P01233 (CGHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Choriogonadotropin subunit beta
Short name=CG-beta

Alternative name(s):
Chorionic gonadotrophin chain beta

Gene names

Name:	CGB
Synonyms:	CGB3
AND
Name:	CGB5
AND
Name:	CGB7
AND
Name:	CGB8

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	165 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.
Subunit structure	Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin.
Subcellular location	Secreted.
Tissue specificity	Placenta.
Developmental stage	Made by the first trimester placenta.
Pharmaceutical use	Available under the names Novarel (Ferring) and Profasi (Serono). Used as adjunctive therapy in the treatment of obesity. There is no substantial evidence that it increases weight loss beyond that resulting from caloric restriction, that it causes a more attractive or 'normal' distribution of fat, or that it decreases the hunger and discomfort associated with calorie-restricted diets.
Sequence similarities	Belongs to the glycoprotein hormones subunit beta family.
Sequence caution	The sequence CAA25068.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA25069.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Traceable author statement PubMed 7723844. Source: ProtInc cell-cell signaling Traceable author statement Ref.3. Source: ProtInc cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome female gamete generation Traceable author statement PubMed 10468638. Source: ProtInc peptide hormone processing Traceable author statement. Source: Reactome signal transduction Traceable author statement PubMed 10468638. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	hormone activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P01233-1)

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: P01233-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MEMF → MGRPGLGAAVSDPGEAVSLS

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.1 Ref.12 Ref.13

Chain

21 – 165

145

Choriogonadotropin subunit beta

PRO_0000011676

Amino acid modifications

Glycosylation

33

1

N-linked (GlcNAc...)

CAR_000042

Glycosylation

50

1

N-linked (GlcNAc...)

CAR_000043

Glycosylation

141

1

O-linked (GalNAc...) Ref.12

Glycosylation

147

1

O-linked (GalNAc...) Ref.12

Glycosylation

152

1

O-linked (GalNAc...) Ref.12

Glycosylation

158

1

O-linked (GalNAc...) Ref.12

Disulfide bond

29 ↔ 77

Ref.14 Ref.15 Ref.17

Disulfide bond

43 ↔ 92

Ref.14 Ref.15 Ref.17

Disulfide bond

46 ↔ 130

Ref.14 Ref.15 Ref.17

Disulfide bond

54 ↔ 108

Ref.14 Ref.15 Ref.17

Disulfide bond

58 ↔ 110

Ref.14 Ref.15 Ref.17

Disulfide bond

113 ↔ 120

Ref.14 Ref.15 Ref.17

Natural variations

Alternative sequence

1 – 4

4

MEMF → MGRPGLGAAVSDPGEAVSLS in isoform 2.

VSP_038396

Natural variant

4

1

F → L. Ref.8
Corresponds to variant rs6516 [ dbSNP | Ensembl ].

VAR_014585

Natural variant

18

1

T → A. Ref.11

VAR_015231

Natural variant

22

1

K → R. Ref.11
Corresponds to variant rs6518 [ dbSNP | Ensembl ].

VAR_014586

Natural variant

24

1

P → M Requires 2 nucleotide substitutions. Ref.3 Ref.11

VAR_015232

Natural variant

28

1

R → W. Ref.11

VAR_015233

Natural variant

30

1

R → H. Ref.11

VAR_015234

Natural variant

35

1

T → I. Ref.11
Corresponds to variant rs6515 [ dbSNP | Ensembl ].

VAR_014587

Natural variant

97

1

N → D.
Corresponds to variant rs6519 [ dbSNP | Ensembl ].

VAR_014588

Natural variant

137

1

D → A in gene 6. Ref.2 Ref.3 Ref.8 Ref.11
Corresponds to variant rs7452 [ dbSNP | Ensembl ].

VAR_003188

Natural variant

147

1

S → C. Ref.11

VAR_015235

Experimental info

Sequence conflict

123

1

P → T in AAL69709. Ref.11

Isoform 2:

Sequence conflict

7

1

G → R in CAA25069. Ref.2

Sequence conflict

9

1

A → V in CAA25069. Ref.2

Sequence conflict

12

1

D → G in CAA25069. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

165

Helix Strand Turn

Details...

Beta strand

25 – 38

14

Beta strand

47 – 60

14

Beta strand

75 – 88

14

Beta strand

99 – 112

14

Turn

115 – 117

3

Beta strand

118 – 121

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 5598FB9E51A05748	FASTA	165	17,739
	10 20 30 40 50 60 MEMFQGLLLL LLLSMGGTWA SKEPLRPRCR PINATLAVEK EGCPVCITVN TTICAGYCPT 70 80 90 100 110 120 MTRVLQGVLP ALPQVVCNYR DVRFESIRLP GCPRGVNPVV SYAVALSCQC ALCRRSTTDC 130 140 150 160 GGPKDHPLTC DDPRFQDSSS SKAPPPSLPS PSRLPGPSDT PILPQ
	Isoform 2 [UniParc]. Checksum: 853B736271867359	FASTA	181	19,053
	10 20 30 40 50 60 MGRPGLGAAV SDPGEAVSLS QGLLLLLLLS MGGTWASKEP LRPRCRPINA TLAVEKEGCP 70 80 90 100 110 120 VCITVNTTIC AGYCPTMTRV LQGVLPALPQ VVCNYRDVRF ESIRLPGCPR GVNPVVSYAV 130 140 150 160 170 180 ALSCQCALCR RSTTDCGGPK DHPLTCDDPR FQDSSSSKAP PPSLPSPSRL PGPSDTPILP Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cDNA for the beta-subunit of human chorionic gonadotropin suggests evolution of a gene by readthrough into the 3'-untranslated region." Fiddes J.C., Goodman H.M. Nature 286:684-687(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Evolution of the genes for the beta subunits of human chorionic gonadotropin and luteinizing hormone." Talmadge K., Vamvakopoulos N.C., Fiddes J.C. Nature 307:37-40(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-137.
[3]	"The beta subunit of human chorionic gonadotropin is encoded by multiple genes." Policastro P., Ovitt C.E., Hoshina M., Fukuoka H., Boothby M.R., Boime I. J. Biol. Chem. 258:11492-11499(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-24 AND ALA-137.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"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). Tissue: Placenta.
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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].
[8]	"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), VARIANTS LEU-4 AND ALA-137. Tissue: Brain and Placenta.
[9]	"The amino acid sequences of the prepeptides contained in the alpha and beta subunits of human choriogonadotropin." Birken S., Fetherston J., Canfield R.E., Boime I. J. Biol. Chem. 256:1816-1823(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20.
[10]	"A map of the hCG beta-LH beta gene cluster." Policastro P.F., Daniels-Mcqueen S., Carle G., Boime I. J. Biol. Chem. 261:5907-5916(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
[11]	"Chorionic gonadotropin has a recent origin within primates and an evolutionary history of selection." Maston G.A., Ruvolo M. Mol. Biol. Evol. 19:320-335(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-164, VARIANTS ALA-18; ARG-22; MET-24; TRP-28; HIS-30; ILE-35; ALA-137 AND CYS-147.
[12]	"The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit." Morgan F.J., Birken S., Canfield R.E. J. Biol. Chem. 250:5247-5258(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-165.
[13]	"Human chorionic gonadotropin. Linear amino acid sequence of the beta subunit." Carlsen R.B., Bahl O.P., Swaminathan N. J. Biol. Chem. 248:6810-6827(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 21-165.
[14]	"Assignment of disulfide bonds in the beta subunit of human chorionic gonadotropin." Mise T., Bahl O.P. J. Biol. Chem. 256:6587-6592(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
[15]	"Role of disulfide bond formation in the folding of human chorionic gonadotropin beta subunit into an alpha beta dimer assembly-competent form." Saccuzo Beebe J., Mountjoy K., Krzesicki R.F., Perini F., Ruddon R.W. J. Biol. Chem. 265:312-317(1990) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[16]	"Site-specific N-glycosylation of human chorionic gonadotrophin --structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy." Weisshaar G., Hiyama J., Renwick A.G.C. Glycobiology 1:393-404(1991) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES.
[17]	"Crystal structure of human chorionic gonadotropin." Lapthorn A.J., Harris D.C., Littlejohn A., Lustbader J.W., Canfield R.E., Machin K.J., Morgan F.J., Isaacs N.W. Nature 369:455-461(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Wikipedia

Chorionic gonadotropin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00117 mRNA. Translation: AAA96690.1.
X00265 Genomic DNA. Translation: CAA25068.1. Different initiation.
X00266 Genomic DNA. Translation: CAA25069.1. Different initiation.
K03189, K03187, K03188 Genomic DNA. Translation: AAA53288.1.
K03183, K00092, K03182 Genomic DNA. Translation: AAA53287.1.
BT006890 mRNA. Translation: AAP35536.1.
AK291552 mRNA. Translation: BAF84241.1.
AC008687 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52434.1.
CH471177 Genomic DNA. Translation: EAW52437.1.
CH471177 Genomic DNA. Translation: EAW52438.1.
CH471177 Genomic DNA. Translation: EAW52439.1.
BC006290 mRNA. Translation: AAH06290.1.
BC022796 mRNA. Translation: AAH22796.1.
BC030994 mRNA. Translation: AAH30994.1.
BC041054 mRNA. Translation: AAH41054.1.
BC051378 mRNA. Translation: AAH51378.1.
BC069526 mRNA. Translation: AAH69526.1.
BC103969 mRNA. Translation: AAI03970.1.
BC103970 mRNA. Translation: AAI03971.1.
BC103971 mRNA. Translation: AAI03972.1.
BC106059 mRNA. Translation: AAI06060.1.
BC106723 mRNA. Translation: AAI06724.1.
BC106724 mRNA. Translation: AAI06725.1.
BC128603 mRNA. Translation: AAI28604.1.
M13503 Genomic DNA. Translation: AAA52009.1.
M13504 Genomic DNA. Translation: AAA52005.1.
M13505 Genomic DNA. Translation: AAA52008.1.
AF397576 Genomic DNA. Translation: AAL69704.1.
AF397577 Genomic DNA. Translation: AAL69705.1.
AF397578 Genomic DNA. Translation: AAL69706.1.
AF397579 Genomic DNA. Translation: AAL69707.1.
AF397580 Genomic DNA. Translation: AAL69708.1.
AF397581 Genomic DNA. Translation: AAL69709.1.

IPI

IPI00000870.
IPI00954109.

PIR

KTHUB. A93230.
I37231.

RefSeq

NP_000728.1. NM_000737.3.
NP_149032.1. NM_033043.1.
NP_149133.1. NM_033142.1.
NP_149439.1. NM_033183.2.

UniGene

Hs.172944.
Hs.446683.
Hs.659014.
Hs.681647.
Hs.740996.
Hs.741782.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HCN	X-ray	2.60	B	21-165	[»]
1HRP	X-ray	3.00	B	21-165	[»]
1QFW	X-ray	3.50	B	21-165	[»]
1XUL	model	-	B	21-165	[»]

DisProt

DP00013.

ProteinModelPortal

P01233.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6183N.

PTM databases

GlycoSuiteDB

P01233.

PhosphoSite

P01233.

Proteomic databases

PaxDb

P01233.

PeptideAtlas

P01233.

PRIDE

P01233.

Protocols and materials databases

DNASU

1082.
93659.
94027.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301408; ENSP00000301408; ENSG00000189052.
ENST00000357383; ENSP00000349954; ENSG00000104827.
ENST00000377280; ENSP00000366493; ENSG00000196337.
ENST00000448456; ENSP00000403649; ENSG00000213030.
ENST00000596965; ENSP00000469076; ENSG00000196337.
ENST00000597853; ENSP00000470813; ENSG00000196337.

GeneID

1082.
93659.
94027.
94115.

KEGG

hsa:1082.
hsa:93659.
hsa:94027.
hsa:94115.

UCSC

uc002plv.2. human.

Organism-specific databases

CTD

1082.
93659.
94027.
94115.

GeneCards

GC19M049526.
GC19M049550.
GC19M049557.
GC19P049547.

HGNC

HGNC:1886. CGB.
HGNC:16452. CGB5.
HGNC:16451. CGB7.
HGNC:16453. CGB8.

HPA

CAB000042.
CAB010884.
HPA038925.
HPA038934.

MIM

118860. gene.
608825. gene.
608826. gene.
608827. gene.

neXtProt

NX_P01233.

PharmGKB

PA26439.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG284462.

HOVERGEN

HBG006698.

InParanoid

P01233.

KO

K10045.

OrthoDB

EOG4STS5W.

PhylomeDB

P01233.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P01233.

Bgee

P01233.

CleanEx

HS_CGB.
HS_CGB5.
HS_CGB7.

Genevestigator

P01233.

GermOnline

ENSG00000104827. Homo sapiens.
ENSG00000189052. Homo sapiens.

Family and domain databases

InterPro

IPR006208. Cys_knot.
IPR001545. Gonadotropin_bsu.
IPR018245. Gonadotropin_bsu_CS.
[Graphical view]

PANTHER

PTHR11515. PTHR11515. 1 hit.

Pfam

PF00007. Cys_knot. 1 hit.
[Graphical view]

SMART

SM00068. GHB. 1 hit.
[Graphical view]

PROSITE

PS00261. GLYCO_HORMONE_BETA_1. 1 hit.
PS00689. GLYCO_HORMONE_BETA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00097. Choriogonadotropin alfa.

EvolutionaryTrace

P01233.

NextBio

4508.

SOURCE

Search...

Entry information

Entry name

CGHB_HUMAN

Accession

Primary (citable) accession number: P01233
Secondary accession number(s): A1A5E0 , B9ZVP5, Q13991, Q14000, Q3KPI3, Q3SY41, Q8WTT5, Q8WXL1, Q8WXL2, Q8WXL3, Q8WXL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 159 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.