Q8N556 (AFAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin filament-associated protein 1

Alternative name(s):
110 kDa actin filament-associated protein
Short name=AFAP-110

Gene names

Name:	AFAP1
Synonyms:	AFAP

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

General annotation (Comments)

Function	Can cross-link actin filaments into both network and bundle structures By similarity. May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells. Ref.1 Ref.8
Subunit structure	Monomer and homomultimer. Interacts via its C-terminus with F-actin; probably involving AFAP1 multimers By similarity. Interacts with activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with PRKCA, PRKCB and PRKCI By similarity. Ref.1
Subcellular location	Cytoplasm › cytoskeleton. Note: Localizes with stress fibers in quiescent cells, concentrated in cell motility structures such as lamellipodia, filopodia and membrane ruffles upon their induction. Ref.1
Tissue specificity	Low expression in normal breast epithelial cell line MCF-10A and in tumorigenic breast cancer cell lines MCF-7, T-47D and ZR-75-1. Highly expressed in the invasive breast cancer cell lines MDA-MB-231 and MDA-MB-435. Overexpressed in prostate carcinoma. Ref.7 Ref.8
Post-translational modification	Phosphorylated on tyrosine residues by SRC. Ref.1
Miscellaneous	Knockdown in MDA-MB-231 cells resulted in loss of actin stress fibers, decreased adhesion and spreading on fibronectin.
Sequence similarities	Contains 2 PH domains.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: HPA cytoplasm Inferred from direct assay. Source: HPA focal adhesion Inferred from direct assay. Source: HPA
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8N556-1)

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: Q8N556-2)

The sequence of this isoform differs from the canonical sequence as follows:
     510-510: S → SWEPEDGFPA...GRASLGLNSQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 730	730	Actin filament-associated protein 1		PRO_0000317658
Regions
	Domain	153 – 249	97	PH 1
	Domain	347 – 441	95	PH 2
	Region	594 – 637	44	Interaction with F-actin By similarity
	Coiled coil	557 – 648	92	Potential
	Motif	71 – 74	4	SH3-binding By similarity
	Motif	94 – 97	4	SH2-binding 1 By similarity
	Motif	451 – 456	6	SH2-binding 2 By similarity
	Compositional bias	60 – 106	47	Pro-rich
Amino acid modifications
	Modified residue	282	1	Phosphoserine Ref.9
	Modified residue	283	1	Phosphoserine Ref.9
	Modified residue	546	1	Phosphothreonine By similarity
	Modified residue	548	1	Phosphoserine Ref.10
	Modified residue	664	1	Phosphoserine Ref.9
	Modified residue	665	1	Phosphoserine Ref.9
	Modified residue	668	1	Phosphoserine Ref.9 Ref.10 Ref.11
	Modified residue	679	1	Phosphoserine Ref.9
	Modified residue	687	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	510	1	S → SWEPEDGFPASCSRGLGEEV LYDNAGLYDNLPPPHIFARY SPADRKASRLSADKLSSNHY KYPASAQSVTNTSSVGRASL GLNSQ in isoform 2.		VSP_044838
	Natural variant	403	1	S → C. Ref.2 Ref.4 Corresponds to variant rs28406288 [ dbSNP | Ensembl ].		VAR_038578
	Natural variant	518	1	V → M. Ref.5 Corresponds to variant rs41264705 [ dbSNP | Ensembl ].		VAR_038579
Experimental info
	Mutagenesis	71	1	P → A: Decreased tyrosine phosphorylation. Ref.1
	Mutagenesis	77	1	P → A: No effect on tyrosine phosphorylation. Ref.1
	Mutagenesis	93	1	Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-94; F-125; F-451 and F-453. Ref.1
	Mutagenesis	94	1	Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-125; F-451 and F-453. Ref.1
	Mutagenesis	125	1	Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-451 and F-453. Ref.1
	Mutagenesis	451	1	Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-453. Ref.1
	Mutagenesis	453	1	Y → F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-451. Ref.1
	Sequence conflict	197	1	P → L in AAG17055. Ref.1
	Sequence conflict	223	1	G → D in AAG17055. Ref.1
	Sequence conflict	238	1	E → G in AAG17055. Ref.1
	Sequence conflict	465	1	T → A in BAF83496. Ref.2
Isoform 2:
	Sequence conflict	561	1	A → V in BAG60004. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 4E916BB4F82F5547	FASTA	730	80,725
	10 20 30 40 50 60 MEELIVELRL FLELLDHEYL TSTVREKKAV ITNILLRIQS SKGFDVKDHA QKQETANSLP 70 80 90 100 110 120 APPQMPLPEI PQPWLPPDSG PPPLPTSSLP EGYYEEAVPL SPGKAPEYIT SNYDSDAMSS 130 140 150 160 170 180 SYESYDEEEE DGKGKKTRHQ WPSEEASMDL VKDAKICAFL LRKKRFGQWT KLLCVIKDTK 190 200 210 220 230 240 LLCYKSSKDQ QPQMELPLQG CNITYIPKDS KKKKHELKIT QQGTDPLVLA VQSKEQAEQW 250 260 270 280 290 300 LKVIKEAYSG CSGPVDSECP PPPSSPVHKA ELEKKLSSER PSSDGEGVVE NGITTCNGKE 310 320 330 340 350 360 QVKRKKSSKS EAKGTVSKVT GKKITKIISL GKKKPSTDEQ TSSAEEDVPT CGYLNVLSNS 370 380 390 400 410 420 RWRERWCRVK DNKLIFHKDR TDLKTHIVSI PLRGCEVIPG LDSKHPLTFR LLRNGQEVAV 430 440 450 460 470 480 LEASSSEDMG RWIGILLAET GSSTDPEALH YDYIDVEMSA SVIQTAKQTF CFMNRRVISA 490 500 510 520 530 540 NPYLGGTSNG YAHPSGTALH YDDVPCINGS LKGKKPPVAS NGVTGKGKTL SSQPKKADPA 550 560 570 580 590 600 AVVKRTGSNA AQYKYGKNRV EADAKRLQTK EEELLKRKEA LRNRLAQLRK ERKDLRAAIE 610 620 630 640 650 660 VNAGRKPQAI LEEKLKQLEE ECRQKEAERV SLELELTEVK ESLKKALAGG VTLGLAIEPK 670 680 690 700 710 720 SGTSSPQSPV FRHRTLENSP ISSCDTSDTE GPVPVNSAAV LKKSQAAPGS SPCRGHVLRK 730 AKEWELKNGT
	Isoform 2 [UniParc]. Checksum: B066A95292C261FC	FASTA	814	89,795
	10 20 30 40 50 60 MEELIVELRL FLELLDHEYL TSTVREKKAV ITNILLRIQS SKGFDVKDHA QKQETANSLP 70 80 90 100 110 120 APPQMPLPEI PQPWLPPDSG PPPLPTSSLP EGYYEEAVPL SPGKAPEYIT SNYDSDAMSS 130 140 150 160 170 180 SYESYDEEEE DGKGKKTRHQ WPSEEASMDL VKDAKICAFL LRKKRFGQWT KLLCVIKDTK 190 200 210 220 230 240 LLCYKSSKDQ QPQMELPLQG CNITYIPKDS KKKKHELKIT QQGTDPLVLA VQSKEQAEQW 250 260 270 280 290 300 LKVIKEAYSG CSGPVDSECP PPPSSPVHKA ELEKKLSSER PSSDGEGVVE NGITTCNGKE 310 320 330 340 350 360 QVKRKKSSKS EAKGTVSKVT GKKITKIISL GKKKPSTDEQ TSSAEEDVPT CGYLNVLSNS 370 380 390 400 410 420 RWRERWCRVK DNKLIFHKDR TDLKTHIVSI PLRGCEVIPG LDSKHPLTFR LLRNGQEVAV 430 440 450 460 470 480 LEASSSEDMG RWIGILLAET GSSTDPEALH YDYIDVEMSA SVIQTAKQTF CFMNRRVISA 490 500 510 520 530 540 NPYLGGTSNG YAHPSGTALH YDDVPCINGS WEPEDGFPAS CSRGLGEEVL YDNAGLYDNL 550 560 570 580 590 600 PPPHIFARYS PADRKASRLS ADKLSSNHYK YPASAQSVTN TSSVGRASLG LNSQLKGKKP 610 620 630 640 650 660 PVASNGVTGK GKTLSSQPKK ADPAAVVKRT GSNAAQYKYG KNRVEADAKR LQTKEEELLK 670 680 690 700 710 720 RKEALRNRLA QLRKERKDLR AAIEVNAGRK PQAILEEKLK QLEEECRQKE AERVSLELEL 730 740 750 760 770 780 TEVKESLKKA LAGGVTLGLA IEPKSGTSSP QSPVFRHRTL ENSPISSCDT SDTEGPVPVN 790 800 810 SAAVLKKSQA APGSSPCRGH VLRKAKEWEL KNGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conversion of mechanical force into biochemical signaling." Han B., Bai X.H., Lodyga M., Xu J., Yang B.B., Keshavjee S., Post M., Liu M. J. Biol. Chem. 279:54793-54801(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRC, PHOSPHORYLATION BY SRC, MUTAGENESIS OF PRO-71; PRO-77; TYR-93; TYR-94; TYR-125; TYR-451 AND TYR-453. Tissue: Lung.
[2]	"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), VARIANT CYS-403. Tissue: Brain and Kidney.
[3]	"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].
[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] (ISOFORM 1), VARIANT CYS-403. Tissue: Brain.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-730 (ISOFORM 1), VARIANT MET-518. Tissue: Brain.
[6]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells." Dorfleutner A., Stehlik C., Zhang J., Gallick G.E., Flynn D.C. J. Cell. Physiol. 213:740-749(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, KNOCKDOWN IN MDA-MB-231 CELLS.
[8]	"AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts." Zhang J., Park S.I., Artime M.C., Summy J.M., Shah A.N., Bomser J.A., Dorfleutner A., Flynn D.C., Gallick G.E. J. Clin. Invest. 117:2962-2973(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, POSSIBLE FUNCTION IN PROSTATE CANCER PROGRESSION.
[9]	"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-282; SER-283; SER-664; SER-665; SER-668; SER-679 AND SER-687, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-548 AND SER-668, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF188700 mRNA. Translation: AAG17055.1. AK290807 mRNA. Translation: BAF83496.1. AK297631 mRNA. Translation: BAG60004.1. AC004169 Genomic DNA. No translation available. AC097381 Genomic DNA. No translation available. AC112254 Genomic DNA. No translation available. AC141931 Genomic DNA. No translation available. AC144451 Genomic DNA. No translation available. BC032777 mRNA. Translation: AAH32777.1. AB209676 mRNA. Translation: BAD92913.1.
IPI	IPI00398154. IPI00910135.
RefSeq	NP_001128119.1. NM_001134647.1. NP_940997.1. NM_198595.2.
UniGene	Hs.529369.
3D structure databases
HSSP	HSSP built from PDB template 2COF based on UniProtKB Q8N4X5.
ProteinModelPortal	Q8N556.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N556. 1 interaction.
STRING	9606.ENSP00000410689.
PTM databases
PhosphoSite	Q8N556.
Polymorphism databases
DMDM	166919564.
Proteomic databases
PaxDb	Q8N556.
PRIDE	Q8N556.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358461; ENSP00000351245; ENSG00000196526. ENST00000360265; ENSP00000353402; ENSG00000196526. ENST00000382543; ENSP00000371983; ENSG00000196526. ENST00000420658; ENSP00000410689; ENSG00000196526.
GeneID	60312.
KEGG	hsa:60312.
UCSC	uc003gkg.1. human.
Organism-specific databases
CTD	60312.
GeneCards	GC04M007682.
H-InvDB	HIX0031430.
HGNC	HGNC:24017. AFAP1.
HPA	CAB024712. HPA015642.
MIM	608252. gene.
neXtProt	NX_Q8N556.
PharmGKB	PA162375733.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG48103.
HOGENOM	HOG000033832.
HOVERGEN	HBG106875.
InParanoid	Q8N556.
OMA	SPVHKTE.
OrthoDB	EOG4J117M.
PhylomeDB	Q8N556.
Gene expression databases
ArrayExpress	Q8N556.
Bgee	Q8N556.
CleanEx	HS_AFAP1.
Genevestigator	Q8N556.
Family and domain databases
Gene3D	2.30.29.30. 2 hits.
InterPro	IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. [Graphical view]
Pfam	PF00169. PH. 2 hits. [Graphical view]
SMART	SM00233. PH. 2 hits. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AFAP1. human.
GenomeRNAi	60312.
NextBio	65281.
SOURCE	Search...

Entry information

Entry name

AFAP1_HUMAN

Accession

Primary (citable) accession number: Q8N556
Secondary accession number(s): A8K442 , B4DMU2, E9PDT7, Q59EY5, Q9HBY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 77 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.