Q13435 (SF3B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Splicing factor 3B subunit 2

Alternative name(s):
Pre-mRNA-splicing factor SF3b 145 kDa subunit
Short name=SF3b145
SF3b150
Spliceosome-associated protein 145
Short name=SAP 145

Gene names

Name:	SF3B2
Synonyms:	SAP145

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

General annotation (Comments)

Function	Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.
Subunit structure	Identified in the spliceosome C complex. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of splicing factor SF3B which is composed of at least eight subunits; SF3B1/SAP155/SF3B155, SF3B2/SAP145/SF3B145, SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B14A, PHF5A/SF3B14B, SF3B10 and SF3B125. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). SF3B2 interacts directly with SF3B4. Interacts with HIV-1 Vpr. Ref.10
Subcellular location	Nucleus By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Sequence similarities	Contains 1 SAP domain.
Sequence caution	The sequence AAA97461.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAA97461.1 differs from that shown. Reason: Frameshift at position 28. The sequence AAH53577.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAG61831.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Host-virus interaction mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW nuclear mRNA splicing, via spliceosome Inferred by curator Ref.6. Source: UniProtKB
Cellular component	U12-type spliceosomal complex Inferred from direct assay Ref.8. Source: UniProtKB catalytic step 2 spliceosome Inferred from direct assay Ref.6. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 895

895

Splicing factor 3B subunit 2

PRO_0000174328

Regions

Domain

24 – 58

35

SAP

Coiled coil

140 – 199

60

Potential

Compositional bias

16 – 21

6

Poly-Pro

Compositional bias

91 – 96

6

Poly-Pro

Compositional bias

104 – 113

10

Poly-Pro

Compositional bias

129 – 132

4

Poly-Pro

Compositional bias

249 – 253

5

Poly-Pro

Compositional bias

292 – 297

6

Poly-Glu

Compositional bias

331 – 335

5

Poly-Lys

Compositional bias

699 – 702

4

Poly-Glu

Compositional bias

720 – 726

7

Poly-Glu

Amino acid modifications

Modified residue

201

1

Phosphothreonine Ref.16

Modified residue

217

1

Phosphothreonine Ref.16

Modified residue

275

1

N6-acetyllysine Ref.20

Modified residue

289

1

Phosphoserine Ref.13 Ref.16

Modified residue

307

1

Phosphoserine Ref.11 Ref.15 Ref.16 Ref.18 Ref.19

Modified residue

309

1

Phosphoserine Ref.11 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19

Modified residue

311

1

Phosphothreonine Ref.14 Ref.16

Modified residue

343

1

Phosphoserine Ref.12

Modified residue

360

1

Phosphoserine Ref.12 Ref.19

Modified residue

362

1

Phosphoserine Ref.9 Ref.19

Modified residue

416

1

Phosphoserine Ref.9

Modified residue

431

1

Phosphoserine Ref.9 Ref.12 Ref.16 Ref.17

Modified residue

435

1

Phosphoserine Ref.9 Ref.12 Ref.16 Ref.17

Modified residue

436

1

Phosphoserine Ref.9 Ref.12 Ref.16 Ref.17

Modified residue

778

1

Phosphoserine Ref.12

Modified residue

780

1

Phosphothreonine Ref.12 Ref.16 Ref.18 Ref.19

Experimental info

Sequence conflict

602

1

K → E in BAF83539. Ref.1

Sequence conflict

765

1

E → G in BAF83539. Ref.1

Secondary structure

1

.

.

.

.

.

895

Helix Strand Turn

Details...

Helix

29 – 38

10

Helix

47 – 60

14

Sequences

	Sequence		Length	Mass (Da)
	Q13435 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: D372AFA679443AD6	FASTA	895	100,228
	10 20 30 40 50 60 MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL VERLQSYTRQ 70 80 90 100 110 120 TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP PLQPPPPPPP PPPGLGLGFP 130 140 150 160 170 180 MAHPPNLGPP PPLRVGEPVA LSEEERLKLA QQQAALLMQQ EERAKQQGDH SLKEHELLEQ 190 200 210 220 230 240 QKRAAVLLEQ ERQQEIAKMG TPVPRPPQDM GQIGVRTPLG PRVAAPVGPV GPTPTVLPMG 250 260 270 280 290 300 APVPRPRGPP PPPGDENREM DDPSVGPKIP QALEKILQLK ESRQEEMNSQ QEEEEMETDA 310 320 330 340 350 360 RSSLGQSASE TEEDTVSVSK KEKNRKRRNR KKKKKPQRVR GVSSESSGDR EKDSTRSRGS 370 380 390 400 410 420 DSPAADVEIE YVTEEPEIYE PNFIFFKRIF EAFKLTDDVK KEKEKEPEKL DKLENSAAPK 430 440 450 460 470 480 KKGFEEEHKD SDDDSSDDEQ EKKPEAPKLS KKKLRRMNRF TVAELKQLVA RPDVVEMHDV 490 500 510 520 530 540 TAQDPKLLVH LKATRNSVPV PRHWCFKRKY LQGKRGIEKP PFELPDFIKR TGIQEMREAL 550 560 570 580 590 600 QEKEEQKTMK SKMREKVRPK MGKIDIDYQK LHDAFFKWQT KPKLTIHGDL YYEGKEFETR 610 620 630 640 650 660 LKEKKPGDLS DELRISLGMP VGPNAHKVPP PWLIAMQRYG PPPSYPNLKI PGLNSPIPES 670 680 690 700 710 720 CSFGYHAGGW GKPPVDETGK PLYGDVFGTN AAEFQTKTEE EEIDRTPWGE LEPSDEESSE 730 740 750 760 770 780 EEEEEESDED KPDETGFITP ADSGLITPGG FSSVPAGMET PELIELRKKK IEEAMDGSET 790 800 810 820 830 840 PQLFTVLPEK RTATVGGAMM GSTHIYDMST VMSRKGPAPE LQGVEVALAP EELELDPMAM 850 860 870 880 890 TQKYEEHVRE QQAQVEKEDF SDMVAEHAAK QKQKKRKAQP QDSRGGSKKY KEFKF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Lymphoblast and Peripheral blood.
[2]	"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]. Tissue: Eye, Kidney, Lung and Testis.
[3]	"Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A." Gozani O., Feld R., Reed R. Genes Dev. 10:233-243(1996) [PubMed: 8566756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-895, PROTEIN SEQUENCE OF 174-182 AND 817-840. Tissue: Cervix carcinoma.
[4]	"Functional association of U2 snRNP with the ATP-independent spliceosomal complex E." Das R., Zhou Z., Reed R. Mol. Cell 5:779-787(2000) [PubMed: 10882114] [Abstract] Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
[5]	"Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein." Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R. EMBO J. 21:4978-4988(2002) [PubMed: 12234937] [Abstract] Cited for: IDENTIFICATION IN THE SF3B COMPLEX.
[6]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[7]	"Molecular architecture of the multiprotein splicing factor SF3b." Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H. Science 300:980-984(2003) [PubMed: 12738865] [Abstract] Cited for: IDENTIFICATION IN THE SF3B COMPLEX, ELECTRON MICROSCOPY OF THE SF3B COMPLEX.
[8]	"The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome." Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R. RNA 10:929-941(2004) [PubMed: 15146077] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, MASS SPECTROMETRY.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-416; SER-431; SER-435 AND SER-436, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145." Terada Y., Yasuda Y. Mol. Cell. Biol. 26:8149-8158(2006) [PubMed: 16923959] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-309, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-360; SER-431; SER-435; SER-436; SER-778 AND THR-780, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND THR-311, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-309, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; THR-217; SER-289; SER-307; SER-309; THR-311; SER-431; SER-435; SER-436 AND THR-780, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435 AND SER-436, MASS SPECTROMETRY. Tissue: Liver.
[18]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-309 AND THR-780, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-309; SER-360; SER-362 AND THR-780, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275, MASS SPECTROMETRY.
[21]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"Solution structure of the SAP domain of human splicing factor 3B subunit 2." RIKEN structural genomics initiative (RSGI) Submitted (APR-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 24-68.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK290850 mRNA. Translation: BAF83539.1.
AK300016 mRNA. Translation: BAG61831.1. Different initiation.
BC000401 mRNA. Translation: AAH00401.2.
BC007610 mRNA. Translation: AAH07610.1.
BC014125 mRNA. Translation: AAH14125.2.
BC053577 mRNA. Translation: AAH53577.1. Sequence problems.
U41371 mRNA. Translation: AAA97461.1. Frameshift.

IPI

IPI00221106.

RefSeq

NP_006833.2. NM_006842.2.

UniGene

Hs.406423.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DO5	NMR	-	A	24-68	[»]

ProteinModelPortal

Q13435.

SMR

Q13435. Positions 26-68.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13435. 7 interactions.

MINT

MINT-4915443.

STRING

Q13435.

PTM databases

PhosphoSite

Q13435.

Polymorphism databases

DMDM

296452908.

Proteomic databases

PRIDE

Q13435.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322535; ENSP00000318861; ENSG00000087365.
ENST00000355456; ENSP00000347631; ENSG00000087365.

GeneID

10992.

KEGG

hsa:10992.

Organism-specific databases

CTD

10992.

GeneCards

GC11P065827.

H-InvDB

HIX0009823.

HGNC

HGNC:10769. SF3B2.

HPA

HPA045028.

MIM

605591. gene.

neXtProt

NX_Q13435.

PharmGKB

PA35687.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05951.

GeneTree

ENSGT00390000006734.

HOVERGEN

HBG054023.

InParanoid

Q13435.

OMA

TRQTGMV.

OrthoDB

EOG4GB75Q.

PhylomeDB

Q13435.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q13435.

Bgee

Q13435.

CleanEx

HS_SF3B2.

Genevestigator

Q13435.

GermOnline

ENSG00000087365. Homo sapiens.

Family and domain databases

InterPro

IPR007180. DUF382.
IPR006568. PSP.
IPR003034. SAP_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.

KO

K12829.

Pfam

PF04037. DUF382. 1 hit.
PF04046. PSP. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]

SMART

SM00581. PSP. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]

PROSITE

PS50800. SAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

PMAP-CutDB

Q13435.

SOURCE

Search...

Entry information

Entry name

SF3B2_HUMAN

Accession

Primary (citable) accession number: Q13435
Secondary accession number(s): A8K485 , B4DT19, Q7L4T5, Q7Z627, Q969K1, Q96CM6, Q9BWD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 108 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.