Q00722 (PLCB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase C-beta-2
Phospholipase C-beta-2
Short name=PLC-beta-2

Gene names

Name:

PLCB2

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	1185 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Binds 1 calcium ion per subunit.
Subunit structure	Interacts with RAC1.
Miscellaneous	The receptor-mediated activation of PLC-beta-2 is most effectively mediated by one G-protein alpha subunit, alpha-16.
Sequence similarities	Contains 1 C2 domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of phospholipase C activity Traceable author statement PubMed 7649993. Source: ProtInc intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Traceable author statement Ref.1. Source: ProtInc sensory perception of bitter taste Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Traceable author statement Ref.1. Source: ProtInc signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q00722-1)

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: Q00722-2)

The sequence of this isoform differs from the canonical sequence as follows:
     492-495: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1185

1185

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2

PRO_0000088489

Regions

Domain

312 – 463

152

PI-PLC X-box

Domain

546 – 662

117

PI-PLC Y-box

Domain

669 – 767

99

C2

Coiled coil

988 – 1147

160

Potential

Compositional bias

500 – 545

46

Glu-rich

Sites

Active site

327

1

By similarity

Active site

374

1

By similarity

Metal binding

328

1

Calcium

Metal binding

357

1

Calcium

Metal binding

359

1

Calcium

Metal binding

408

1

Calcium

Natural variations

Alternative sequence

492 – 495

4

Missing in isoform 2.

VSP_035770

Natural variant

324

1

N → I.
Corresponds to variant rs45628633 [ dbSNP | Ensembl ].

VAR_047509

Natural variant

598

1

R → H.
Corresponds to variant rs8025153 [ dbSNP | Ensembl ].

VAR_047510

Natural variant

664

1

P → L.
Corresponds to variant rs9972332 [ dbSNP | Ensembl ].

VAR_047511

Natural variant

712

1

G → R.
Corresponds to variant rs28395835 [ dbSNP | Ensembl ].

VAR_047512

Natural variant

1095

1

E → G. Ref.2
Corresponds to variant rs936212 [ dbSNP | Ensembl ].

VAR_047513

Experimental info

Mutagenesis

52

1

Q → A: Strongly reduces interaction with RAC1. Ref.4

Sequence conflict

119

1

K → R in BAF84346. Ref.2

Sequence conflict

1060

1

K → R in BAF84346. Ref.2

Secondary structure

1

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1185

Helix Strand Turn

Details...

Helix

15 – 19

5

Beta strand

21 – 26

6

Turn

28 – 30

3

Beta strand

33 – 40

8

Beta strand

46 – 51

6

Beta strand

56 – 60

5

Helix

61 – 63

3

Beta strand

64 – 69

6

Helix

70 – 72

3

Helix

79 – 84

6

Turn

85 – 88

4

Helix

94 – 96

3

Beta strand

98 – 103

6

Beta strand

105 – 109

5

Beta strand

111 – 121

11

Helix

122 – 135

14

Helix

139 – 141

3

Helix

144 – 157

14

Helix

167 – 173

7

Helix

178 – 187

10

Beta strand

193 – 195

3

Helix

200 – 202

3

Helix

205 – 215

11

Helix

219 – 222

4

Helix

238 – 247

10

Helix

267 – 274

8

Helix

288 – 296

9

Helix

305 – 308

4

Helix

318 – 320

3

Beta strand

321 – 323

3

Beta strand

325 – 328

4

Beta strand

331 – 333

3

Beta strand

335 – 338

4

Helix

343 – 350

8

Beta strand

355 – 361

7

Turn

365 – 368

4

Helix

384 – 394

11

Turn

395 – 397

3

Beta strand

403 – 409

7

Helix

414 – 428

15

Helix

429 – 431

3

Turn

451 – 456

6

Beta strand

458 – 461

4

Helix

523 – 531

9

Helix

534 – 538

5

Helix

544 – 547

4

Helix

561 – 567

7

Beta strand

572 – 577

6

Helix

578 – 587

10

Helix

589 – 598

10

Beta strand

599 – 604

6

Helix

618 – 622

5

Beta strand

626 – 628

3

Helix

637 – 645

9

Turn

646 – 648

3

Helix

649 – 651

3

Beta strand

653 – 656

4

Helix

659 – 661

3

Turn

675 – 680

6

Beta strand

682 – 693

12

Beta strand

701 – 708

8

Beta strand

724 – 726

3

Beta strand

738 – 745

8

Helix

746 – 748

3

Beta strand

750 – 757

8

Turn

758 – 760

3

Beta strand

761 – 769

9

Helix

770 – 772

3

Beta strand

776 – 783

8

Beta strand

789 – 799

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: A0397309D943672A	FASTA	1,185	134,024
	10 20 30 40 50 60 MSLLNPVLLP PKVKAYLSQG ERFIKWDDET TVASPVILRV DPKGYYLYWT YQSKEMEFLD 70 80 90 100 110 120 ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT VVSGPDMVDL TFHNFVSYKE 130 140 150 160 170 180 NVGKAWAEDV LALVKHPLTA NASRSTFLDK ILVKLKMQLN SEGKIPVKNF FQMFPADRKR 190 200 210 220 230 240 VEAALSACHL PKGKNDAINP EDFPEPVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH 250 260 270 280 290 300 LTKFINQKQR DSRLNSLLFP PARPDQVQGL IDKYEPSGIN AQRGQLSPEG MVWFLCGPEN 310 320 330 340 350 360 SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC 370 380 390 400 410 420 WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP YPIILSFENH VDSPRQQAKM 430 440 450 460 470 480 AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS PEDLRGKILI KNKKNQFSGP TSSSKDTGGE 490 500 510 520 530 540 AEGSSPPSAP AGEGTVWAGE EGTELEEEEV EEEEEEESGN LDEEEIKKMQ SDEGTAGLEV 550 560 570 580 590 600 TAYEEMSSLV NYIQPTKFVS FEFSAQKNRS YVISSFTELK AYDLLSKASV QFVDYNKRQM 610 620 630 640 650 660 SRIYPKGTRM DSSNYMPQMF WNAGCQMVAL NFQTMDLPMQ QNMAVFEFNG QSGYLLKHEF 670 680 690 700 710 720 MRRPDKQFNP FSVDRIDVVV ATTLSITVIS GQFLSERSVR TYVEVELFGL PGDPKRRYRT 730 740 750 760 770 780 KLSPSTNSIN PVWKEEPFVF EKILMPELAS LRVAVMEEGN KFLGHRIIPI NALNSGYHHL 790 800 810 820 830 840 CLHSESNMPL TMPALFIFLE MKDYIPGAWA DLTVALANPI KFFSAHDTKS VKLKEAMGGL 850 860 870 880 890 900 PEKPFPLASP VASQVNGALA PTSNGSPAAR AGAREEAMKE AAEPRTASLE ELRELKGVVK 910 920 930 940 950 960 LQRRHEKELR ELERRGARRW EELLQRGAAQ LAELGPPGVG GVGACKLGPG KGSRKKRSLP 970 980 990 1000 1010 1020 REESAGAAPG EGPEGVDGRV RELKDRLELE LLRQGEEQYE CVLKRKEQHV AEQISKMMEL 1030 1040 1050 1060 1070 1080 AREKQAAELK ALKETSENDT KEMKKKLETK RLERIQGMTK VTTDKMAQER LKREINNSHI 1090 1100 1110 1120 1130 1140 QEVVQVIKQM TENLERHQEK LEEKQAACLE QIREMEKQFQ KEALAEYEAR MKGLEAEVKE 1150 1160 1170 1180 SVRACLRTCF PSEAKDKPER ACECPPELCE QDPLIAKADA QESRL
	Isoform 2 [UniParc]. Checksum: 7A6889F204D17FA4	FASTA	1,181	133,680
	10 20 30 40 50 60 MSLLNPVLLP PKVKAYLSQG ERFIKWDDET TVASPVILRV DPKGYYLYWT YQSKEMEFLD 70 80 90 100 110 120 ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT VVSGPDMVDL TFHNFVSYKE 130 140 150 160 170 180 NVGKAWAEDV LALVKHPLTA NASRSTFLDK ILVKLKMQLN SEGKIPVKNF FQMFPADRKR 190 200 210 220 230 240 VEAALSACHL PKGKNDAINP EDFPEPVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH 250 260 270 280 290 300 LTKFINQKQR DSRLNSLLFP PARPDQVQGL IDKYEPSGIN AQRGQLSPEG MVWFLCGPEN 310 320 330 340 350 360 SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC 370 380 390 400 410 420 WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP YPIILSFENH VDSPRQQAKM 430 440 450 460 470 480 AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS PEDLRGKILI KNKKNQFSGP TSSSKDTGGE 490 500 510 520 530 540 AEGSSPPSAP AVWAGEEGTE LEEEEVEEEE EEESGNLDEE EIKKMQSDEG TAGLEVTAYE 550 560 570 580 590 600 EMSSLVNYIQ PTKFVSFEFS AQKNRSYVIS SFTELKAYDL LSKASVQFVD YNKRQMSRIY 610 620 630 640 650 660 PKGTRMDSSN YMPQMFWNAG CQMVALNFQT MDLPMQQNMA VFEFNGQSGY LLKHEFMRRP 670 680 690 700 710 720 DKQFNPFSVD RIDVVVATTL SITVISGQFL SERSVRTYVE VELFGLPGDP KRRYRTKLSP 730 740 750 760 770 780 STNSINPVWK EEPFVFEKIL MPELASLRVA VMEEGNKFLG HRIIPINALN SGYHHLCLHS 790 800 810 820 830 840 ESNMPLTMPA LFIFLEMKDY IPGAWADLTV ALANPIKFFS AHDTKSVKLK EAMGGLPEKP 850 860 870 880 890 900 FPLASPVASQ VNGALAPTSN GSPAARAGAR EEAMKEAAEP RTASLEELRE LKGVVKLQRR 910 920 930 940 950 960 HEKELRELER RGARRWEELL QRGAAQLAEL GPPGVGGVGA CKLGPGKGSR KKRSLPREES 970 980 990 1000 1010 1020 AGAAPGEGPE GVDGRVRELK DRLELELLRQ GEEQYECVLK RKEQHVAEQI SKMMELAREK 1030 1040 1050 1060 1070 1080 QAAELKALKE TSENDTKEMK KKLETKRLER IQGMTKVTTD KMAQERLKRE INNSHIQEVV 1090 1100 1110 1120 1130 1140 QVIKQMTENL ERHQEKLEEK QAACLEQIRE MEKQFQKEAL AEYEARMKGL EAEVKESVRA 1150 1160 1170 1180 CLRTCFPSEA KDKPERACEC PPELCEQDPL IAKADAQESR L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2." Park D., Jhon D.-Y., Kriz R., Knopf J., Rhee S.G. J. Biol. Chem. 267:16048-16055(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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] (ISOFORM 1), VARIANT GLY-1095. Tissue: Placenta.
[3]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Crystal structure of Rac1 bound to its effector phospholipase C-beta2." Jezyk M.R., Snyder J.T., Gershberg S., Worthylake D.K., Harden T.K., Sondek J. Nat. Struct. Mol. Biol. 13:1135-1140(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-803 (ISOFORM 2) IN COMPLEX WITH RAC1, MUTAGENESIS OF GLN-52.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M95678 mRNA. Translation: AAA36453.1.
AK291657 mRNA. Translation: BAF84346.1.
AC020658 Genomic DNA. No translation available.

IPI

IPI00784327.
IPI00914935.

PIR

A43346.

RefSeq

NP_004564.2. NM_004573.2.

UniGene

Hs.355888.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FJU	X-ray	2.20	B	1-803	[»]
2ZKM	X-ray	1.62	X	1-799	[»]

ProteinModelPortal

Q00722.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29259N.

STRING

9606.ENSP00000260402.

PTM databases

PhosphoSite

Q00722.

Polymorphism databases

DMDM

215273902.

Proteomic databases

PaxDb

Q00722.

PRIDE

Q00722.

Protocols and materials databases

DNASU

5330.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260402; ENSP00000260402; ENSG00000137841.
ENST00000557821; ENSP00000453975; ENSG00000137841.

GeneID

5330.

KEGG

hsa:5330.

UCSC

uc001zld.3. human.
uc010bbo.3. human.

Organism-specific databases

CTD

5330.

GeneCards

GC15M040580.

H-InvDB

HIX0012125.

HGNC

HGNC:9055. PLCB2.

HPA

CAB009443.

MIM

604114. gene.

neXtProt

NX_Q00722.

PharmGKB

PA33385.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG149692.

HOGENOM

HOG000232046.

HOVERGEN

HBG053609.

InParanoid

Q00722.

KO

K05858.

OMA

FIKWDDE.

Enzyme and pathway databases

BioCyc

MetaCyc:HS06408-MONOMER.

BRENDA

3.1.4.11. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
endothelinpathway. Endothelins.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
s1p_s1p1_pathway. S1P1 pathway.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q00722.

Bgee

Q00722.

CleanEx

HS_PLCB2.

Genevestigator

Q00722.

GermOnline

ENSG00000137841. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.
3.20.20.190. 2 hits.

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR011992. EF-hand-like_dom.
IPR001192. Pinositol_PLipase_C.
IPR016280. PLC-beta.
IPR014815. PLC-beta_C.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]

PANTHER

PTHR10336. PTHR10336. 1 hit.

Pfam

PF00168. C2. 1 hit.
PF09279. efhand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF08703. PLC-beta_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000956. PLC-beta. 1 hit.

PRINTS

PR00390. PHPHLIPASEC.

SMART

SM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.

PROSITE

PS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3620.

ChiTaRS

PLCB2. human.

EvolutionaryTrace

Q00722.

GenomeRNAi

5330.

NextBio

20640.

SOURCE

Search...

Entry information

Entry name

PLCB2_HUMAN

Accession

Primary (citable) accession number: Q00722
Secondary accession number(s): A8K6J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 131 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.