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Q8IWU9

- TPH2_HUMAN

UniProt

Q8IWU9 - TPH2_HUMAN

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Protein

Tryptophan 5-hydroxylase 2

Gene

TPH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.

Cofactori

Fe2+ ion.By similarity

Kineticsi

  1. KM=41.3 µM for L-tryptophan1 Publication

Vmax=833 nmol/min/mg enzyme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi318 – 3181IronBy similarity
Metal bindingi323 – 3231IronBy similarity
Metal bindingi363 – 3631IronBy similarity

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. tryptophan 5-monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. aromatic amino acid family metabolic process Source: InterPro
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. cellular response to lithium ion Source: Ensembl
  4. circadian rhythm Source: Ensembl
  5. indolalkylamine biosynthetic process Source: Reactome
  6. response to activity Source: Ensembl
  7. response to calcium ion Source: Ensembl
  8. response to estrogen Source: Ensembl
  9. response to glucocorticoid Source: Ensembl
  10. response to nutrient levels Source: Ensembl
  11. serotonin biosynthetic process Source: UniProtKB-UniPathway
  12. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Serotonin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06603-MONOMER.
ReactomeiREACT_15439. Serotonin and melatonin biosynthesis.
SABIO-RKQ8IWU9.
UniPathwayiUPA00846; UER00799.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan 5-hydroxylase 2 (EC:1.14.16.4)
Alternative name(s):
Neuronal tryptophan hydroxylase
Tryptophan 5-monooxygenase 2
Gene namesi
Name:TPH2
Synonyms:NTPH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:20692. TPH2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. neuron projection Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Major depressive disorder (MDD) [MIM:608516]: A common psychiatric disorder. It is a complex trait characterized by one or more major depressive episodes without a history of manic, mixed, or hypomanic episodes. A major depressive episode is characterized by at least 2 weeks during which there is a new onset or clear worsening of either depressed mood or loss of interest or pleasure in nearly all activities. Four additional symptoms must also be present including changes in appetite, weight, sleep, and psychomotor activity; decreased energy; feelings of worthlessness or guilt; difficulty thinking, concentrating, or making decisions; or recurrent thoughts of death or suicidal ideation, plans, or attempts. The episode must be accompanied by distress or impairment in social, occupational, or other important areas of functioning.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Attention deficit-hyperactivity disorder 7 (ADHD7) [MIM:613003]: A neurobehavioral developmental disorder primarily characterized by the coexistence of attentional problems and hyperactivity, with each behavior occurring infrequently alone.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Naturally occurring variants of TPH2 with impaired enzyme activity could cause deficiency of serotonin production and result in an increased risk of developing behavioral disorders.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031R → W in ADHD7; has severely reduced solubility and is completely inactive; loss of function may lead to a reduced serotonin synthesis which in turn makes the mutation carriers susceptible to ADHD and possibly other psychiatric disorders. 1 Publication
VAR_058942

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi608516. phenotype.
613003. phenotype.
PharmGKBiPA128747823.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Tryptophan 5-hydroxylase 2PRO_0000205574Add
BLAST

Proteomic databases

PaxDbiQ8IWU9.
PRIDEiQ8IWU9.

PTM databases

PhosphoSiteiQ8IWU9.

Expressioni

Tissue specificityi

Brain specific.

Gene expression databases

BgeeiQ8IWU9.
CleanExiHS_TPH2.
ExpressionAtlasiQ8IWU9. baseline.
GenevestigatoriQ8IWU9.

Organism-specific databases

HPAiHPA046274.

Interactioni

Protein-protein interaction databases

BioGridi125720. 1 interaction.
IntActiQ8IWU9. 1 interaction.
MINTiMINT-7997360.
STRINGi9606.ENSP00000329093.

Structurei

3D structure databases

ProteinModelPortaliQ8IWU9.
SMRiQ8IWU9. Positions 48-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 14076ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3186.
GeneTreeiENSGT00390000010268.
HOGENOMiHOG000233373.
HOVERGENiHBG006841.
InParanoidiQ8IWU9.
KOiK00502.
OMAiEDVSMFL.
OrthoDBiEOG7KM5T1.
PhylomeDBiQ8IWU9.
TreeFamiTF313327.

Family and domain databases

Gene3Di1.10.800.10. 1 hit.
InterProiIPR002912. ACT_dom.
IPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005963. Trp_5_mOase.
IPR019773. Tyrosine_3-monooxygenase-like.
[Graphical view]
PANTHERiPTHR11473. PTHR11473. 1 hit.
PfamiPF01842. ACT. 1 hit.
PF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFiPIRSF000336. TH. 1 hit.
PRINTSiPR00372. FYWHYDRXLASE.
SUPFAMiSSF56534. SSF56534. 1 hit.
TIGRFAMsiTIGR01270. Trp_5_monoox. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform a (identifier: Q8IWU9-1) [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

        10         20         30         40         50
MQPAMMMFSS KYWARRGFSL DSAVPEEHQL LGSSTLNKPN SGKNDDKGNK
60 70 80 90 100
GSSKREAATE SGKTAVVFSL KNEVGGLVKA LRLFQEKRVN MVHIESRKSR
110 120 130 140 150
RRSSEVEIFV DCECGKTEFN ELIQLLKFQT TIVTLNPPEN IWTEEEELED
160 170 180 190 200
VPWFPRKISE LDKCSHRVLM YGSELDADHP GFKDNVYRQR RKYFVDVAMG
210 220 230 240 250
YKYGQPIPRV EYTEEETKTW GVVFRELSKL YPTHACREYL KNFPLLTKYC
260 270 280 290 300
GYREDNVPQL EDVSMFLKER SGFTVRPVAG YLSPRDFLAG LAYRVFHCTQ
310 320 330 340 350
YIRHGSDPLY TPEPDTCHEL LGHVPLLADP KFAQFSQEIG LASLGASDED
360 370 380 390 400
VQKLATCYFF TIEFGLCKQE GQLRAYGAGL LSSIGELKHA LSDKACVKAF
410 420 430 440 450
DPKTTCLQEC LITTFQEAYF VSESFEEAKE KMRDFAKSIT RPFSVYFNPY
460 470 480 490
TQSIEILKDT RSIENVVQDL RSDLNTVCDA LNKMNQYLGI
Length:490
Mass (Da):56,057
Last modified:March 1, 2003 - v1
Checksum:i753645E6E0CE430B
GO
Isoform b (identifier: Q8IWU9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-147: E → GKE

Show »
Length:492
Mass (Da):56,242
Checksum:i5B90CB629F9F6DD6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → N in AAI14500. (PubMed:15489334)Curated

RNA editingi

Modulates the kinetic properties of both isoforms.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361L → P The property of the variant is indistinguishable from the wild-type.
VAR_058938
Natural varianti36 – 361L → V The property of the variant is indistinguishable from the wild-type.
Corresponds to variant rs34115267 [ dbSNP | Ensembl ].
VAR_058939
Natural varianti41 – 411S → Y The property of the variant is indistinguishable from the wild-type.
Corresponds to variant rs78162420 [ dbSNP | Ensembl ].
VAR_058940
Natural varianti55 – 551R → C The property of the variant is indistinguishable from the wild-type.
Corresponds to variant rs75558144 [ dbSNP | Ensembl ].
VAR_058941
Natural varianti206 – 2061P → S May be associated with susceptibility to bipolar affective disorder; decreases solubility; decreases thermal stability; catalytic activity as the wild type; moderate loss-of-function observed manifested via stability and solubility effect. 1 Publication
Corresponds to variant rs17110563 [ dbSNP | Ensembl ].
VAR_046136
Natural varianti303 – 3031R → W in ADHD7; has severely reduced solubility and is completely inactive; loss of function may lead to a reduced serotonin synthesis which in turn makes the mutation carriers susceptible to ADHD and possibly other psychiatric disorders. 1 Publication
VAR_058942
Natural varianti328 – 3281A → V Moderate loss-of-function observed manifested via stability and solubility effect.
Corresponds to variant rs2887147 [ dbSNP | Ensembl ].
VAR_058943
Natural varianti433 – 4331R → G in RNA edited version.
VAR_065019
Natural varianti441 – 4411R → H May be due to a rare RNA editing event; functional polymorphism linked with susceptibility to major depressive disorder; 80% loss of function; decreases solubility; decreases thermal stability; reduces catalytic activity. 1 Publication
VAR_026749
Natural varianti468 – 4681Q → R in RNA edited version.
VAR_065020
Natural varianti479 – 4791D → E Moderate loss-of-function observed manifested via stability and solubility effect.
Corresponds to variant rs7488262 [ dbSNP | Ensembl ].
VAR_058944

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei147 – 1471E → GKE in isoform b. CuratedVSP_040971

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY098914 mRNA. Translation: AAM28946.1.
AC090109 Genomic DNA. No translation available.
BC114499 mRNA. Translation: AAI14500.1.
CCDSiCCDS31859.1. [Q8IWU9-1]
RefSeqiNP_775489.2. NM_173353.3. [Q8IWU9-1]
UniGeneiHs.736576.

Genome annotation databases

EnsembliENST00000333850; ENSP00000329093; ENSG00000139287. [Q8IWU9-1]
GeneIDi121278.
KEGGihsa:121278.
UCSCiuc001swy.2. human. [Q8IWU9-1]

Polymorphism databases

DMDMi30580625.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY098914 mRNA. Translation: AAM28946.1 .
AC090109 Genomic DNA. No translation available.
BC114499 mRNA. Translation: AAI14500.1 .
CCDSi CCDS31859.1. [Q8IWU9-1 ]
RefSeqi NP_775489.2. NM_173353.3. [Q8IWU9-1 ]
UniGenei Hs.736576.

3D structure databases

ProteinModelPortali Q8IWU9.
SMRi Q8IWU9. Positions 48-484.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125720. 1 interaction.
IntActi Q8IWU9. 1 interaction.
MINTi MINT-7997360.
STRINGi 9606.ENSP00000329093.

Chemistry

BindingDBi Q8IWU9.
ChEMBLi CHEMBL5433.
DrugBanki DB00150. L-Tryptophan.
GuidetoPHARMACOLOGYi 1242.

PTM databases

PhosphoSitei Q8IWU9.

Polymorphism databases

DMDMi 30580625.

Proteomic databases

PaxDbi Q8IWU9.
PRIDEi Q8IWU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333850 ; ENSP00000329093 ; ENSG00000139287 . [Q8IWU9-1 ]
GeneIDi 121278.
KEGGi hsa:121278.
UCSCi uc001swy.2. human. [Q8IWU9-1 ]

Organism-specific databases

CTDi 121278.
GeneCardsi GC12P072332.
HGNCi HGNC:20692. TPH2.
HPAi HPA046274.
MIMi 607478. gene.
608516. phenotype.
613003. phenotype.
neXtProti NX_Q8IWU9.
PharmGKBi PA128747823.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3186.
GeneTreei ENSGT00390000010268.
HOGENOMi HOG000233373.
HOVERGENi HBG006841.
InParanoidi Q8IWU9.
KOi K00502.
OMAi EDVSMFL.
OrthoDBi EOG7KM5T1.
PhylomeDBi Q8IWU9.
TreeFami TF313327.

Enzyme and pathway databases

UniPathwayi UPA00846 ; UER00799 .
BioCyci MetaCyc:HS06603-MONOMER.
Reactomei REACT_15439. Serotonin and melatonin biosynthesis.
SABIO-RK Q8IWU9.

Miscellaneous databases

GeneWikii TPH2.
GenomeRNAii 121278.
NextBioi 80710.
PROi Q8IWU9.
SOURCEi Search...

Gene expression databases

Bgeei Q8IWU9.
CleanExi HS_TPH2.
ExpressionAtlasi Q8IWU9. baseline.
Genevestigatori Q8IWU9.

Family and domain databases

Gene3Di 1.10.800.10. 1 hit.
InterProi IPR002912. ACT_dom.
IPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005963. Trp_5_mOase.
IPR019773. Tyrosine_3-monooxygenase-like.
[Graphical view ]
PANTHERi PTHR11473. PTHR11473. 1 hit.
Pfami PF01842. ACT. 1 hit.
PF00351. Biopterin_H. 1 hit.
[Graphical view ]
PIRSFi PIRSF000336. TH. 1 hit.
PRINTSi PR00372. FYWHYDRXLASE.
SUPFAMi SSF56534. SSF56534. 1 hit.
TIGRFAMsi TIGR01270. Trp_5_monoox. 1 hit.
PROSITEi PS51671. ACT. 1 hit.
PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Synthesis of serotonin by a second tryptophan hydroxylase isoform."
    Walther D.J., Peter J.-U., Bashammakh S., Hortnagl H., Voits M., Fink H., Bader M.
    Science 299:76-76(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 A).
  4. "Brain-specific tryptophan hydroxylase 2 (TPH2): a functional Pro206Ser substitution and variation in the 5'-region are associated with bipolar affective disorder."
    Cichon S., Winge I., Mattheisen M., Georgi A., Karpushova A., Freudenberg J., Freudenberg-Hua Y., Babadjanova G., Van Den Bogaert A., Abramova L.I., Kapiletti S., Knappskog P.M., McKinney J., Maier W., Jamra R.A., Schulze T.G., Schumacher J., Propping P.
    , Rietschel M., Haavik J., Noethen M.M.
    Hum. Mol. Genet. 17:87-97(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, VARIANT SER-206, CHARACTERIZATION OF VARIANTS SER-206 AND HIS-441.
  5. Cited for: ALTERNATIVE SPLICING (ISOFORMS A AND B), RNA EDITING OF POSITIONS 433; 441 AND 468.
    Tissue: Brain.
  6. "Loss-of-function mutation in tryptophan hydroxylase-2 identified in unipolar major depression."
    Zhang X., Gainetdinov R.R., Beaulieu J.-M., Sotnikova T.D., Burch L.H., Williams R.B., Schwartz D.A., Krishnan K.R.R., Caron M.G.
    Neuron 45:11-16(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-441, CHARACTERIZATION OF VARIANT HIS-441.
  7. "A loss-of-function mutation in tryptophan hydroxylase 2 segregating with attention-deficit/hyperactivity disorder."
    McKinney J., Johansson S., Halmoy A., Dramsdahl M., Winge I., Knappskog P.M., Haavik J.
    Mol. Psychiatry 13:365-367(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ADHD7 TRP-303.
  8. "Functional properties of missense variants of human tryptophan hydroxylase 2."
    McKinney J.A., Turel B., Winge I., Knappskog P.M., Haavik J.
    Hum. Mutat. 30:787-794(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS VAL-36; PRO-36; TYR-41; CYS-55; SER-206; TRP-303; VAL-328; HIS-441 AND GLU-479.

Entry informationi

Entry nameiTPH2_HUMAN
AccessioniPrimary (citable) accession number: Q8IWU9
Secondary accession number(s): A6NGA4, Q14CB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 115 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3