SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00505

- AATM_HUMAN

UniProt

P00505 - AATM_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Aspartate aminotransferase, mitochondrial

Gene
GOT2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.1 Publication

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.

Cofactori

Pyridoxal phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651Substrate; via amide nitrogen By similarity
Binding sitei162 – 1621Substrate By similarity
Binding sitei215 – 2151Substrate By similarity
Binding sitei407 – 4071Substrate By similarity

GO - Molecular functioni

  1. kynurenine-oxoglutarate transaminase activity Source: UniProtKB-EC
  2. L-aspartate:2-oxoglutarate aminotransferase activity Source: UniProtKB
  3. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  4. poly(A) RNA binding Source: UniProtKB
  5. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: UniProtKB
  2. 4-hydroxyproline catabolic process Source: BHF-UCL
  3. aspartate biosynthetic process Source: Ensembl
  4. aspartate catabolic process Source: UniProtKB
  5. aspartate metabolic process Source: UniProtKB
  6. carbohydrate metabolic process Source: Reactome
  7. cellular amino acid biosynthetic process Source: Reactome
  8. cellular nitrogen compound metabolic process Source: Reactome
  9. fatty acid transport Source: UniProtKB
  10. gluconeogenesis Source: Reactome
  11. glucose metabolic process Source: Reactome
  12. glutamate catabolic process to 2-oxoglutarate Source: Ensembl
  13. glutamate catabolic process to aspartate Source: Ensembl
  14. glutamate metabolic process Source: UniProtKB
  15. oxaloacetate metabolic process Source: Ensembl
  16. response to ethanol Source: UniProtKB
  17. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS04858-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
REACT_238. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, mitochondrial (EC:2.6.1.1, EC:2.6.1.7)
Short name:
mAspAT
Alternative name(s):
Fatty acid-binding protein
Short name:
FABP-1
Glutamate oxaloacetate transaminase 2
Kynurenine aminotransferase 4
Kynurenine aminotransferase IV
Kynurenine--oxoglutarate transaminase 4
Kynurenine--oxoglutarate transaminase IV
Plasma membrane-associated fatty acid-binding protein
Short name:
FABPpm
Transaminase A
Gene namesi
Name:GOT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:4433. GOT2.

Subcellular locationi

Mitochondrion matrix. Cell membrane
Note: Exposure to alcohol promotes translocation to the cell membrane.1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: UniProtKB
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28818.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929Mitochondrion1 PublicationAdd
BLAST
Chaini30 – 430401Aspartate aminotransferase, mitochondrialPRO_0000001215Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-acetyllysine By similarity
Modified residuei73 – 731N6-acetyllysine; alternate1 Publication
Modified residuei73 – 731N6-succinyllysine; alternate By similarity
Modified residuei82 – 821N6-acetyllysine By similarity
Modified residuei90 – 901N6-acetyllysine; alternate1 Publication
Modified residuei90 – 901N6-succinyllysine; alternate By similarity
Modified residuei96 – 961Nitrated tyrosine By similarity
Modified residuei107 – 1071N6-acetyllysine; alternate By similarity
Modified residuei107 – 1071N6-succinyllysine; alternate By similarity
Modified residuei122 – 1221N6-acetyllysine; alternate By similarity
Modified residuei122 – 1221N6-succinyllysine; alternate By similarity
Modified residuei159 – 1591N6-acetyllysine; alternate1 Publication
Modified residuei159 – 1591N6-succinyllysine; alternate By similarity
Modified residuei185 – 1851N6-acetyllysine; alternate By similarity
Modified residuei185 – 1851N6-succinyllysine; alternate By similarity
Modified residuei227 – 2271N6-succinyllysine By similarity
Modified residuei234 – 2341N6-acetyllysine1 Publication
Modified residuei279 – 2791N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residuei279 – 2791N6-acetyllysine; alternate By similarity
Modified residuei296 – 2961N6-acetyllysine; alternate1 Publication
Modified residuei296 – 2961N6-succinyllysine; alternate By similarity
Modified residuei302 – 3021N6-acetyllysine By similarity
Modified residuei309 – 3091N6-acetyllysine; alternate By similarity
Modified residuei309 – 3091N6-succinyllysine; alternate By similarity
Modified residuei338 – 3381N6-acetyllysine; alternate By similarity
Modified residuei338 – 3381N6-succinyllysine; alternate By similarity
Modified residuei345 – 3451N6-acetyllysine By similarity
Modified residuei363 – 3631N6-acetyllysine; alternate By similarity
Modified residuei363 – 3631N6-succinyllysine; alternate By similarity
Modified residuei364 – 3641N6-acetyllysine By similarity
Modified residuei387 – 3871N6-acetyllysine By similarity
Modified residuei396 – 3961N6-acetyllysine; alternate1 Publication
Modified residuei396 – 3961N6-succinyllysine; alternate By similarity
Modified residuei404 – 4041N6-acetyllysine; alternate1 Publication
Modified residuei404 – 4041N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiP00505.
PaxDbiP00505.
PRIDEiP00505.

2D gel databases

UCD-2DPAGEP00505.

PTM databases

PhosphoSiteiP00505.

Expressioni

Inductioni

Up-regulated by long-time exposure to alcohol.1 Publication

Gene expression databases

ArrayExpressiP00505.
BgeeiP00505.
CleanExiHS_GOT2.
GenevestigatoriP00505.

Organism-specific databases

HPAiHPA018139.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi109068. 15 interactions.
IntActiP00505. 7 interactions.
MINTiMINT-1406848.
STRINGi9606.ENSP00000245206.

Structurei

3D structure databases

ProteinModelPortaliP00505.
SMRiP00505. Positions 30-430.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1448.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00505.
KOiK14455.
OMAiRVGAFTM.
OrthoDBiEOG74J980.
PhylomeDBiP00505.
TreeFamiTF300641.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 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 1 (identifier: P00505-1) [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

MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA    50
FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG 100
GLAEFCKASA ELALGENSEV LKSGRFVTVQ TISGTGALRI GASFLQRFFK 150
FSRDVFLPKP TWGNHTPIFR DAGMQLQGYR YYDPKTCGFD FTGAVEDISK 200
IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA FFDMAYQGFA 250
SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE 300
AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKVMADR 350
IIGMRTQLVS NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI 400
YMTKDGRISV AGVTSSNVGY LAHAIHQVTK 430
Length:430
Mass (Da):47,518
Last modified:October 5, 2010 - v3
Checksum:iF559567ABF2DB346
GO
Isoform 2 (identifier: P00505-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-125: Missing.

Show »
Length:387
Mass (Da):43,030
Checksum:iFF09030A2B5C4E62
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → S.
Corresponds to variant rs11558171 [ dbSNP | Ensembl ].
VAR_055494
Natural varianti188 – 1881G → S.
Corresponds to variant rs11076256 [ dbSNP | Ensembl ].
VAR_031710
Natural varianti346 – 3461V → G.3 Publications
Corresponds to variant rs30842 [ dbSNP | Ensembl ].
VAR_031711
Natural varianti428 – 4281V → A.1 Publication
Corresponds to variant rs17849335 [ dbSNP | Ensembl ].
VAR_031712

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei83 – 12543Missing in isoform 2. VSP_054848Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1112AE → EA AA sequence 1 Publication
Sequence conflicti255 – 2551D → N AA sequence 1 Publication
Sequence conflicti258 – 2581A → T in BAD96991. 1 Publication
Sequence conflicti305 – 3051E → Q AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22632 mRNA. Translation: AAA35568.1.
AK295993 mRNA. Translation: BAG58768.1.
AK223271 mRNA. Translation: BAD96991.1.
AC012183 Genomic DNA. No translation available.
BC000525 mRNA. Translation: AAH00525.1.
CCDSiCCDS10801.1. [P00505-1]
CCDS67045.1. [P00505-2]
PIRiA31873. XNHUDM.
RefSeqiNP_001273149.1. NM_001286220.1. [P00505-2]
NP_002071.2. NM_002080.3. [P00505-1]
UniGeneiHs.599470.

Genome annotation databases

EnsembliENST00000245206; ENSP00000245206; ENSG00000125166.
ENST00000434819; ENSP00000394100; ENSG00000125166.
GeneIDi2806.
KEGGihsa:2806.
UCSCiuc002eof.1. human. [P00505-1]

Polymorphism databases

DMDMi308153643.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22632 mRNA. Translation: AAA35568.1 .
AK295993 mRNA. Translation: BAG58768.1 .
AK223271 mRNA. Translation: BAD96991.1 .
AC012183 Genomic DNA. No translation available.
BC000525 mRNA. Translation: AAH00525.1 .
CCDSi CCDS10801.1. [P00505-1 ]
CCDS67045.1. [P00505-2 ]
PIRi A31873. XNHUDM.
RefSeqi NP_001273149.1. NM_001286220.1. [P00505-2 ]
NP_002071.2. NM_002080.3. [P00505-1 ]
UniGenei Hs.599470.

3D structure databases

ProteinModelPortali P00505.
SMRi P00505. Positions 30-430.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109068. 15 interactions.
IntActi P00505. 7 interactions.
MINTi MINT-1406848.
STRINGi 9606.ENSP00000245206.

Chemistry

DrugBanki DB00128. L-Aspartic Acid.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSitei P00505.

Polymorphism databases

DMDMi 308153643.

2D gel databases

UCD-2DPAGE P00505.

Proteomic databases

MaxQBi P00505.
PaxDbi P00505.
PRIDEi P00505.

Protocols and materials databases

DNASUi 2806.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000245206 ; ENSP00000245206 ; ENSG00000125166 .
ENST00000434819 ; ENSP00000394100 ; ENSG00000125166 .
GeneIDi 2806.
KEGGi hsa:2806.
UCSCi uc002eof.1. human. [P00505-1 ]

Organism-specific databases

CTDi 2806.
GeneCardsi GC16M058741.
H-InvDB HIX0013095.
HGNCi HGNC:4433. GOT2.
HPAi HPA018139.
MIMi 138150. gene.
neXtProti NX_P00505.
PharmGKBi PA28818.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1448.
HOGENOMi HOG000185898.
HOVERGENi HBG000951.
InParanoidi P00505.
KOi K14455.
OMAi RVGAFTM.
OrthoDBi EOG74J980.
PhylomeDBi P00505.
TreeFami TF300641.

Enzyme and pathway databases

BioCyci MetaCyc:HS04858-MONOMER.
Reactomei REACT_1520. Gluconeogenesis.
REACT_238. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSi Got2. human.
GeneWikii GOT2.
GenomeRNAii 2806.
NextBioi 11061.
PROi P00505.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00505.
Bgeei P00505.
CleanExi HS_GOT2.
Genevestigatori P00505.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11879. PTHR11879. 1 hit.
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
PRINTSi PR00799. TRANSAMINASE.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA."
    Pol S., Bousquet-Lemercier B., Pave-Preux M., Pawlak A., Nalpas B., Berthelot P., Hanoune J., Barouki R.
    Biochem. Biophys. Res. Commun. 157:1309-1315(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-346.
  2. "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 2), VARIANT GLY-346.
    Tissue: Subthalamic nucleus.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Gastric mucosa.
  4. "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].
  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 1), VARIANT ALA-428.
    Tissue: Muscle.
  6. "The primary structure of mitochondrial aspartate aminotransferase from human heart."
    Martini F., Angelaccio S., Barra D., Pascarella S., Maras B., Doonan S., Bossa F.
    Biochim. Biophys. Acta 832:46-51(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-430, VARIANT GLY-346.
  7. "Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells."
    Zhou S.L., Gordon R.E., Bradbury M., Stump D., Kiang C.L., Berk P.D.
    Hepatology 27:1064-1074(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
  8. "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-73; LYS-90; LYS-159; LYS-234; LYS-296; LYS-396 AND LYS-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAATM_HUMAN
AccessioniPrimary (citable) accession number: P00505
Secondary accession number(s): B4DJA6
, E7ERW2, Q53FL3, Q9BWA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 159 of the entry and version 3 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

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi