P01229 (LSHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lutropin subunit beta
Short name=Lutropin beta chain

Alternative name(s):
Luteinizing hormone subunit beta
Short name=LH-B
Short name=LSH-B
Short name=LSH-beta

Gene names

Name:

LHB

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	141 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	Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids.
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	Pituitary gland.
Involvement in disease	Hypogonadism LHB-related (HGON-LHB) [MIM:152780]: Characterized by infertility and pseudohermaphroditism. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8
Sequence similarities	Belongs to the glycoprotein hormones subunit beta family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Pseudohermaphroditism
Domain	Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell-cell signaling Traceable author statement PubMed 10484773. Source: ProtInc cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome male gonad development Traceable author statement PubMed 6785294. Source: ProtInc peptide hormone processing Traceable author statement. Source: Reactome progesterone biosynthetic process Traceable author statement PubMed 14557487. Source: BHF-UCL signal transduction Traceable author statement PubMed 10484773. Source: ProtInc
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	receptor binding Traceable author statement PubMed 10484773. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.2 Ref.3

Chain

21 – 141

121

Lutropin subunit beta

PRO_0000011726

Amino acid modifications

Glycosylation

50

1

N-linked (GlcNAc...)

CAR_000045

Disulfide bond

29 ↔ 77

By similarity

Disulfide bond

43 ↔ 92

By similarity

Disulfide bond

46 ↔ 130

By similarity

Disulfide bond

54 ↔ 108

By similarity

Disulfide bond

58 ↔ 110

By similarity

Disulfide bond

113 ↔ 120

By similarity

Natural variations

Natural variant

15

1

M → I.
Corresponds to variant rs34247911 [ dbSNP | Ensembl ].

VAR_034098

Natural variant

18

1

A → T More effective in stimulating IP3 but not cAMP production. Ref.11
Corresponds to variant rs5030775 [ dbSNP | Ensembl ].

VAR_015672

Natural variant

28

1

W → R. Ref.10
Corresponds to variant rs1800447 [ dbSNP | Ensembl ].

VAR_014589

Natural variant

35

1

I → T. Ref.10
Corresponds to variant rs34349826 [ dbSNP | Ensembl ].

VAR_014590

Natural variant

74

1

Q → R in HGON-LHB; lack of receptor-binding. Ref.8
Corresponds to variant rs5030773 [ dbSNP | Ensembl ].

VAR_003189

Natural variant

122

1

G → S May be implicated in female infertility. Ref.9
Corresponds to variant rs5030774 [ dbSNP | Ensembl ].

VAR_015673

Experimental info

Sequence conflict

39

1

E → Q AA sequence Ref.2

Sequence conflict

76

1

Missing AA sequence Ref.2

Sequence conflict

132 – 135

4

HPQL → PQH AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

141

Helix Strand Turn

Details...

Beta strand

21 – 23

3

Beta strand

28 – 38

11

Beta strand

47 – 55

9

Beta strand

75 – 88

14

Beta strand

99 – 112

14

Turn

115 – 117

3

Sequences

	Sequence		Length	Mass (Da)
	P01229 [UniParc]. Last modified November 1, 1995. Version 3. Checksum: E411766253113F7C	FASTA	141	15,345
	10 20 30 40 50 60 MEMLQGLLLL LLLSMGGAWA SREPLRPWCH PINAILAVEK EGCPVCITVN TTICAGYCPT 70 80 90 100 110 120 MMRVLQAVLP PLPQVVCTYR DVRFESIRLP GCPRGVDPVV SFPVALSCRC GPCRRSTSDC 130 140 GGPKDHPLTC DHPQLSGLLF L

References

[1]	"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].
[2]	"Human pituitary lutropin. Isolation, properties, and the complete amino acid sequence of the beta-subunit." Sairam M.R., Li C.H. Biochim. Biophys. Acta 412:70-81(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-141.
[3]	"The primary structure of the hormone-specific, beta subunit of human pituitary luteinizing hormone (hLH)." Shome B., Parlow A.F. J. Clin. Endocrinol. Metab. 36:618-621(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 21-141.
[4]	"Structure and significance of human luteinizing hormone-beta core fragment purified from human pituitary extracts." Birken S., Chen Y., Gawinowicz M.A., Agosto G.M., Canfield R.E., Hartree A.S. Endocrinology 133:985-989(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-40 AND 75-89. Tissue: Pituitary.
[5]	"Human luteinizing hormone. The amino acid sequence of the subunit." Closset J., Hennen G., Lequin R.M. FEBS Lett. 29:97-100(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE.
[6]	"NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin." Weisshaar G., Hiyama J., Renwick A.G.C., Nimtz M. Eur. J. Biochem. 195:257-268(1991) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE.
[7]	"Structure of a receptor-binding fragment from human luteinizing hormone beta-subunit determined by [1H]- and [15N]nuclear magnetic resonance spectroscopy." Keutmann H.T., Hua Q.-X., Weiss M.A. Mol. Endocrinol. 6:904-913(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 58-77.
[8]	"Hypogonadism caused by a single amino acid substitution in the beta subunit of luteinizing hormone." Weiss J., Axelrod L., Whitcomb R.W., Harris P.E., Crowley W.F. Jr., Jameson J.L. N. Engl. J. Med. 326:179-183(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HGON-LHB ARG-74.
[9]	"A new molecular variant of luteinizing hormone associated with female infertility." Liao W.X., Roy A.C., Chan C., Arulkumaran S., Ratnam S.S. Fertil. Steril. 69:102-106(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-122.
[10]	"Increased prevalence of luteinizing hormone beta-subunit variant in Japanese infertility patients." Takahashi K., Kurioka H., Ozaki T., Kanasaki H., Kohsaka M., Miyazaki K., Karino K. Hum. Reprod. 13:3338-3344(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-28 AND THR-35.
[11]	"A novel Ala(-3)Thr mutation in the signal peptide of human luteinizing hormone beta-subunit: potentiation of the inositol phosphate signalling pathway and attenuation of the adenylate cyclase pathway by recombinant variant hormone." Jiang M., Lamminen T., Pakarinen P., Hellman J., Manna P., Herrera R.J., Huhtaniemi I. Mol. Hum. Reprod. 8:201-212(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-18.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Luteinizing hormone entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00264 Genomic DNA. Translation: CAA25067.1.
S71273 Genomic DNA. Translation: AAD14960.1. Sequence problems.

IPI

IPI00000854.

PIR

UTHUB. I37994.

RefSeq

NP_000885.1. NM_000894.2.

UniGene

Hs.154704.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M92	model	-	A	1-141	[»]

ProteinModelPortal

P01229.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000221421.

PTM databases

GlycoSuiteDB

P01229.

Polymorphism databases

DMDM

1170834.

Proteomic databases

PaxDb

P01229.

PRIDE

P01229.

Protocols and materials databases

DNASU

3972.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221421; ENSP00000221421; ENSG00000104826.

GeneID

3972.

KEGG

hsa:3972.

UCSC

uc002plt.3. human.

Organism-specific databases

CTD

3972.

GeneCards

GC19M049519.

HGNC

HGNC:6584. LHB.

HPA

HPA038925.

MIM

152780. gene+phenotype.

neXtProt

NX_P01229.

Orphanet

755. Leydig cell hypoplasia.

PharmGKB

PA30356.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG44551.

HOGENOM

HOG000116098.

HOVERGEN

HBG006698.

InParanoid

P01229.

KO

K08521.

PhylomeDB

P01229.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P01229.

Bgee

P01229.

CleanEx

HS_LHB.

Genevestigator

P01229.

GermOnline

ENSG00000104826. 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

DB00044. Lutropin alfa.
DB00032. Menotropins.

GenomeRNAi

3972.

NextBio

15570.

SOURCE

Search...

Entry information

Entry name

LSHB_HUMAN

Accession

Primary (citable) accession number: P01229
Secondary accession number(s): Q9UDI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 138 of the entry and version 3 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.