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O15382

- BCAT2_HUMAN

UniProt

O15382 - BCAT2_HUMAN

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Protein
Branched-chain-amino-acid aminotransferase, mitochondrial
Gene
BCAT2, BCATM, BCT2, ECA40
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.

Catalytic activityi

L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.
L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.

Cofactori

Pyridoxal phosphate.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681Substrate

GO - Molecular functioni

  1. L-isoleucine transaminase activity Source: UniProtKB-EC
  2. L-leucine transaminase activity Source: UniProtKB-EC
  3. L-valine transaminase activity Source: UniProtKB-EC
  4. branched-chain-amino-acid transaminase activity Source: Reactome
Complete GO annotation...

GO - Biological processi

  1. branched-chain amino acid biosynthetic process Source: ProtInc
  2. branched-chain amino acid catabolic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. isoleucine catabolic process Source: Ensembl
  5. leucine metabolic process Source: Ensembl
  6. regulation of hormone levels Source: Ensembl
  7. small molecule metabolic process Source: Reactome
  8. valine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.42. 2681.
ReactomeiREACT_197. Branched-chain amino acid catabolism.
SABIO-RKiO15382.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferase, mitochondrial (EC:2.6.1.42)
Short name:
BCAT(m)
Alternative name(s):
Placental protein 18
Short name:
PP18
Gene namesi
Name:BCAT2
Synonyms:BCATM, BCT2, ECA40
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:977. BCAT2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi342 – 3421C → A: Reduces activity about 6-fold. 1 Publication
Mutagenesisi345 – 3451C → A: Slight reduction of activity. 1 Publication

Organism-specific databases

PharmGKBiPA25289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727Mitochondrion
Add
BLAST
Chaini28 – 392365Branched-chain-amino-acid aminotransferase, mitochondrial
PRO_0000001271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291N6-(pyridoxal phosphate)lysine
Modified residuei321 – 3211N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO15382.
PaxDbiO15382.
PRIDEiO15382.

PTM databases

PhosphoSiteiO15382.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiO15382.
BgeeiO15382.
CleanExiHS_BCAT2.
GenevestigatoriO15382.

Organism-specific databases

HPAiHPA054091.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi107062. 7 interactions.
IntActiO15382. 3 interactions.
STRINGi9606.ENSP00000322991.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 363
Beta strandi51 – 533
Turni57 – 593
Beta strandi63 – 719
Beta strandi72 – 754
Beta strandi79 – 835
Beta strandi86 – 883
Helixi93 – 964
Beta strandi100 – 1023
Beta strandi105 – 1095
Beta strandi115 – 1195
Helixi120 – 13314
Helixi141 – 15414
Helixi156 – 1583
Beta strandi162 – 1643
Beta strandi166 – 17510
Beta strandi181 – 1833
Beta strandi186 – 19712
Beta strandi200 – 2056
Beta strandi209 – 2135
Helixi231 – 2333
Turni234 – 2363
Helixi237 – 24610
Beta strandi250 – 2567
Turni257 – 2604
Beta strandi261 – 2655
Beta strandi268 – 2758
Beta strandi281 – 2855
Beta strandi289 – 2924
Helixi296 – 30813
Beta strandi310 – 3156
Helixi320 – 3289
Beta strandi332 – 3398
Turni340 – 3423
Beta strandi343 – 35210
Beta strandi355 – 3584
Helixi362 – 3643
Helixi367 – 38014
Beta strandi389 – 3913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKFX-ray1.95A/B28-392[»]
1EKPX-ray2.50A/B28-392[»]
1EKVX-ray2.25A/B28-392[»]
1KT8X-ray1.90A/B28-392[»]
1KTAX-ray1.90A/B28-392[»]
2A1HX-ray1.80A/B28-392[»]
2HDKX-ray2.40A/B28-392[»]
2HG8X-ray1.80A/B28-392[»]
2HGWX-ray1.98A/B28-392[»]
2HGXX-ray1.80A/B28-392[»]
2HHFX-ray1.80A/B28-392[»]
ProteinModelPortaliO15382.
SMRiO15382. Positions 30-392.

Miscellaneous databases

EvolutionaryTraceiO15382.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0115.
HOGENOMiHOG000276704.
HOVERGENiHBG050678.
InParanoidiO15382.
KOiK00826.
OrthoDBiEOG7NGQB7.
PhylomeDBiO15382.
TreeFamiTF300882.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 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 A (identifier: O15382-1) [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

MAAAALGQIW ARKLLSVPWL LCGPRRYASS SFKAADLQLE MTQKPHKKPG    50
PGEPLVFGKT FTDHMLMVEW NDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ 100
LFEGMKAFKG KDQQVRLFRP WLNMDRMLRS AMRLCLPSFD KLELLECIRR 150
LIEVDKDWVP DAAGTSLYVR PVLIGNEPSL GVSQPTRALL FVILCPVGAY 200
FPGGSVTPVS LLADPAFIRA WVGGVGNYKL GGNYGPTVLV QQEALKRGCE 250
QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV LELVTPPLNG VILPGVVRQS 300
LLDMAQTWGE FRVVERTITM KQLLRALEEG RVREVFGSGT ACQVCPVHRI 350
LYKDRNLHIP TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV 392
Length:392
Mass (Da):44,288
Last modified:May 2, 2002 - v2
Checksum:iEC07047264B190DA
GO
Isoform B (identifier: O15382-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     9-100: Missing.

Show »
Length:300
Mass (Da):33,777
Checksum:i656A626FEC867073
GO

Sequence cautioni

The sequence AAB53087.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861T → R.2 Publications
Corresponds to variant rs11548193 [ dbSNP | Ensembl ].
VAR_048234

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 10092Missing in isoform B.
VSP_000236Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541V → L in AAB53087. 1 Publication
Sequence conflicti207 – 2071T → N in AAB53087. 1 Publication
Sequence conflicti214 – 2163DPA → EPT in AAB53087. 1 Publication
Sequence conflicti253 – 2531L → F in AAB53087. 1 Publication
Sequence conflicti326 – 3261A → P in AAB53087. 1 Publication
Sequence conflicti330 – 3301G → A in AAB53087. 1 Publication
Sequence conflicti349 – 3491R → G in AAB53087. 1 Publication
Sequence conflicti357 – 3571L → F in AAB53087. 1 Publication
Sequence conflicti370 – 3701L → F in AAB53087. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U68418 mRNA. Translation: AAB67672.1.
AF268047 mRNA. Translation: AAK38368.1.
AF268048 mRNA. Translation: AAK38369.1.
AK314548 mRNA. Translation: BAG37134.1.
CH471177 Genomic DNA. Translation: EAW52403.1.
BC001900 mRNA. Translation: AAH01900.1.
BC004243 mRNA. Translation: AAH04243.2.
U62739 mRNA. Translation: AAB53087.1. Different initiation.
CCDSiCCDS12735.1. [O15382-1]
CCDS54290.1. [O15382-2]
RefSeqiNP_001158245.1. NM_001164773.1. [O15382-2]
NP_001181.2. NM_001190.3. [O15382-1]
NP_001271254.1. NM_001284325.1.
UniGeneiHs.512670.

Genome annotation databases

EnsembliENST00000316273; ENSP00000322991; ENSG00000105552. [O15382-1]
ENST00000545387; ENSP00000440973; ENSG00000105552. [O15382-2]
GeneIDi587.
KEGGihsa:587.
UCSCiuc002pkq.4. human. [O15382-1]
uc002pkt.3. human. [O15382-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U68418 mRNA. Translation: AAB67672.1 .
AF268047 mRNA. Translation: AAK38368.1 .
AF268048 mRNA. Translation: AAK38369.1 .
AK314548 mRNA. Translation: BAG37134.1 .
CH471177 Genomic DNA. Translation: EAW52403.1 .
BC001900 mRNA. Translation: AAH01900.1 .
BC004243 mRNA. Translation: AAH04243.2 .
U62739 mRNA. Translation: AAB53087.1 . Different initiation.
CCDSi CCDS12735.1. [O15382-1 ]
CCDS54290.1. [O15382-2 ]
RefSeqi NP_001158245.1. NM_001164773.1. [O15382-2 ]
NP_001181.2. NM_001190.3. [O15382-1 ]
NP_001271254.1. NM_001284325.1.
UniGenei Hs.512670.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EKF X-ray 1.95 A/B 28-392 [» ]
1EKP X-ray 2.50 A/B 28-392 [» ]
1EKV X-ray 2.25 A/B 28-392 [» ]
1KT8 X-ray 1.90 A/B 28-392 [» ]
1KTA X-ray 1.90 A/B 28-392 [» ]
2A1H X-ray 1.80 A/B 28-392 [» ]
2HDK X-ray 2.40 A/B 28-392 [» ]
2HG8 X-ray 1.80 A/B 28-392 [» ]
2HGW X-ray 1.98 A/B 28-392 [» ]
2HGX X-ray 1.80 A/B 28-392 [» ]
2HHF X-ray 1.80 A/B 28-392 [» ]
ProteinModelPortali O15382.
SMRi O15382. Positions 30-392.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107062. 7 interactions.
IntActi O15382. 3 interactions.
STRINGi 9606.ENSP00000322991.

Chemistry

DrugBanki DB00142. L-Glutamic Acid.
DB00167. L-Isoleucine.
DB00149. L-Leucine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSitei O15382.

Proteomic databases

MaxQBi O15382.
PaxDbi O15382.
PRIDEi O15382.

Protocols and materials databases

DNASUi 587.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316273 ; ENSP00000322991 ; ENSG00000105552 . [O15382-1 ]
ENST00000545387 ; ENSP00000440973 ; ENSG00000105552 . [O15382-2 ]
GeneIDi 587.
KEGGi hsa:587.
UCSCi uc002pkq.4. human. [O15382-1 ]
uc002pkt.3. human. [O15382-2 ]

Organism-specific databases

CTDi 587.
GeneCardsi GC19M049298.
HGNCi HGNC:977. BCAT2.
HPAi HPA054091.
MIMi 113530. gene.
neXtProti NX_O15382.
PharmGKBi PA25289.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0115.
HOGENOMi HOG000276704.
HOVERGENi HBG050678.
InParanoidi O15382.
KOi K00826.
OrthoDBi EOG7NGQB7.
PhylomeDBi O15382.
TreeFami TF300882.

Enzyme and pathway databases

BRENDAi 2.6.1.42. 2681.
Reactomei REACT_197. Branched-chain amino acid catabolism.
SABIO-RKi O15382.

Miscellaneous databases

EvolutionaryTracei O15382.
GenomeRNAii 587.
NextBioi 2399.
PROi O15382.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15382.
Bgeei O15382.
CleanExi HS_BCAT2.
Genevestigatori O15382.

Family and domain databases

InterProi IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view ]
PANTHERi PTHR11825. PTHR11825. 1 hit.
Pfami PF01063. Aminotran_4. 1 hit.
[Graphical view ]
PIRSFi PIRSF006468. BCAT1. 1 hit.
SUPFAMi SSF56752. SSF56752. 1 hit.
TIGRFAMsi TIGR01123. ilvE_II. 1 hit.
PROSITEi PS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm)."
    Bledsoe R.K., Dawson P.A., Hutson S.M.
    Biochim. Biophys. Acta 1339:9-13(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-186.
  2. "Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant."
    Than N.G., Sumegi B., Than G.N., Bellyei S., Bohn H.
    Placenta 22:235-243(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
    Tissue: Placenta.
  3. "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 A).
    Tissue: Heart.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Lung and Skin.
  6. "Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases."
    Eden A., Simchen G., Benvenisty N.
    J. Biol. Chem. 271:20242-20245(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-392 (ISOFORM A), VARIANT ARG-186.
    Tissue: Brain.
  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-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The structure of human mitochondrial branched-chain aminotransferase."
    Yennawar N.H., Dunbar J., Conway M.E., Hutson S.M., Farber G.K.
    Acta Crystallogr. D 57:506-515(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-392 IN COMPLEX WITH COFACTOR, SUBUNIT.
  10. "Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms."
    Yennawar N.H., Conway M.E., Yennawar H.P., Farber G.K., Hutson S.M.
    Biochemistry 41:11592-11601(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATES.
  11. "Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin."
    Goto M., Miyahara I., Hirotsu K., Conway M., Yennawar N., Islam M.M., Hutson S.M.
    J. Biol. Chem. 280:37246-37256(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATE ANALOGS.
  12. "Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis."
    Yennawar N.H., Islam M.M., Conway M., Wallin R., Hutson S.M.
    J. Biol. Chem. 281:39660-39671(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR AND SUBSTRATE ANALOGS, MUTAGENESIS OF CYS-342 AND CYS-345.

Entry informationi

Entry nameiBCAT2_HUMAN
AccessioniPrimary (citable) accession number: O15382
Secondary accession number(s): B2RB87
, O00269, Q96KG1, Q9BTB6, Q9BUU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: September 3, 2014
This is version 145 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 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

Similar proteinsi