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Q16775

- GLO2_HUMAN

UniProt

Q16775 - GLO2_HUMAN

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Protein

Hydroxyacylglutathione hydrolase, mitochondrial

Gene

HAGH

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

Functioni

Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.

Catalytic activityi

S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate.

Cofactori

Binds 2 zinc ions per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021Zinc 1
Metal bindingi104 – 1041Zinc 1
Metal bindingi106 – 1061Zinc 2
Metal bindingi107 – 1071Zinc 2
Metal bindingi158 – 1581Zinc 1
Metal bindingi182 – 1821Zinc 1
Metal bindingi182 – 1821Zinc 2
Metal bindingi221 – 2211Zinc 2

GO - Molecular functioni

  1. hydroxyacylglutathione hydrolase activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. glutathione biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.2.6. 5596.
SABIO-RKQ16775.
UniPathwayiUPA00619; UER00676.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacylglutathione hydrolase, mitochondrial (EC:3.1.2.6)
Alternative name(s):
Glyoxalase II
Short name:
Glx II
Gene namesi
Name:HAGH
Synonyms:GLO2, HAGH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:4805. HAGH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial matrix Source: UniProtKB
  4. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Organism-specific databases

MIMi138760. gene+phenotype.
PharmGKBiPA29179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1313MitochondrionSequence AnalysisAdd
BLAST
Chaini14 – 308295Hydroxyacylglutathione hydrolase, mitochondrialPRO_0000192342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei229 – 2291N6-acetyllysine; alternate1 Publication
Modified residuei229 – 2291N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16775.
PaxDbiQ16775.
PRIDEiQ16775.

PTM databases

PhosphoSiteiQ16775.

Expressioni

Tissue specificityi

Expressed in liver and kidney.1 Publication

Gene expression databases

BgeeiQ16775.
CleanExiHS_HAGH.
ExpressionAtlasiQ16775. baseline and differential.
GenevestigatoriQ16775.

Organism-specific databases

HPAiCAB033531.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi109279. 6 interactions.
IntActiQ16775. 1 interaction.
STRINGi9606.ENSP00000380514.

Structurei

Secondary structure

1
308
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 567
Turni57 – 593
Beta strandi60 – 678
Turni68 – 714
Beta strandi72 – 776
Helixi81 – 9111
Beta strandi94 – 996
Helixi105 – 1084
Helixi111 – 1177
Beta strandi122 – 1265
Beta strandi134 – 1363
Beta strandi142 – 1454
Beta strandi148 – 1547
Beta strandi157 – 1593
Beta strandi163 – 1686
Beta strandi170 – 1745
Beta strandi177 – 1815
Helixi197 – 2059
Turni206 – 2105
Beta strandi216 – 2216
Helixi224 – 23411
Helixi239 – 25416
Helixi263 – 2697
Turni271 – 2766
Helixi278 – 2847
Helixi289 – 30214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QH3X-ray1.90A/B49-308[»]
1QH5X-ray1.45A/B49-308[»]
2F50model-A64-225[»]
ProteinModelPortaliQ16775.
SMRiQ16775. Positions 49-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16775.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1933Substrate binding
Regioni221 – 2233Substrate binding
Regioni297 – 3004Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0491.
GeneTreeiENSGT00530000063033.
HOGENOMiHOG000058041.
HOVERGENiHBG001152.
InParanoidiQ16775.
KOiK01069.
OMAiSTPCHTT.
PhylomeDBiQ16775.
TreeFamiTF105273.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01374. Glyoxalase_2.
InterProiIPR001279. Beta-lactamas-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFiPIRSF005457. Glx. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform 1 (identifier: Q16775-1) [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
MVVGRGLLGR RSLAALGAAC ARRGLGPALL GVFCHTDLRK NLTVDEGTMK
60 70 80 90 100
VEVLPALTDN YMYLVIDDET KEAAIVDPVQ PQKVVDAARK HGVKLTTVLT
110 120 130 140 150
THHHWDHAGG NEKLVKLESG LKVYGGDDRI GALTHKITHL STLQVGSLNV
160 170 180 190 200
KCLATPCHTS GHICYFVSKP GGSEPPAVFT GDTLFVAGCG KFYEGTADEM
210 220 230 240 250
CKALLEVLGR LPPDTRVYCG HEYTINNLKF ARHVEPGNAA IREKLAWAKE
260 270 280 290 300
KYSIGEPTVP STLAEEFTYN PFMRVREKTV QQHAGETDPV TTMRAVRREK

DQFKMPRD
Length:308
Mass (Da):33,806
Last modified:September 1, 2009 - v2
Checksum:i64E5C214B6EC61CB
GO
Isoform 2 (identifier: Q16775-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: Produced by alternative splicing. Also produced by alternative initiation at Met-49 of isoform 1.

Show »
Length:260
Mass (Da):28,860
Checksum:i4C3DEC87FB27A1D2
GO
Isoform 3 (identifier: Q16775-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     146-236: GSLNVKCLAT...NLKFARHVEP → TPCLWLAAGS...WQRSLPTTPS
     237-308: Missing.

Note: No experimental confirmation available.

Show »
Length:236
Mass (Da):25,455
Checksum:i25A00E2EAD5E9A15
GO

Sequence cautioni

The sequence AAH00840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA62483.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671D → G in BAG60445. (PubMed:14702039)Curated
Sequence conflicti121 – 1211L → P in BAG61219. (PubMed:14702039)Curated
Sequence conflicti202 – 2021K → E in BAF82844. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848Missing in isoform 2. 1 PublicationVSP_037929Add
BLAST
Alternative sequencei146 – 23691GSLNV…RHVEP → TPCLWLAAGSSMKGLRMRCV KLCWRSWAGSPRTQESTVAT STPSTTSSLHATWSPAMPPS GRSWPGPRRSTASGSPQCHP PWQRSLPTTPS in isoform 3. 1 PublicationVSP_055199Add
BLAST
Alternative sequencei237 – 30872Missing in isoform 3. 1 PublicationVSP_055200Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK290155 mRNA. Translation: BAF82844.1.
AK298174 mRNA. Translation: BAG60445.1.
AK299173 mRNA. Translation: BAG61219.1.
AE006639 Genomic DNA. Translation: AAK61294.1.
AC012180 Genomic DNA. No translation available.
BC000840 mRNA. Translation: AAH00840.1. Different initiation.
BC002627 mRNA. Translation: AAH02627.2.
X90999 mRNA. Translation: CAA62483.1. Different initiation.
CCDSiCCDS10447.2. [Q16775-1]
CCDS32366.1. [Q16775-2]
CCDS66900.1. [Q16775-3]
RefSeqiNP_001035517.1. NM_001040427.1. [Q16775-2]
NP_001273178.1. NM_001286249.1. [Q16775-3]
NP_005317.2. NM_005326.4. [Q16775-1]
UniGeneiHs.157394.

Genome annotation databases

EnsembliENST00000397353; ENSP00000380511; ENSG00000063854. [Q16775-2]
ENST00000397356; ENSP00000380514; ENSG00000063854. [Q16775-1]
ENST00000455446; ENSP00000406552; ENSG00000063854. [Q16775-3]
GeneIDi3029.
KEGGihsa:3029.
UCSCiuc002cmz.3. human. [Q16775-1]

Polymorphism databases

DMDMi257051015.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK290155 mRNA. Translation: BAF82844.1 .
AK298174 mRNA. Translation: BAG60445.1 .
AK299173 mRNA. Translation: BAG61219.1 .
AE006639 Genomic DNA. Translation: AAK61294.1 .
AC012180 Genomic DNA. No translation available.
BC000840 mRNA. Translation: AAH00840.1 . Different initiation.
BC002627 mRNA. Translation: AAH02627.2 .
X90999 mRNA. Translation: CAA62483.1 . Different initiation.
CCDSi CCDS10447.2. [Q16775-1 ]
CCDS32366.1. [Q16775-2 ]
CCDS66900.1. [Q16775-3 ]
RefSeqi NP_001035517.1. NM_001040427.1. [Q16775-2 ]
NP_001273178.1. NM_001286249.1. [Q16775-3 ]
NP_005317.2. NM_005326.4. [Q16775-1 ]
UniGenei Hs.157394.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QH3 X-ray 1.90 A/B 49-308 [» ]
1QH5 X-ray 1.45 A/B 49-308 [» ]
2F50 model - A 64-225 [» ]
ProteinModelPortali Q16775.
SMRi Q16775. Positions 49-308.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109279. 6 interactions.
IntActi Q16775. 1 interaction.
STRINGi 9606.ENSP00000380514.

Chemistry

BindingDBi Q16775.
ChEMBLi CHEMBL2261.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei Q16775.

Polymorphism databases

DMDMi 257051015.

Proteomic databases

MaxQBi Q16775.
PaxDbi Q16775.
PRIDEi Q16775.

Protocols and materials databases

DNASUi 3029.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000397353 ; ENSP00000380511 ; ENSG00000063854 . [Q16775-2 ]
ENST00000397356 ; ENSP00000380514 ; ENSG00000063854 . [Q16775-1 ]
ENST00000455446 ; ENSP00000406552 ; ENSG00000063854 . [Q16775-3 ]
GeneIDi 3029.
KEGGi hsa:3029.
UCSCi uc002cmz.3. human. [Q16775-1 ]

Organism-specific databases

CTDi 3029.
GeneCardsi GC16M001845.
HGNCi HGNC:4805. HAGH.
HPAi CAB033531.
MIMi 138760. gene+phenotype.
neXtProti NX_Q16775.
PharmGKBi PA29179.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0491.
GeneTreei ENSGT00530000063033.
HOGENOMi HOG000058041.
HOVERGENi HBG001152.
InParanoidi Q16775.
KOi K01069.
OMAi STPCHTT.
PhylomeDBi Q16775.
TreeFami TF105273.

Enzyme and pathway databases

UniPathwayi UPA00619 ; UER00676 .
BRENDAi 3.1.2.6. 5596.
SABIO-RK Q16775.

Miscellaneous databases

EvolutionaryTracei Q16775.
GeneWikii HAGH.
GenomeRNAii 3029.
NextBioi 11990.
PROi Q16775.
SOURCEi Search...

Gene expression databases

Bgeei Q16775.
CleanExi HS_HAGH.
ExpressionAtlasi Q16775. baseline and differential.
Genevestigatori Q16775.

Family and domain databases

Gene3Di 3.60.15.10. 1 hit.
HAMAPi MF_01374. Glyoxalase_2.
InterProi IPR001279. Beta-lactamas-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view ]
Pfami PF00753. Lactamase_B. 1 hit.
[Graphical view ]
PIRSFi PIRSF005457. Glx. 1 hit.
SMARTi SM00849. Lactamase_B. 1 hit.
[Graphical view ]
SUPFAMi SSF56281. SSF56281. 1 hit.
TIGRFAMsi TIGR03413. GSH_gloB. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Thalamus.
  2. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
    Tissue: Cervix and Uterus.
  5. "Molecular cloning, heterologous expression, and characterization of human glyoxalase II."
    Ridderstroem M., Saccucci F., Hellman U., Bergman T., Principato G., Mannervik B.
    J. Biol. Chem. 271:319-323(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-308 (ISOFORMS 1/2).
    Tissue: Liver.
  6. "The human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II."
    Cordell P.A., Futers T.S., Grant P.J., Pease R.J.
    J. Biol. Chem. 279:28653-28661(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue."
    Cameron A.D., Ridderstroem M., Olin B., Mannervik B.
    Structure 7:1067-1077(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 49-308 IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS.
    Tissue: Liver.

Entry informationi

Entry nameiGLO2_HUMAN
AccessioniPrimary (citable) accession number: Q16775
Secondary accession number(s): A8K290
, B4DP33, B4DRA7, E7EN93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 1, 2009
Last modified: October 29, 2014
This is version 135 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3