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Q6YP21

- KAT3_HUMAN

UniProt

Q6YP21 - KAT3_HUMAN

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Protein

Kynurenine--oxoglutarate transaminase 3

Gene
CCBL2, KAT3
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). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond By similarity. Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) By similarity.

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
RS-CH(2)-CH(NH3+)COO- + H2O = RSH + NH3 + pyruvate.
L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine.

Cofactori

Pyridoxal phosphate By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Substrate By similarity
Binding sitei71 – 711Substrate; via amide nitrogen By similarity
Binding sitei218 – 2181Substrate By similarity
Binding sitei429 – 4291Substrate By similarity

GO - Molecular functioni

  1. cysteine-S-conjugate beta-lyase activity Source: UniProtKB-EC
  2. kynurenine-glyoxylate transaminase activity Source: UniProtKB
  3. kynurenine-oxoglutarate transaminase activity Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: Ensembl
  2. biosynthetic process Source: InterPro
  3. cellular amino acid metabolic process Source: UniProtKB
  4. cellular nitrogen compound metabolic process Source: Reactome
  5. kynurenine metabolic process Source: UniProtKB
  6. L-kynurenine metabolic process Source: GOC
  7. small molecule metabolic process Source: Reactome
  8. tryptophan catabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS06422-MONOMER.
BRENDAi2.6.1.7. 2681.
ReactomeiREACT_916. Tryptophan catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynurenine--oxoglutarate transaminase 3 (EC:2.6.1.7)
Alternative name(s):
Cysteine-S-conjugate beta-lyase 2 (EC:4.4.1.13)
Kynurenine aminotransferase III
Short name:
KATIII
Kynurenine--glyoxylate transaminase (EC:2.6.1.63)
Kynurenine--oxoglutarate transaminase III
Gene namesi
Name:CCBL2
Synonyms:KAT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:33238. CCBL2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162381274.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Kynurenine--oxoglutarate transaminase 3PRO_0000287704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161N6-acetyllysine; alternate1 Publication
Modified residuei116 – 1161N6-succinyllysine; alternate By similarity
Modified residuei280 – 2801N6-(pyridoxal phosphate)lysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ6YP21.
PaxDbiQ6YP21.
PRIDEiQ6YP21.

PTM databases

PhosphoSiteiQ6YP21.

Expressioni

Gene expression databases

ArrayExpressiQ6YP21.
BgeeiQ6YP21.
CleanExiHS_CCBL2.
GenevestigatoriQ6YP21.

Organism-specific databases

HPAiHPA026538.
HPA027168.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi121128. 7 interactions.
IntActiQ6YP21. 6 interactions.
MINTiMINT-1402454.
STRINGi9606.ENSP00000260508.

Structurei

3D structure databases

ProteinModelPortaliQ6YP21.
SMRiQ6YP21. Positions 41-450.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0436.
HOGENOMiHOG000223045.
HOVERGENiHBG008391.
InParanoidiQ6YP21.
KOiK00816.
OMAiGWSIGPN.
OrthoDBiEOG76DTSB.
PhylomeDBiQ6YP21.
TreeFamiTF352342.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6YP21-1) [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

MFLAQRSLCS LSGRAKFLKT ISSSKILGFS TSAKMSLKFT NAKRIEGLDS    50
NVWIEFTKLA ADPSVVNLGQ GFPDISPPTY VKEELSKIAA IDSLNQYTRG 100
FGHPSLVKAL SYLYEKLYQK QIDSNKEILV TVGAYGSLFN TIQALIDEGD 150
EVILIVPFYD CYEPMVRMAG ATPVFIPLRS KPVYGKRWSS SDWTLDPQEL 200
ESKFNSKTKA IILNTPHNPL GKVYNREELQ VIADLCIKYD TLCISDEVYE 250
WLVYSGNKHL KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPNHLIK 300
HLQTVQQNTI YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR 350
DRMVRLLESV GLKPIVPDGG YFIIADVSLL DPDLSDMKNN EPYDYKFVKW 400
MTKHKKLSAI PVSAFCNSET KSQFEKFVRF CFIKKDSTLD AAEEIIKAWS 450
VQKS 454
Length:454
Mass (Da):51,400
Last modified:July 5, 2004 - v1
Checksum:i2059D4646058BBB3
GO
Isoform 2 (identifier: Q6YP21-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-167: VILIVPFYDCYEPMVR → YNACTVKFTNLKCTAG
     168-454: Missing.

Note: No experimental confirmation available.

Show »
Length:167
Mass (Da):18,352
Checksum:i6CA0C2A9BC6BA211
GO
Isoform 3 (identifier: Q6YP21-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Show »
Length:420
Mass (Da):47,753
Checksum:i1BB37BC0D96DB2EE
GO

Sequence cautioni

The sequence AAC72959.1 differs from that shown. Reason: Frameshift at position 336.
The sequence CAG29278.1 differs from that shown. Reason: Frameshift at position 336.
The sequence AAH00819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAI21695.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI21696.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI41339.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI41340.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061S → P.2 Publications
Corresponds to variant rs1059370 [ dbSNP | Ensembl ].
VAR_032352

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434Missing in isoform 3. VSP_042841Add
BLAST
Alternative sequencei152 – 16716VILIV…EPMVR → YNACTVKFTNLKCTAG in isoform 2. VSP_025603Add
BLAST
Alternative sequencei168 – 454287Missing in isoform 2. VSP_025604Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511W → R in CAG29278. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028624 mRNA. Translation: AAK26163.1.
CR627392 mRNA. Translation: CAH10487.1.
AK057176 mRNA. Translation: BAG51875.1.
AL445991 Genomic DNA. Translation: CAI41345.1.
AL139416, AL445991 Genomic DNA. Translation: CAI21695.1. Sequence problems.
AL445991, AL139416 Genomic DNA. Translation: CAI41339.1. Sequence problems.
AL139416, AL445991 Genomic DNA. Translation: CAI21696.1. Sequence problems.
AL445991, AL139416 Genomic DNA. Translation: CAI41340.1. Sequence problems.
BC000819 mRNA. Translation: AAH00819.1. Different initiation.
AF091090 mRNA. Translation: AAC72959.1. Frameshift.
CR450282 mRNA. Translation: CAG29278.1. Frameshift.
CCDSiCCDS30766.1. [Q6YP21-1]
CCDS30767.1. [Q6YP21-3]
RefSeqiNP_001008661.1. NM_001008661.2. [Q6YP21-1]
NP_001008662.1. NM_001008662.2. [Q6YP21-3]
UniGeneiHs.481898.

Genome annotation databases

EnsembliENST00000260508; ENSP00000260508; ENSG00000137944. [Q6YP21-1]
ENST00000370485; ENSP00000359516; ENSG00000137944. [Q6YP21-2]
ENST00000370491; ENSP00000359522; ENSG00000137944. [Q6YP21-3]
GeneIDi56267.
KEGGihsa:56267.
UCSCiuc001dmp.2. human. [Q6YP21-1]

Polymorphism databases

DMDMi74710502.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028624 mRNA. Translation: AAK26163.1 .
CR627392 mRNA. Translation: CAH10487.1 .
AK057176 mRNA. Translation: BAG51875.1 .
AL445991 Genomic DNA. Translation: CAI41345.1 .
AL139416 , AL445991 Genomic DNA. Translation: CAI21695.1 . Sequence problems.
AL445991 , AL139416 Genomic DNA. Translation: CAI41339.1 . Sequence problems.
AL139416 , AL445991 Genomic DNA. Translation: CAI21696.1 . Sequence problems.
AL445991 , AL139416 Genomic DNA. Translation: CAI41340.1 . Sequence problems.
BC000819 mRNA. Translation: AAH00819.1 . Different initiation.
AF091090 mRNA. Translation: AAC72959.1 . Frameshift.
CR450282 mRNA. Translation: CAG29278.1 . Frameshift.
CCDSi CCDS30766.1. [Q6YP21-1 ]
CCDS30767.1. [Q6YP21-3 ]
RefSeqi NP_001008661.1. NM_001008661.2. [Q6YP21-1 ]
NP_001008662.1. NM_001008662.2. [Q6YP21-3 ]
UniGenei Hs.481898.

3D structure databases

ProteinModelPortali Q6YP21.
SMRi Q6YP21. Positions 41-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121128. 7 interactions.
IntActi Q6YP21. 6 interactions.
MINTi MINT-1402454.
STRINGi 9606.ENSP00000260508.

Chemistry

ChEMBLi CHEMBL2046260.
DrugBanki DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSitei Q6YP21.

Polymorphism databases

DMDMi 74710502.

Proteomic databases

MaxQBi Q6YP21.
PaxDbi Q6YP21.
PRIDEi Q6YP21.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260508 ; ENSP00000260508 ; ENSG00000137944 . [Q6YP21-1 ]
ENST00000370485 ; ENSP00000359516 ; ENSG00000137944 . [Q6YP21-2 ]
ENST00000370491 ; ENSP00000359522 ; ENSG00000137944 . [Q6YP21-3 ]
GeneIDi 56267.
KEGGi hsa:56267.
UCSCi uc001dmp.2. human. [Q6YP21-1 ]

Organism-specific databases

CTDi 56267.
GeneCardsi GC01M089401.
HGNCi HGNC:33238. CCBL2.
HPAi HPA026538.
HPA027168.
MIMi 610656. gene.
neXtProti NX_Q6YP21.
PharmGKBi PA162381274.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0436.
HOGENOMi HOG000223045.
HOVERGENi HBG008391.
InParanoidi Q6YP21.
KOi K00816.
OMAi GWSIGPN.
OrthoDBi EOG76DTSB.
PhylomeDBi Q6YP21.
TreeFami TF352342.

Enzyme and pathway databases

BioCyci MetaCyc:HS06422-MONOMER.
BRENDAi 2.6.1.7. 2681.
Reactomei REACT_916. Tryptophan catabolism.

Miscellaneous databases

GenomeRNAii 56267.
NextBioi 61929.
PROi Q6YP21.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6YP21.
Bgeei Q6YP21.
CleanExi HS_CCBL2.
Genevestigatori Q6YP21.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family."
    Yu P., Li Z., Zhang L., Tagle D.A., Cai T.
    Gene 365:111-118(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal kidney.
  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 3).
    Tissue: Stomach.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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] OF 85-454 (ISOFORM 1).
    Tissue: Placenta.
  6. "Full-insert sequence of mapped XREF EST."
    Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-454, VARIANT PRO-206.
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-338, VARIANT PRO-206.
  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-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKAT3_HUMAN
AccessioniPrimary (citable) accession number: Q6YP21
Secondary accession number(s): B3KQ13
, O95335, Q5JS27, Q5T9T7, Q5T9T8, Q6AI27, Q6ICW1, Q9BVY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 94 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 1
    Human chromosome 1: 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

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