Tyrosine 3-monooxygenase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P07101 (TY3H_HUMAN)

Last modified July 7, 2009. Version 116. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Tyrosine 3-monooxygenase
    EC=1.14.16.2
Alternative name(s):
    Tyrosine 3-hydroxylase
      Short name=TH

Gene names

Name:	TH
Synonyms:	TYH

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Plays an important role in the physiology of adrenergic neurons.
Catalytic activity	L-tyrosine + tetrahydrobiopterin + O₂ = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin.
Cofactor	Fe²⁺ ion.
Enzyme regulation	Phosphorylation leads to an increase in the catalytic activity.
Pathway	Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Tissue specificity	Mainly expressed in the brain and adrenal glands.
Involvement in disease	Defects in TH are the cause of dystonia DOPA-responsive autosomal recessive (ARDRD) [MIM:605407]; also known as autosomal recessive Segawa syndrome. ARDRD is a form of DOPA-responsive dystonia presenting in infancy or early childhood. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Some cases of ARDRD present with parkinsonian symptoms in infancy. Unlike all other forms of dystonia, it is an eminently treatable condition, due to a favorable response to L-DOPA.
Sequence similarities	Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

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Ontologies

Keywords
Biological process	Catecholamine biosynthesis Neurotransmitter biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dystonia Parkinsonism
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	dopamine biosynthetic process from tyrosine Non-traceable author statement. Source: UniProtKB embryonic camera-type eye morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB epinephrine biosynthetic process Inferred from direct assay. Source: UniProtKB eye photoreceptor cell development Inferred from sequence or structural similarity. Source: UniProtKB heart morphogenesis Non-traceable author statement. Source: UniProtKB learning Inferred from sequence or structural similarity. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB memory Inferred from sequence or structural similarity. Source: UniProtKB neurotransmitter biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW norepinephrine biosynthetic process Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pigmentation Traceable author statement. Source: UniProtKB regulation of heart contraction Inferred from sequence or structural similarity. Source: UniProtKB response to ethanol Inferred from direct assay. Source: UniProtKB response to hypoxia Inferred from direct assay. Source: UniProtKB synaptic transmission, dopaminergic Inferred from sequence or structural similarity. Source: UniProtKB visual perception Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	internal side of plasma membrane Inferred from direct assay. Source: UniProtKB melanosome membrane Inferred from direct assay. Source: UniProtKB neuron projection Inferred from direct assay. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB perikaryon Inferred from sequence or structural similarity. Source: UniProtKB smooth endoplasmic reticulum Inferred from direct assay. Source: UniProtKB
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB tyrosine 3-monooxygenase activity Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: P07101-1) 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 1 (identifier: P07101-2) The sequence of this isoform differs from the canonical sequence as follows: 31-34: Missing.

Isoform 2 (identifier: P07101-3) The sequence of this isoform differs from the canonical sequence as follows: 31-61: Missing.

Isoform 4 (identifier: P07101-4) The sequence of this isoform differs from the canonical sequence as follows: 1-33: Missing. 34-34: Q → M

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 528

527

Tyrosine 3-monooxygenase

PRO_0000205561

Regions

Compositional bias

85 – 90

Poly-Ala

Sites

Metal binding

361

Iron By similarity

Metal binding

366

Iron By similarity

Metal binding

406

Iron By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence

1 – 33

Missing in isoform 4.

VSP_000541

Alternative sequence

31 – 61

Missing in isoform 2.

VSP_000544

Alternative sequence

31 – 34

Missing in isoform 1.

VSP_000543

Alternative sequence

Q → M in isoform 4.

VSP_000542

Natural variant

112

V → M Common polymorphism. dbSNP rs6356. Ref.9 Ref.12 Ref.15

VAR_014025

Natural variant

233

R → H in ARDRD.

VAR_014026

Natural variant

236

L → P in ARDRD; severe parkinsonian symptoms in early infancy; strongly reduced stability and catalytic activity; rare mutation.

VAR_014027

Natural variant

276

T → P in ARDRD; parkinsonian symptoms in infancy. dbSNP rs28934581.

VAR_014028

Natural variant

314

T → M in ARDRD; parkinsonian symptoms in infancy.

VAR_014029

Natural variant

337

R → H in ARDRD; parkinsonian symptoms in infancy. dbSNP rs28934580.

VAR_014030

Natural variant

412

Q → K in ARDRD; reduced affinity for L-tyrosine.

VAR_014031

Natural variant

494

T → M in ARDRD; parkinsonian symptoms in infancy. dbSNP rs45471299.

VAR_014032

Natural variant

499

V → M: dbSNP rs1800033. Ref.13

VAR_014033

Experimental info

Sequence conflict

401

Y → S in AAA61179. Ref.1

Sequence conflict

401

Y → S in CAA28908. Ref.2

Sequence conflict

401

Y → S in CAA68472. Ref.3

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Sequences

Sequence		Length	Mass (Da)
Isoform 3 [UniParc]. Last modified June 16, 2009. Version 5. Checksum: 31D2D49955ACF070 Show »	FASTA	528	58,600
10 20 30 40 50 60 MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM VRGQGAPGPS LTGSPWPGTA APAASYTPTP 70 80 90 100 110 120 RSPRFIGRRQ SLIEDARKER EAAVAAAAAA VPSEPGDPLE AVAFEEKEGK AVLNLLFSPR 130 140 150 160 170 180 ATKPSALSRA VKVFETFEAK IHHLETRPAQ RPRAGGPHLE YFVRLEVRRG DLAALLSGVR 190 200 210 220 230 240 QVSEDVRSPA GPKVPWFPRK VSELDKCHHL VTKFDPDLDL DHPGFSDQVY RQRRKLIAEI 250 260 270 280 290 300 AFQYRHGDPI PRVEYTAEEI ATWKEVYTTL KGLYATHACG EHLEAFALLE RFSGYREDNI 310 320 330 340 350 360 PQLEDVSRFL KERTGFQLRP VAGLLSARDF LASLAFRVFQ CTQYIRHASS PMHSPEPDCC 370 380 390 400 410 420 HELLGHVPML ADRTFAQFSQ DIGLASLGAS DEEIEKLSTL YWFTVEFGLC KQNGEVKAYG 430 440 450 460 470 480 AGLLSSYGEL LHCLSEEPEI RAFDPEAAAV QPYQDQTYQS VYFVSESFSD AKDKLRSYAS 490 500 510 520 RIQRPFSVKF DPYTLAIDVL DSPQAVRRSL EGVQDELDTL AHALSAIG « Hide
Isoform 1. Checksum: 708422BBD3304A6C Show »	FASTA	524	58,160
10 20 30 40 50 60 MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM GAPGPSLTGS PWPGTAAPAA SYTPTPRSPR 70 80 90 100 110 120 FIGRRQSLIE DARKEREAAV AAAAAAVPSE PGDPLEAVAF EEKEGKAVLN LLFSPRATKP 130 140 150 160 170 180 SALSRAVKVF ETFEAKIHHL ETRPAQRPRA GGPHLEYFVR LEVRRGDLAA LLSGVRQVSE 190 200 210 220 230 240 DVRSPAGPKV PWFPRKVSEL DKCHHLVTKF DPDLDLDHPG FSDQVYRQRR KLIAEIAFQY 250 260 270 280 290 300 RHGDPIPRVE YTAEEIATWK EVYTTLKGLY ATHACGEHLE AFALLERFSG YREDNIPQLE 310 320 330 340 350 360 DVSRFLKERT GFQLRPVAGL LSARDFLASL AFRVFQCTQY IRHASSPMHS PEPDCCHELL 370 380 390 400 410 420 GHVPMLADRT FAQFSQDIGL ASLGASDEEI EKLSTLYWFT VEFGLCKQNG EVKAYGAGLL 430 440 450 460 470 480 SSYGELLHCL SEEPEIRAFD PEAAAVQPYQ DQTYQSVYFV SESFSDAKDK LRSYASRIQR 490 500 510 520 PFSVKFDPYT LAIDVLDSPQ AVRRSLEGVQ DELDTLAHAL SAIG « Hide
Isoform 2. Checksum: 6CB8EDC9C4874288 Show »	FASTA	497	55,612
10 20 30 40 50 60 MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE AAVAAAAAAV 70 80 90 100 110 120 PSEPGDPLEA VAFEEKEGKA VLNLLFSPRA TKPSALSRAV KVFETFEAKI HHLETRPAQR 130 140 150 160 170 180 PRAGGPHLEY FVRLEVRRGD LAALLSGVRQ VSEDVRSPAG PKVPWFPRKV SELDKCHHLV 190 200 210 220 230 240 TKFDPDLDLD HPGFSDQVYR QRRKLIAEIA FQYRHGDPIP RVEYTAEEIA TWKEVYTTLK 250 260 270 280 290 300 GLYATHACGE HLEAFALLER FSGYREDNIP QLEDVSRFLK ERTGFQLRPV AGLLSARDFL 310 320 330 340 350 360 ASLAFRVFQC TQYIRHASSP MHSPEPDCCH ELLGHVPMLA DRTFAQFSQD IGLASLGASD 370 380 390 400 410 420 EEIEKLSTLY WFTVEFGLCK QNGEVKAYGA GLLSSYGELL HCLSEEPEIR AFDPEAAAVQ 430 440 450 460 470 480 PYQDQTYQSV YFVSESFSDA KDKLRSYASR IQRPFSVKFD PYTLAIDVLD SPQAVRRSLE 490 GVQDELDTLA HALSAIG « Hide
Isoform 4. Checksum: 20B194A87A66BD3D Show »	FASTA	495	55,077
10 20 30 40 50 60 MGAPGPSLTG SPWPGTAAPA ASYTPTPRSP RFIGRRQSLI EDARKEREAA VAAAAAAVPS 70 80 90 100 110 120 EPGDPLEAVA FEEKEGKAVL NLLFSPRATK PSALSRAVKV FETFEAKIHH LETRPAQRPR 130 140 150 160 170 180 AGGPHLEYFV RLEVRRGDLA ALLSGVRQVS EDVRSPAGPK VPWFPRKVSE LDKCHHLVTK 190 200 210 220 230 240 FDPDLDLDHP GFSDQVYRQR RKLIAEIAFQ YRHGDPIPRV EYTAEEIATW KEVYTTLKGL 250 260 270 280 290 300 YATHACGEHL EAFALLERFS GYREDNIPQL EDVSRFLKER TGFQLRPVAG LLSARDFLAS 310 320 330 340 350 360 LAFRVFQCTQ YIRHASSPMH SPEPDCCHEL LGHVPMLADR TFAQFSQDIG LASLGASDEE 370 380 390 400 410 420 IEKLSTLYWF TVEFGLCKQN GEVKAYGAGL LSSYGELLHC LSEEPEIRAF DPEAAAVQPY 430 440 450 460 470 480 QDQTYQSVYF VSESFSDAKD KLRSYASRIQ RPFSVKFDPY TLAIDVLDSP QAVRRSLEGV 490 QDELDTLAHA LSAIG « Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a novel cDNA clone for human tyrosine hydroxylase: alternative RNA splicing produces four kinds of mRNA from a single gene." Kaneda N., Kobayashi K., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., Nagatsu T. Biochem. Biophys. Res. Commun. 146:971-975(1987) [PubMed: 2887169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]	"A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics." Grima B., Lamouroux A., Boni C., Julien J.-F., Javoy-Agid F., Mallet J. Nature 326:707-711(1987) [PubMed: 2882428] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]	"Isolation of a full-length cDNA clone encoding human tyrosine hydroxylase type 3." Kobayashi K., Kaneda N., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., Nagatsu T. Nucleic Acids Res. 15:6733-6733(1987) [PubMed: 2888085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Structure of the human tyrosine hydroxylase gene: alternative splicing from a single gene accounts for generation of four mRNA types." Kobayashi K., Kaneda N., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., Nagatsu T. J. Biochem. 103:907-912(1988) [PubMed: 2902075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Analysis of the 5' region of the human tyrosine hydroxylase gene: combinatorial patterns of exon splicing generate multiple regulated tyrosine hydroxylase isoforms." le Bourdelles B., Boularand S., Boni C., Horellou P., Dumas S., Grima B., Mallet J. J. Neurochem. 50:988-991(1988) [PubMed: 2892893] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Expression of human tyrosine hydroxylase cDNA in invertebrate cells using a baculovirus vector." Ginns E.I., Rehavi M., Martin B.M., Weller M., O'Malley K.L., Lamarca M.E., McAllister C.G., Paul S.M. J. Biol. Chem. 263:7406-7410(1988) [PubMed: 2896667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
[8]	"A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome." Luedecke B., Dworniczak B., Bartholome K. Hum. Genet. 95:123-125(1995) [PubMed: 7814018] [Abstract] Cited for: VARIANT ARDRD LYS-412.
[9]	"Frequent sequence variant in the human tyrosine hydroxylase gene." Luedecke B., Bartholome K. Hum. Genet. 95:716-716(1995) [PubMed: 7789962] [Abstract] Cited for: VARIANT MET-112.
[10]	"Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene." Knappskog P.M., Flatmark T., Mallet J., Luedecke B., Bartholome K. Hum. Mol. Genet. 4:1209-1212(1995) [PubMed: 8528210] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ARDRD LYS-412.
[11]	"Recessively inherited L-DOPA-responsive parkinsonism in infancy caused by a point mutation (L205P) in the tyrosine hydroxylase gene." Luedecke B., Knappskog P.M., Clayton P.T., Surtees R.A.H., Clelland J.D., Heales S.J.R., Brand M.P., Bartholome K., Flatmark T. Hum. Mol. Genet. 5:1023-1028(1996) [PubMed: 8817341] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ARDRD PRO-236.
[12]	"Association study of structural mutations of the tyrosine hydroxylase gene with schizophrenia and Parkinson's disease." Kunugi H., Kawada Y., Hattori M., Ueki A., Otsuka M., Nanko S. Am. J. Med. Genet. 81:131-133(1998) [PubMed: 9613851] [Abstract] Cited for: VARIANT ARDRD PRO-236, VARIANT MET-112.
[13]	"Systematic search for variations in the tyrosine hydroxylase gene and their associations with schizophrenia, affective disorders, and alcoholism." Ishiguro H., Arinami T., Saito T., Akazawa S., Enomoto M., Mitushio H., Fujishiro H., Tada K., Akimoto Y., Mifune H., Shiozuka S., Hamaguchi H., Toru M., Shibuya H. Am. J. Med. Genet. 81:388-396(1998) [PubMed: 9754624] [Abstract] Cited for: VARIANT MET-499.
[14]	"A common point mutation in the tyrosine hydroxylase gene in autosomal recessive L-DOPA-responsive dystonia in the Dutch population." van den Heuvel L.P.W.J., Luiten B., Smeitink J.A.M., de Rijk-van Andel J.F., Hyland K., Steenbergen-Spanjers G.C.H., Janssen R.J.T., Wevers R.A. Hum. Genet. 102:644-646(1998) [PubMed: 9703425] [Abstract] Cited for: VARIANT ARDRD HIS-233.
[15]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANT MET-112.
[16]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[17]	"Four novel mutations in the tyrosine hydroxylase gene in patients with infantile parkinsonism." Swaans R.J.M., Rondot P., Renier W.O., Van Den Heuvel L.P.W.J., Steenbergen-Spanjers G.C.H., Wevers R.A. Ann. Hum. Genet. 64:25-31(2000) [PubMed: 11246459] [Abstract] Cited for: VARIANTS ARDRD PRO-276; MET-314; HIS-337 AND MET-494.
+	Additional computationally mapped references.

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Web resources

GeneReviews

Wikipedia

Tyrosine hydroxylase entry

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Cross-references

Sequence databases
	M17589 mRNA. Translation: AAA61179.1. X05290 mRNA. Translation: CAA28908.1. Y00414 mRNA. Translation: CAA68472.1. AC132217 Genomic DNA. No translation available. M24791, M24787, M24789 Genomic DNA. Translation: AAA61173.1. M24791, M24787 Genomic DNA. Translation: AAA61170.1. M20911 mRNA. Translation: AAA61167.1.
IPI	IPI00010178. IPI00218275. IPI00218276. IPI00398179.
PIR	WHHUY4. A30002.
RefSeq	NP_000351.2.
UniGene	Hs.435609 Hs.523414
3D structure databases
HSSP	HSSP built from PDB template 1TOH based on UniProtKB P04177.
SMR	P07101. Positions 192-526, 193-527.
ModBase	Search...
PTM databases
PhosphoSite	P07101.
Proteomic databases
PRIDE	P07101.
Genome annotation databases
Ensembl	ENSG00000180176. Homo sapiens. [Contig view]
GeneID	7054.
KEGG	hsa:7054.
UCSC	uc001lvp.1. human. uc001lvq.1. human.
Organism-specific databases
GeneCards	GC11M002141.
H-InvDB	HIX0035928.
HGNC	HGNC:11782. TH.
HPA	CAB002522.
MIM	191290. gene. 605407. phenotype.
Orphanet	255. Dystonia, dopa-responsive. 101150. Dystonia, dopa-responsive, autosomal recessive.
PharmGKB	PA27004.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P07101.
HOVERGEN	P07101.
Enzyme and pathway databases
BRENDA	1.14.16.2. 247.
Pathway_Interaction_DB	alphasynuclein_pathway. Alpha-synuclein signaling. p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
Reactome	REACT_13685. Synaptic Transmission. REACT_15314. Hormone biosynthesis.
Gene expression databases
ArrayExpress	P07101.
Bgee	P07101.
CleanEx	HS_TH.
GermOnline	ENSG00000180176. Homo sapiens.
Family and domain databases
InterPro	IPR001273. ArAA_hydroxylase. IPR018301. ArAA_hydroxylase_Fe/CU_BS. IPR019774. Aromatic-AA_hydroxylase_C. IPR005962. Tyr_3_mOase. IPR019773. Tyrosine_3-monooxygenase-like. [Graphical view]
Gene3D	G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.
PANTHER	PTHR11473. Aaa_hydroxylase. 1 hit.
Pfam	PF00351. Biopterin_H. 1 hit. [Graphical view]
PIRSF	PIRSF000336. TH. 1 hit.
PRINTS	PR00372. FYWHYDRXLASE.
ProDom	PD002559. Aaa_hydroxylase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01269. Tyr_3_monoox. 1 hit.
PROSITE	PS00367. BIOPTERIN_HYDROXYL. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00120. L-Phenylalanine. DB00135. L-Tyrosine. DB00765. Metyrosine. DB00360. Tetrahydrobiopterin.
NextBio	27583.
SOURCE	Search...

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Entry information

Entry name

TY3H_HUMAN

Accession

Primary (citable) accession number: P07101
Secondary accession number(s): Q15585, Q15588, Q15589

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	June 16, 2009
Last modified:	July 7, 2009
This is version 116 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents