P11831 (SRF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serum response factor
Short name=SRF

Gene names

Name:

SRF

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

General annotation (Comments)

Function	SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Required for cardiac differentiation and maturation.
Subunit structure	Binds DNA as a multimer, probably a dimer. Interacts with MLLT7/FOXO4, NKX3A and SSRP1. Interacts with ARID2 and SRFBP1 By similarity. Forms complexes with ARID2, MYOCD, NKX2-5 and SRFBP1 By similarity. Forms a nuclear ternary complex with MKL1 and SCAI. Interacts with LPXN. Ref.9 Ref.11 Ref.13
Subcellular location	Nucleus Ref.13.
Post-translational modification	Phosphorylated by PRKDC. Ref.5 Ref.6 Ref.8
Sequence similarities	Contains 1 MADS-box domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis involved in wound healing Traceable author statement PubMed 15180964. Source: BHF-UCL associative learning Inferred from electronic annotation. Source: Compara cardiac myofibril assembly Inferred from electronic annotation. Source: Compara cardiac vascular smooth muscle cell differentiation Inferred from electronic annotation. Source: Compara cell migration involved in sprouting angiogenesis Inferred from mutant phenotype PubMed 15180964. Source: BHF-UCL cell-matrix adhesion Inferred from electronic annotation. Source: Compara cellular senescence Inferred from mutant phenotype PubMed 15282327. Source: BHF-UCL contractile actin filament bundle assembly Inferred from electronic annotation. Source: Compara developmental growth Inferred from electronic annotation. Source: Compara dorsal aorta morphogenesis Inferred from electronic annotation. Source: Compara epithelial cell-cell adhesion Inferred from electronic annotation. Source: Compara epithelial structure maintenance Inferred from electronic annotation. Source: Compara erythrocyte development Inferred from electronic annotation. Source: Compara eyelid development in camera-type eye Inferred from electronic annotation. Source: Compara heart looping Inferred from sequence or structural similarity. Source: BHF-UCL heart trabecula formation Inferred from electronic annotation. Source: Compara hematopoietic stem cell differentiation Inferred from electronic annotation. Source: Compara hippocampus development Inferred from electronic annotation. Source: Compara long term synaptic depression Inferred from electronic annotation. Source: Compara mRNA transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL megakaryocyte development Inferred from electronic annotation. Source: Compara mesoderm formation Inferred from electronic annotation. Source: Compara morphogenesis of an epithelial sheet Inferred from electronic annotation. Source: Compara muscle cell homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of beta-amyloid clearance Inferred from mutant phenotype PubMed 19098903. Source: BHF-UCL neuron development Traceable author statement PubMed 17200232. Source: BHF-UCL neuron migration Inferred from electronic annotation. Source: Compara neuron projection development Inferred from electronic annotation. Source: Compara patterning of blood vessels Inferred from electronic annotation. Source: Compara platelet activation Inferred from electronic annotation. Source: Compara platelet formation Inferred from electronic annotation. Source: Compara positive regulation of cell differentiation Inferred from direct assay PubMed 17576768. Source: MGI positive regulation of filopodium assembly Inferred from electronic annotation. Source: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 19098903. Source: BHF-UCL positive regulation of smooth muscle contraction Inferred from direct assay PubMed 17215356. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Inferred from genetic interaction PubMed 19783823. Source: BHF-UCL positive regulation of transcription initiation from RNA polymerase II promoter Inferred from direct assay PubMed 8887666. Source: BHF-UCL positive regulation of transcription via serum response element binding Inferred from direct assay Ref.1PubMed 8887666. Source: BHF-UCL positive thymic T cell selection Inferred from electronic annotation. Source: Compara primitive streak formation Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from electronic annotation. Source: Compara regulation of smooth muscle cell differentiation Traceable author statement PubMed 17215356. Source: BHF-UCL regulation of water loss via skin Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from mutant phenotype PubMed 15180964. Source: BHF-UCL response to hormone stimulus Inferred from direct assay PubMed 17975004. Source: BHF-UCL response to hypoxia Inferred from expression pattern PubMed 19098903. Source: BHF-UCL response to toxin Traceable author statement PubMed 12660819. Source: BHF-UCL sarcomere organization Inferred from electronic annotation. Source: Compara skin morphogenesis Inferred from electronic annotation. Source: Compara stress fiber assembly Inferred from electronic annotation. Source: Compara tangential migration from the subventricular zone to the olfactory bulb Inferred from electronic annotation. Source: Compara tight junction assembly Inferred from electronic annotation. Source: Compara trophectodermal cell differentiation Inferred from direct assay PubMed 17576768. Source: MGI
Cellular_component	cytoplasm Traceable author statement PubMed 15180964. Source: BHF-UCL nuclear chromatin Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 2108863. Source: BHF-UCL
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from sequence or structural similarity. Source: BHF-UCL RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 20808827. Source: UniProtKB RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara RNA polymerase II transcription factor binding transcription factor activity Inferred from electronic annotation. Source: Compara chromatin DNA binding Inferred from electronic annotation. Source: Compara serum response element binding Inferred from direct assay Ref.1. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MKL1	Q969V6	2	EBI-493034,EBI-493122
MKL2	Q9ULH7	3	EBI-493034,EBI-493007
MYOCD	Q8IZQ8	2	EBI-493034,EBI-493384

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 508

508

Serum response factor

PRO_0000199423

Regions

Domain

141 – 201

61

MADS-box

DNA binding

133 – 222

90

Region

168 – 222

55

Involved in dimerization

Compositional bias

13 – 142

130

Gly-rich

Compositional bias

80 – 90

11

Asp/Glu-rich (acidic)

Compositional bias

242 – 258

17

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

77

1

Phosphoserine Ref.6 Ref.12

Modified residue

79

1

Phosphoserine Ref.6 Ref.12

Modified residue

83

1

Phosphoserine Ref.6 Ref.12

Modified residue

85

1

Phosphoserine Ref.6 Ref.12

Modified residue

103

1

Phosphoserine Ref.6

Modified residue

224

1

Phosphoserine Ref.10 Ref.12 Ref.14

Modified residue

253

1

Phosphoserine Ref.5

Modified residue

435

1

Phosphoserine; by dsDNA kinase Ref.8

Modified residue

446

1

Phosphoserine; by dsDNA kinase Ref.8

Glycosylation

277

1

O-linked (GlcNAc) Ref.7

CAR_000181

Glycosylation

307

1

O-linked (GlcNAc) Probable

Glycosylation

309

1

O-linked (GlcNAc) Probable

Glycosylation

316

1

O-linked (GlcNAc) Ref.7

CAR_000196

Glycosylation

383

1

O-linked (GlcNAc) Probable

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

508

Helix Strand Turn

Details...

Helix

154 – 179

26

Beta strand

182 – 188

7

Beta strand

190 – 192

3

Beta strand

194 – 198

5

Helix

200 – 205

6

Helix

209 – 220

12

Sequences

	Sequence		Length	Mass (Da)
	P11831 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 25505828D3276F44	FASTA	508	51,593
	10 20 30 40 50 60 MLPTQAGAAA ALGRGSALGG SLNRTPTGRP GGGGGTRGAN GGRVPGNGAG LGPGRLEREA 70 80 90 100 110 120 AAAAATTPAP TAGALYSGSE GDSESGEEEE LGAERRGLKR SLSEMEIGMV VGGPEASAAA 130 140 150 160 170 180 TGGYGPVSGA VSGAKPGKKT RGRVKIKMEF IDNKLRRYTT FSKRKTGIMK KAYELSTLTG 190 200 210 220 230 240 TQVLLLVASE TGHVYTFATR KLQPMITSET GKALIQTCLN SPDSPPRSDP TTDQRMSATG 250 260 270 280 290 300 FEETDLTYQV SESDSSGETK DTLKPAFTVT NLPGTTSTIQ TAPSTSTTMQ VSSGPSFPIT 310 320 330 340 350 360 NYLAPVSASV SPSAVSSANG TVLKSTGSGP VSSGGLMQLP TSFTLMPGGA VAQQVPVQAI 370 380 390 400 410 420 QVHQAPQQAS PSRDSSTDLT QTSSSGTVTL PATIMTSSVP TTVGGHMMYP SPHAVMYAPT 430 440 450 460 470 480 SGLGDGSLTV LNAFSQAPST MQVSHSQVQE PGGVPQVFLT ASSGTVQIPV SAVQLHQMAV 490 500 IGQQAGSSSN LTELQVVNLD TAHSTKSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element." Norman C., Runswick M., Pollock R., Treisman R. Cell 55:989-1003(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Lung and Lymph.
[5]	"C-terminal phosphorylation of the serum-response factor." Janknecht R., Ernst W.H., Houthaeve T., Nordheim A. Eur. J. Biochem. 216:469-475(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 210-221 AND 253-264, PHOSPHORYLATION AT SER-253.
[6]	"Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties." Janknecht R., Hipskind R.A., Houthaeve T., Nordheim A., Stunnenberg H.G. EMBO J. 11:1045-1054(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-77; SER-79; SER-83; SER-85 AND SER-103.
[7]	"Localization of O-GlcNAc modification on the serum response transcription factor." Reason A.J., Morris H.R., Panico M., Marais R., Treisman R.H., Haltiwanger R.S., Hart G.W., Kelly W.G., Dell A. J. Biol. Chem. 267:16911-16921(1992) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-277; SER-307; SER-309; SER-316 AND SER-383.
[8]	"The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites." Liu S.-H., Ma J.-T., Yueh A.Y., Lees-Miller S.P., Anderson C.W., Ng S.-Y. J. Biol. Chem. 268:21147-21154(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-435 AND SER-446.
[9]	"Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin." Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N. Dev. Cell 9:261-270(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MLLT7.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription." Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M. Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LPXN.
[12]	"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-77; SER-79; SER-83; SER-85 AND SER-224, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin." Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P., Grosse R. Nat. Cell Biol. 11:557-568(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MKL1 AND SCAI, SUBCELLULAR LOCATION.
[14]	"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-224, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Structure of serum response factor core bound to DNA." Pellegrini L., Tan S., Richmond T.J. Nature 376:490-498(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 132-223.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03161 mRNA. Translation: AAA36647.1.
AL133375, AL355385 Genomic DNA. Translation: CAI20207.1.
AL355385, AL133375 Genomic DNA. Translation: CAI13785.1.
CH471081 Genomic DNA. Translation: EAX04161.1.
BC048211 mRNA. Translation: AAH48211.1.
BC052572 mRNA. Translation: AAH52572.1.

IPI

IPI00007879.

PIR

A31637.

RefSeq

NP_003122.1. NM_003131.2.

UniGene

Hs.520140.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HBX	X-ray	3.15	A/B/D/E	132-223	[»]
1K6O	X-ray	3.19	B/C	133-235	[»]
1SRS	X-ray	3.20	A/B	132-223	[»]

ProteinModelPortal

P11831.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-49N.

IntAct

P11831. 6 interactions.

STRING

9606.ENSP00000265354.

PTM databases

GlycoSuiteDB

P11831.

PhosphoSite

P11831.

Polymorphism databases

DMDM

134876.

Proteomic databases

PaxDb

P11831.

PRIDE

P11831.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265354; ENSP00000265354; ENSG00000112658.

GeneID

6722.

KEGG

hsa:6722.

UCSC

uc003oui.3. human.

Organism-specific databases

CTD

6722.

GeneCards

GC06P043138.

HGNC

HGNC:11291. SRF.

HPA

CAB005416.
HPA001819.

MIM

600589. gene.

neXtProt

NX_P11831.

PharmGKB

PA36116.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5068.

HOGENOM

HOG000012380.

HOVERGEN

HBG014968.

InParanoid

P11831.

KO

K04378.

OMA

MITSDTG.

OrthoDB

EOG48KRCZ.

PhylomeDB

P11831.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
pdgfrapathway. PDGFR-alpha signaling pathway.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.

Gene expression databases

ArrayExpress

P11831.

Bgee

P11831.

CleanEx

HS_SRF.

Genevestigator

P11831.

GermOnline

ENSG00000112658. Homo sapiens.

Family and domain databases

InterPro

IPR002100. TF_MADSbox.
[Graphical view]

Pfam

PF00319. SRF-TF. 1 hit.
[Graphical view]

PRINTS

PR00404. MADSDOMAIN.

SMART

SM00432. MADS. 1 hit.
[Graphical view]

SUPFAM

SSF55455. TF_MADSbox. 1 hit.

PROSITE

PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P11831.

GenomeRNAi

6722.

NextBio

26222.

PMAP-CutDB

P11831.

SOURCE

Search...

Entry information

Entry name

SRF_HUMAN

Accession

Primary (citable) accession number: P11831
Secondary accession number(s): Q5T648

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	May 1, 2013
This is version 153 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.