIKWALHELK GHYAITRKAL SDAIKKWQEL SPETSGKRKK RKQMNQYSYI 70 80 90 100 110 120 DFKFEQGDIK IEKRMFFLEN KRRHCRSYDR RALLPAVQQE QEFYEQKIKE MAEHEDFLLA 130 140 150 160 170 180 LQMNEEQYQK DGQLIECRCC YGEFPFEELT QCADAHLFCK ECLIRYAQEA VFGSGKLELS 190 200 210 220 230 240 CMEGSCTCSF PTSELEKVLP QTILYKYYER KAEEEVAAAY ADELVRCPSC SFPALLDSDV 250 260 270 280 290 300 KRFSCPNPHC RKETCRKCQG LWKEHNGLTC EELAEKDDIK YRTSIEEKMT AARIRKCHKC 310 320 330 340 350 360 GTGLIKSEGC NRMSCRCGAQ MCYLCRVSIN GYDHFCQHPR SPGAPCQECS RCSLWTDPTE 370 380 390 400 410 420 DDEKLIEEIQ KEAEEEQKRK NGENTFKRIG PPLEKPVEKV QRVEALPRPV PQNLPQPQMP 430 440 450 460 470 480 PYAFAHPPFP LPPVRPVFNN FPLNMGPIPA PYVPPLPNVR VNYDFGPIHM PLEHNLPMHF GPQPRHRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation." Chen D., Li X., Zhai Z., Shu H.-B. J. Biol. Chem. 277:15985-15991(2002) [PubMed: 11854271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH RIPK1.
[2]	"Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors." Chuang T.-H., Ulevitch R.J. Nat. Immunol. 5:495-502(2004) [PubMed: 15107846] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION WITH TLR3; TLR4; TLR5 AND TLR9. Tissue: Placenta.
[3]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Endometrium.
[4]	"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: 12853948] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney and Uterus.
[6]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-866 (ISOFORMS 1/2/3). Tissue: Embryo.
[7]	"Identification of a novel TRIAD protein, TRIAD3." van der Reijden B.A., Jansen J.H. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 509-866 (ISOFORMS 1/2/3).
[8]	"Ring finger protein ZIN interacts with human immunodeficiency virus type 1 Vif." Feng F., Davis A., Lake J.A., Carr J., Xia W., Burrell C., Li P. J. Virol. 78:10574-10581(2004) [PubMed: 15367624] [Abstract] Cited for: INTERACTION WITH HIV VIF PROTEIN (ISOFORM 3).
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS signaling pathway by targeting TRAF3 for degradation." Nakhaei P., Mesplede T., Solis M., Sun Q., Zhao T., Yang L., Chuang T.H., Ware C.F., Lin R., Hiscott J. PLoS Pathog. 5:E1000650-E1000650(2009) [PubMed: 19893624] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRAF3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY062174 mRNA. Translation: AAL38043.1. AF513717 mRNA. Translation: AAP47174.1. AF513718 mRNA. Translation: AAP47175.1. AY177396 mRNA. Translation: AAO60361.1. AY177397 mRNA. Translation: AAO60362.1. AY177398 mRNA. Translation: AAO60363.1. BX537406 mRNA. Translation: CAD97648.1. AC008167 Genomic DNA. Translation: AAS07532.1. BC000787 mRNA. Translation: AAH00787.2. BC063825 mRNA. Translation: AAH63825.1. AK000916 mRNA. Translation: BAA91422.1. Different initiation. AF228527 mRNA. Translation: AAF36723.1.
IPI	IPI00375632. IPI00410033. IPI00413022.
RefSeq	NP_996994.1. NM_207111.3. NP_996999.1. NM_207116.2.
UniGene	Hs.487458. Hs.689456.
3D structure databases
ProteinModelPortal	Q9NWF9.
SMR	Q9NWF9. Positions 512-568, 576-650, 667-711.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NWF9. 3 interactions.
MINT	MINT-1194402.
STRING	Q9NWF9.
PTM databases
PhosphoSite	Q9NWF9.
Polymorphism databases
DMDM	57015417.
Proteomic databases
PRIDE	Q9NWF9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000425013; ENSP00000404602; ENSG00000011275.
GeneID	54476.
KEGG	hsa:54476.
UCSC	uc003sox.1. human. uc003soy.1. human.
Organism-specific databases
CTD	54476.
GeneCards	GC07M005661.
H-InvDB	HIX0006456. HIX0025299.
HGNC	HGNC:21698. RNF216.
HPA	HPA018955. HPA021123.
MIM	609948. gene.
neXtProt	NX_Q9NWF9.
PharmGKB	PA162401829.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10173.
GeneTree	ENSGT00510000048032.
HOVERGEN	HBG102854.
OMA	GAQDDSE.
OrthoDB	EOG4VDPXT.
Gene expression databases
ArrayExpress	Q9NWF9.
Bgee	Q9NWF9.
CleanEx	HS_RNF216.
Genevestigator	Q9NWF9.
GermOnline	ENSG00000011275. Homo sapiens.
Family and domain databases
InterPro	IPR002867. Znf_C6HC. [Graphical view]
KO	K11976.
SMART	SM00647. IBR. 2 hits. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	56786.
SOURCE	Search...

Entry information

Entry name

RN216_HUMAN

Accession

Primary (citable) accession number: Q9NWF9
Secondary accession number(s): Q6Y691 , Q75ML7, Q7Z2H7, Q7Z7C1, Q8NHW7, Q9NYT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	January 4, 2005
Last modified:	December 14, 2011
This is version 103 of the entry and version 3 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.