Q9UKK3 (PARP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly [ADP-ribose] polymerase 4
Short name=PARP-4
EC=2.4.2.30

Alternative name(s):
193 kDa vault protein
ADP-ribosyltransferase diphtheria toxin-like 4
Short name=ARTD4
PARP-related/IalphaI-related H5/proline-rich
Short name=PH5P
Vault poly(ADP-ribose) polymerase
Short name=VPARP

Gene names

Name:	PARP4
Synonyms:	ADPRTL1, KIAA0177, PARPL

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	1724 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
Subunit structure	Component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). Binds to MVP. Associates with TEP1.
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › spindle. Note: Also found in the nucleus, associated with mitotic spindles.
Tissue specificity	Widely expressed; the highest levels are in the kidney; also detected in heart, placenta, lung, liver, skeletal muscle, spleen, leukocytes and pancreas.
Sequence similarities	Contains 1 BRCT domain. Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain. Contains 1 VIT domain. Contains 1 VWFA domain.
Sequence caution	The sequence BAA11494.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Ligand	NAD
Molecular function	Glycosyltransferase Ribonucleoprotein Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Non-traceable author statement PubMed 12101391. Source: UniProtKB cell death Inferred from mutant phenotype PubMed 12140175. Source: UniProtKB inflammatory response Inferred from mutant phenotype PubMed 12123754. Source: UniProtKB protein ADP-ribosylation Non-traceable author statement Ref.2. Source: UniProtKB response to drug Non-traceable author statement PubMed 11291045. Source: UniProtKB transport Non-traceable author statement PubMed 11855821. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB nucleus Non-traceable author statement Ref.2. Source: UniProtKB ribonucleoprotein complex Non-traceable author statement PubMed 11479319. Source: UniProtKB spindle microtubule Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	DNA binding Traceable author statement Ref.6. Source: ProtInc NAD+ ADP-ribosyltransferase activity Inferred from direct assay Ref.1. Source: UniProtKB enzyme binding Inferred from direct assay PubMed 15169895. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ORF	Q9Q2G4	3	EBI-2623021,EBI-6248094	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1724	1724	Poly [ADP-ribose] polymerase 4		PRO_0000211330
Regions
	Domain	1 – 94	94	BRCT
	Domain	242 – 370	129	PARP alpha-helical
	Domain	369 – 573	205	PARP catalytic
	Domain	607 – 735	129	VIT
	Domain	876 – 1046	171	VWFA
	Region	1562 – 1724	163	Interaction with the major vault protein
	Motif	19 – 25	7	Nuclear localization signal Potential
	Motif	1237 – 1249	13	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	101	1	Phosphothreonine Ref.8
	Modified residue	1236	1	Phosphoserine Ref.8
	Modified residue	1335	1	Phosphoserine Ref.8 Ref.9
	Modified residue	1504	1	Phosphoserine Ref.8
Natural variations
	Natural variant	81	1	I → V. Corresponds to variant rs35200240 [ dbSNP | Ensembl ].		VAR_056645
	Natural variant	122	1	S → N. Corresponds to variant rs9578751 [ dbSNP | Ensembl ].		VAR_056646
	Natural variant	215	1	F → Y. Corresponds to variant rs9318600 [ dbSNP | Ensembl ].		VAR_056647
	Natural variant	792	1	P → L. Corresponds to variant rs4986818 [ dbSNP | Ensembl ].		VAR_056648
	Natural variant	873	1	S → N. Ref.2 Ref.3 Corresponds to variant rs7140044 [ dbSNP | Ensembl ].		VAR_056649
	Natural variant	899	1	A → T. Ref.1 Corresponds to variant rs2275660 [ dbSNP | Ensembl ].		VAR_056650
	Natural variant	991	1	K → R. Corresponds to variant rs34689435 [ dbSNP | Ensembl ].		VAR_056651
	Natural variant	1012	1	V → I. Corresponds to variant rs9581043 [ dbSNP | Ensembl ].		VAR_056652
	Natural variant	1253	1	S → T. Corresponds to variant rs4986822 [ dbSNP | Ensembl ].		VAR_056653
	Natural variant	1265	1	G → A. Ref.2 Ref.3 Corresponds to variant rs1050110 [ dbSNP | Ensembl ].		VAR_016090
	Natural variant	1280	1	G → R. Ref.2 Ref.3 Corresponds to variant rs13428 [ dbSNP | Ensembl ].		VAR_016091
Experimental info
	Sequence conflict	519	1	S → P in AAD47250. Ref.1
	Sequence conflict	897	1	Q → E in AAC62491. Ref.2
	Sequence conflict	897	1	Q → E in BAA11494. Ref.3
	Sequence conflict	936	1	M → A in AAC62491. Ref.2
	Sequence conflict	936	1	M → A in BAA11494. Ref.3
	Sequence conflict	936	1	M → T in AAD47250. Ref.1
	Sequence conflict	1065	1	V → A in AAD47250. Ref.1
	Sequence conflict	1065	1	V → A in AAC62491. Ref.2
	Sequence conflict	1080	1	L → R in AAD47250. Ref.1
	Sequence conflict	1080	1	L → R in AAC62491. Ref.2
	Sequence conflict	1080	1	L → R in BAA11494. Ref.3
	Sequence conflict	1108	1	R → C in AAD47250. Ref.1
	Sequence conflict	1108	1	R → C in AAC62491. Ref.2
	Sequence conflict	1108	1	R → C in BAA11494. Ref.3
	Sequence conflict	1328	1	P → T in AAD47250. Ref.1
	Sequence conflict	1328	1	P → T in AAC62491. Ref.2
	Sequence conflict	1328	1	P → T in BAA11494. Ref.3
	Sequence conflict	1331	1	A → T in AAD47250. Ref.1
	Sequence conflict	1331	1	A → T in AAC62491. Ref.2
	Sequence conflict	1331	1	A → T in BAA11494. Ref.3
	Sequence conflict	1394	1	S → A in AAD47250. Ref.1
	Sequence conflict	1394	1	S → A in AAC62491. Ref.2
	Sequence conflict	1394	1	S → A in BAA11494. Ref.3
	Sequence conflict	1459	1	S → Y in AAD47250. Ref.1
	Sequence conflict	1459	1	S → Y in AAC62491. Ref.2
	Sequence conflict	1459	1	S → Y in BAA11494. Ref.3
	Sequence conflict	1550	1	L → P in AAD47250. Ref.1
	Sequence conflict	1550	1	L → P in AAC62491. Ref.2
	Sequence conflict	1550	1	L → P in BAA11494. Ref.3
	Sequence conflict	1555	1	V → L in AAD47250. Ref.1
	Sequence conflict	1564	1	I → T in AAD47250. Ref.1
	Sequence conflict	1564	1	I → T in AAC62491. Ref.2
	Sequence conflict	1564	1	I → T in BAA11494. Ref.3
	Sequence conflict	1656	1	A → P in AAD47250. Ref.1
	Sequence conflict	1656	1	A → P in AAC62491. Ref.2
	Sequence conflict	1656	1	A → P in BAA11494. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9UKK3 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: DCA1DD4C001EA22F	FASTA	1,724	192,595
	10 20 30 40 50 60 MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL DNADVLSQYQ 70 80 90 100 110 120 LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI TPPPDQKASS SEVKTEGLCP 130 140 150 160 170 180 DSATEEEDTV ELTEFGMQNV EIPHLPQDFE VAKYNTLEKV GMEGGQEAVV VELQCSRDSR 190 200 210 220 230 240 DCPFLISSHF LLDDGMETRR QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL 250 260 270 280 290 300 ASEQLQALLL EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI 310 320 330 340 350 360 LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC QLIRDMVNVC 370 380 390 400 410 420 ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL QNHHSKSPVD VLQIFRVGRV 430 440 450 460 470 480 NETTEFLSKL GNVRPLLHGS PVQNIVGILC RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD 490 500 510 520 530 540 SLSTSIKYSH PGETDGTRLL LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT 550 560 570 580 590 600 TDFEDDEFVV YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL 610 620 630 640 650 660 PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH VPIEAKYIFP 670 680 690 700 710 720 LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG HGAYLMSQDA PDVFTVSVGN 730 740 750 760 770 780 LPPKAKVLIK ITYITELSIL GTVGVFFMPA TVAPWQQDKA LNENLQDTVE KICIKEIGTK 790 800 810 820 830 840 QSFSLTMSIE MPYVIEFIFS DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL 850 860 870 880 890 900 PRMWVEKHPE KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL 910 920 930 940 950 960 HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN TDFWKTLRYL 970 980 990 1000 1010 1020 SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF ACGIGSTANR HVLRILSQCG 1030 1040 1050 1060 1070 1080 AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL 1090 1100 1110 1120 1130 1140 NDRLLVYGFI PHCTQATLCA LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI 1150 1160 1170 1180 1190 1200 LHENETSHEM KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK 1210 1220 1230 1240 1250 1260 EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM ELSQPEVSED 1270 1280 1290 1300 1310 1320 FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP LFKKVSPWET STSSFFPILA 1330 1340 1350 1360 1370 1380 PAVGSYLPPT ARAHSPASLS FASYRQVASF GSAAPPRQFD ASQFSQGPVP GTCADWIPQS 1390 1400 1410 1420 1430 1440 ASCPTGPPQN PPSSPYCGIV FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS 1450 1460 1470 1480 1490 1500 LPTDPDPIRG FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL 1510 1520 1530 1540 1550 1560 LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL CFLEVKEEDE 1570 1580 1590 1600 1610 1620 IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT NGLHSFLKQK GIQSLGVKGR 1630 1640 1650 1660 1670 1680 ECLLDLIATM LVLQFIRTRL EKEGIVFKSL MKMDDASISR NIPWAFEAIK QASEWVRRTE 1690 1700 1710 1720 GQYPSICPRL ELGNDWDSAT KQLLGLQPIS TVSPLHRVLH YSQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 193 kDa vault protein, VPARP, is a novel poly(ADP-ribose) polymerase." Kickhoefer V.A., Siva A.C., Kedersha N.L., Inman E.M., Ruland C., Streuli M., Rome L.H. J. Cell Biol. 146:917-928(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 306-319, VARIANT THR-899.
[2]	"Identification of a novel gene (ADPRTL1) encoding a potential poly(ADP-ribosyl)transferase protein." Still I.H., Vince P., Cowell J.K. Genomics 62:533-536(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-873; ALA-1265 AND ARG-1280. Tissue: Thymus.
[3]	"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASN-873; ALA-1265 AND ARG-1280. Tissue: Bone marrow.
[4]	Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[5]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The nuclear protein PH5P of the inter-alpha-inhibitor superfamily: a missing link between poly(ADP-ribose)polymerase and the inter-alpha-inhibitor family and a novel actor of DNA repair?" Jean L., Risler J.-L., Nagase T., Coulouarn C., Nomura N., Salier J.-P. FEBS Lett. 446:6-8(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISCUSSION OF SEQUENCE.
[7]	"Vaults and telomerase share a common subunit, TEP1." Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H. J. Biol. Chem. 274:32712-32717(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH TEP1.
[8]	"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 THR-101; SER-1236; SER-1335 AND SER-1504, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1335, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Toward a unified nomenclature for mammalian ADP-ribosyltransferases." Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F. Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF158255 mRNA. Translation: AAD47250.1. AF057160 mRNA. Translation: AAC62491.1. D79999 mRNA. Translation: BAA11494.2. Different initiation. AL359763 Genomic DNA. Translation: CAI12394.1.
IPI	IPI00296909.
RefSeq	NP_006428.2. NM_006437.3.
UniGene	Hs.741173.
3D structure databases
ProteinModelPortal	Q9UKK3.
SMR	Q9UKK3. Positions 4-94, 207-564.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UKK3. 12 interactions.
MINT	MINT-6768840.
STRING	9606.ENSP00000371419.
PTM databases
PhosphoSite	Q9UKK3.
Polymorphism databases
DMDM	308153574.
Proteomic databases
PaxDb	Q9UKK3.
PeptideAtlas	Q9UKK3.
PRIDE	Q9UKK3.
Protocols and materials databases
DNASU	143.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381989; ENSP00000371419; ENSG00000102699.
GeneID	143.
KEGG	hsa:143.
UCSC	uc001upl.3. human.
Organism-specific databases
CTD	143.
GeneCards	GC13M024995.
H-InvDB	HIX0019099.
HGNC	HGNC:271. PARP4.
HPA	HPA011739.
MIM	607519. gene.
neXtProt	NX_Q9UKK3.
PharmGKB	PA24591.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2304.
HOGENOM	HOG000139369.
HOVERGEN	HBG053515.
InParanoid	Q9UKK3.
KO	K10798.
OMA	GKCMDLH.
OrthoDB	EOG4X97GF.
PhylomeDB	Q9UKK3.
Enzyme and pathway databases
BRENDA	2.4.2.30. 2681.
Gene expression databases
Bgee	Q9UKK3.
CleanEx	HS_PARP4.
Genevestigator	Q9UKK3.
GermOnline	ENSG00000102699. Homo sapiens.
Family and domain databases
Gene3D	1.20.142.10. 1 hit.
InterPro	IPR001357. BRCT_dom. IPR012317. Poly(ADP-ribose)pol_cat_dom. IPR004102. Poly(ADP-ribose)pol_reg_dom. IPR013694. VIT. IPR002035. VWF_A. [Graphical view]
Pfam	PF00533. BRCT. 1 hit. PF00644. PARP. 1 hit. PF08487. VIT. 1 hit. PF00092. VWA. 1 hit. [Graphical view]
SMART	SM00292. BRCT. 1 hit. SM00609. VIT. 1 hit. SM00327. VWA. 1 hit. [Graphical view]
SUPFAM	SSF52113. BRCT. 1 hit. SSF47587. PARP_reg. 1 hit.
PROSITE	PS50172. BRCT. 1 hit. PS51060. PARP_ALPHA_HD. 1 hit. PS51059. PARP_CATALYTIC. 1 hit. PS51468. VIT. 1 hit. PS50234. VWFA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL6142.
ChiTaRS	PARP4. human.
GenomeRNAi	143.
NextBio	569.
SOURCE	Search...

Entry information

Entry name

PARP4_HUMAN

Accession

Primary (citable) accession number: Q9UKK3
Secondary accession number(s): O75903 , Q14682, Q5QNZ9, Q9H1M6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 129 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.