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P01233

- CGHB_HUMAN

UniProt

P01233 - CGHB_HUMAN

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Protein

Choriogonadotropin subunit beta

Gene
CGB, CGB3
CGB5
CGB7
CGB8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.

GO - Molecular functioni

  1. hormone activity Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. cell-cell signaling Source: ProtInc
  3. cellular protein metabolic process Source: Reactome
  4. female gamete generation Source: ProtInc
  5. peptide hormone processing Source: Reactome
  6. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_15398. Glycoprotein hormones.

Names & Taxonomyi

Organism-specific databases

Protein namesi
Recommended name:
Choriogonadotropin subunit beta
Short name:
CG-beta
Alternative name(s):
Chorionic gonadotrophin chain beta
Gene namesi
Name:CGB
Synonyms:CGB3
AND
Name:CGB5
AND
Name:CGB7
AND
Name:CGB8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19
HGNCiHGNC:1886. CGB.
HGNC:16452. CGB5.
HGNC:16451. CGB7.
HGNC:16453. CGB8.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

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.

Organism-specific databases

PharmGKBiPA26439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20203 PublicationsAdd
BLAST
Chaini21 – 165145Choriogonadotropin subunit betaPRO_0000011676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 773 Publications
Glycosylationi33 – 331N-linked (GlcNAc...)CAR_000042
Disulfide bondi43 ↔ 923 Publications
Disulfide bondi46 ↔ 1303 Publications
Glycosylationi50 – 501N-linked (GlcNAc...)CAR_000043
Disulfide bondi54 ↔ 1083 Publications
Disulfide bondi58 ↔ 1103 Publications
Disulfide bondi113 ↔ 1203 Publications
Glycosylationi141 – 1411O-linked (GalNAc...)1 Publication
Glycosylationi147 – 1471O-linked (GalNAc...)1 Publication
Glycosylationi152 – 1521O-linked (GalNAc...)1 Publication
Glycosylationi158 – 1581O-linked (GalNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01233.
PaxDbiP01233.
PeptideAtlasiP01233.
PRIDEiP01233.

PTM databases

PhosphoSiteiP01233.
UniCarbKBiP01233.

Expressioni

Tissue specificityi

Placenta.

Developmental stagei

Made by the first trimester placenta.

Gene expression databases

BgeeiP01233.
CleanExiHS_CGB.
HS_CGB5.
HS_CGB7.
GenevestigatoriP01233.

Organism-specific databases

HPAiCAB000042.
CAB010884.
HPA038925.
HPA038934.

Interactioni

Subunit structurei

Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin.

Protein-protein interaction databases

BioGridi107508. 2 interactions.
DIPiDIP-6183N.
MINTiMINT-1510897.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 3814
Beta strandi47 – 6014
Beta strandi75 – 8814
Beta strandi99 – 11214
Turni115 – 1173
Beta strandi118 – 1214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HCNX-ray2.60B21-165[»]
1HRPX-ray3.00B21-165[»]
1QFWX-ray3.50B21-165[»]
1XULmodel-B21-165[»]
DisProtiDP00013.
ProteinModelPortaliP01233.
SMRiP01233. Positions 22-131.

Miscellaneous databases

EvolutionaryTraceiP01233.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG284462.
HOVERGENiHBG006698.
InParanoidiP01233.
KOiK10045.
OMAiTVNATIC.
OrthoDBiEOG7JQBQF.
PhylomeDBiP01233.
TreeFamiTF332940.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR006208. Glyco_hormone_CN.
IPR001545. Gonadotropin_bsu.
IPR018245. Gonadotropin_bsu_CS.
[Graphical view]
PANTHERiPTHR11515. PTHR11515. 1 hit.
PfamiPF00007. Cys_knot. 1 hit.
[Graphical view]
SMARTiSM00068. GHB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00261. GLYCO_HORMONE_BETA_1. 1 hit.
PS00689. GLYCO_HORMONE_BETA_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P01233-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEMFQGLLLL LLLSMGGTWA SKEPLRPRCR PINATLAVEK EGCPVCITVN    50
TTICAGYCPT MTRVLQGVLP ALPQVVCNYR DVRFESIRLP GCPRGVNPVV 100
SYAVALSCQC ALCRRSTTDC GGPKDHPLTC DDPRFQDSSS SKAPPPSLPS 150
PSRLPGPSDT PILPQ 165
Length:165
Mass (Da):17,739
Last modified:July 21, 1986 - v1
Checksum:i5598FB9E51A05748
GO
Isoform 2 (identifier: P01233-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:181
Mass (Da):19,053
Checksum:i853B736271867359
GO

Sequence cautioni

The sequence CAA25068.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA25069.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41F → L.1 Publication
Corresponds to variant rs6516 [ dbSNP | Ensembl ].
VAR_014585
Natural varianti18 – 181T → A.1 Publication
VAR_015231
Natural varianti22 – 221K → R.1 Publication
Corresponds to variant rs6518 [ dbSNP | Ensembl ].
VAR_014586
Natural varianti24 – 241P → M Requires 2 nucleotide substitutions. 2 Publications
VAR_015232
Natural varianti28 – 281R → W.1 Publication
VAR_015233
Natural varianti30 – 301R → H.1 Publication
VAR_015234
Natural varianti35 – 351T → I.1 Publication
Corresponds to variant rs6515 [ dbSNP | Ensembl ].
VAR_014587
Natural varianti97 – 971N → D.
Corresponds to variant rs6519 [ dbSNP | Ensembl ].
VAR_014588
Natural varianti137 – 1371D → A in gene 6. 4 Publications
Corresponds to variant rs7452 [ dbSNP | Ensembl ].
VAR_003188
Natural varianti147 – 1471S → C.1 Publication
VAR_015235

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44MEMF → MGRPGLGAAVSDPGEAVSLS in isoform 2. VSP_038396

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231P → T in AAL69709. 1 Publication
Isoform 2 (identifier: P01233-2)
Sequence conflicti7 – 71G → R in CAA25069. 1 Publication
Sequence conflicti9 – 91A → V in CAA25069. 1 Publication
Sequence conflicti12 – 121D → G in CAA25069. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12749.1. [P01233-1]
PIRiA93230. KTHUB.
I37231.
RefSeqiNP_000728.1. NM_000737.3. [P01233-1]
NP_149032.1. NM_033043.1. [P01233-1]
NP_149133.1. NM_033142.1.
NP_149439.1. NM_033183.2. [P01233-1]
XP_005258480.1. XM_005258423.1. [P01233-2]
XP_005259480.1. XM_005259423.1. [P01233-2]
XP_005259483.1. XM_005259426.1.
XP_006723568.1. XM_006723505.1.
UniGeneiHs.172944.
Hs.446683.
Hs.659014.
Hs.681647.
Hs.743279.
Hs.745468.

Genome annotation databases

EnsembliENST00000301408; ENSP00000301408; ENSG00000189052. [P01233-1]
ENST00000357383; ENSP00000349954; ENSG00000104827. [P01233-1]
ENST00000377280; ENSP00000366493; ENSG00000196337.
ENST00000448456; ENSP00000403649; ENSG00000213030. [P01233-1]
ENST00000596965; ENSP00000469076; ENSG00000196337.
ENST00000597853; ENSP00000470813; ENSG00000196337.
GeneIDi1082.
93659.
94027.
94115.
KEGGihsa:1082.
hsa:93659.
hsa:94027.
hsa:94115.
UCSCiuc002plv.2. human. [P01233-1]

Polymorphism databases

DMDMi116184.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Chorionic gonadotropin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12749.1. [P01233-1 ]
PIRi A93230. KTHUB.
I37231.
RefSeqi NP_000728.1. NM_000737.3. [P01233-1 ]
NP_149032.1. NM_033043.1. [P01233-1 ]
NP_149133.1. NM_033142.1.
NP_149439.1. NM_033183.2. [P01233-1 ]
XP_005258480.1. XM_005258423.1. [P01233-2 ]
XP_005259480.1. XM_005259423.1. [P01233-2 ]
XP_005259483.1. XM_005259426.1.
XP_006723568.1. XM_006723505.1.
UniGenei Hs.172944.
Hs.446683.
Hs.659014.
Hs.681647.
Hs.743279.
Hs.745468.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
DisProti DP00013.
ProteinModelPortali P01233.
SMRi P01233. Positions 22-131.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107508. 2 interactions.
DIPi DIP-6183N.
MINTi MINT-1510897.

Chemistry

DrugBanki DB00097. Choriogonadotropin alfa.

PTM databases

PhosphoSitei P01233.
UniCarbKBi P01233.

Polymorphism databases

DMDMi 116184.

Proteomic databases

MaxQBi P01233.
PaxDbi P01233.
PeptideAtlasi P01233.
PRIDEi P01233.

Protocols and materials databases

DNASUi 1082.
93659.
94027.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301408 ; ENSP00000301408 ; ENSG00000189052 . [P01233-1 ]
ENST00000357383 ; ENSP00000349954 ; ENSG00000104827 . [P01233-1 ]
ENST00000377280 ; ENSP00000366493 ; ENSG00000196337 .
ENST00000448456 ; ENSP00000403649 ; ENSG00000213030 . [P01233-1 ]
ENST00000596965 ; ENSP00000469076 ; ENSG00000196337 .
ENST00000597853 ; ENSP00000470813 ; ENSG00000196337 .
GeneIDi 1082.
93659.
94027.
94115.
KEGGi hsa:1082.
hsa:93659.
hsa:94027.
hsa:94115.
UCSCi uc002plv.2. human. [P01233-1 ]

Organism-specific databases

CTDi 1082.
93659.
94027.
94115.
GeneCardsi GC19M049526.
GC19M049550.
GC19M049557.
GC19P049547.
HGNCi HGNC:1886. CGB.
HGNC:16452. CGB5.
HGNC:16451. CGB7.
HGNC:16453. CGB8.
HPAi CAB000042.
CAB010884.
HPA038925.
HPA038934.
MIMi 118860. gene.
608825. gene.
608826. gene.
608827. gene.
neXtProti NX_P01233.
PharmGKBi PA26439.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG284462.
HOVERGENi HBG006698.
InParanoidi P01233.
KOi K10045.
OMAi TVNATIC.
OrthoDBi EOG7JQBQF.
PhylomeDBi P01233.
TreeFami TF332940.

Enzyme and pathway databases

Reactomei REACT_15398. Glycoprotein hormones.

Miscellaneous databases

EvolutionaryTracei P01233.
GeneWikii CGB7.
Chorionic_gonadotropin_beta.
NextBioi 4508.
PROi P01233.
SOURCEi Search...

Gene expression databases

Bgeei P01233.
CleanExi HS_CGB.
HS_CGB5.
HS_CGB7.
Genevestigatori P01233.

Family and domain databases

Gene3Di 2.10.90.10. 1 hit.
InterProi IPR029034. Cystine-knot_cytokine.
IPR006208. Glyco_hormone_CN.
IPR001545. Gonadotropin_bsu.
IPR018245. Gonadotropin_bsu_CS.
[Graphical view ]
PANTHERi PTHR11515. PTHR11515. 1 hit.
Pfami PF00007. Cys_knot. 1 hit.
[Graphical view ]
SMARTi SM00068. GHB. 1 hit.
[Graphical view ]
SUPFAMi SSF57501. SSF57501. 1 hit.
PROSITEi PS00261. GLYCO_HORMONE_BETA_1. 1 hit.
PS00689. GLYCO_HORMONE_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiCGHB_HUMAN
AccessioniPrimary (citable) accession number: P01233
Secondary accession number(s): A1A5E0
, B9ZVP5, Q13991, Q14000, Q3KPI3, Q3SY41, Q8WTT5, Q8WXL1, Q8WXL2, Q8WXL3, Q8WXL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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