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Protein

Malonyl-CoA-acyl carrier protein transacylase, mitochondrial

Gene

MCAT

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

Functioni

Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias.1 Publication

Catalytic activityi

Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531By similarity
Active sitei270 – 2701By similarity

GO - Molecular functioni

  1. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. transferase activity Source: UniProtKB

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB
  2. metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS02028-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl-CoA-acyl carrier protein transacylase, mitochondrial (EC:2.3.1.39)
Short name:
MCT
Alternative name(s):
Mitochondrial malonyl CoA:ACP acyltransferase
Mitochondrial malonyltransferase
[Acyl-carrier-protein] malonyltransferase
Gene namesi
Name:MCAT
Synonyms:MT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:29622. MCAT.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162395058.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121MitochondrionSequence AnalysisAdd
BLAST
Chaini22 – 390369Malonyl-CoA-acyl carrier protein transacylase, mitochondrialPRO_0000000589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei314 – 3141N6-succinyllysineBy similarity

Proteomic databases

MaxQBiQ8IVS2.
PaxDbiQ8IVS2.
PeptideAtlasiQ8IVS2.
PRIDEiQ8IVS2.

PTM databases

PhosphoSiteiQ8IVS2.

Expressioni

Gene expression databases

BgeeiQ8IVS2.
CleanExiHS_MCAT.
ExpressionAtlasiQ8IVS2. baseline and differential.
GenevestigatoriQ8IVS2.

Organism-specific databases

HPAiHPA035471.

Interactioni

Protein-protein interaction databases

BioGridi118161. 22 interactions.
IntActiQ8IVS2. 2 interactions.
MINTiMINT-4828919.
STRINGi9606.ENSP00000290429.

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 675Combined sources
Turni75 – 839Combined sources
Helixi87 – 9812Combined sources
Helixi102 – 1087Combined sources
Helixi111 – 1155Combined sources
Helixi117 – 13822Combined sources
Helixi140 – 1445Combined sources
Beta strandi146 – 1516Combined sources
Helixi155 – 1628Combined sources
Helixi168 – 18720Combined sources
Beta strandi191 – 1977Combined sources
Helixi204 – 21714Combined sources
Beta strandi225 – 2328Combined sources
Beta strandi235 – 2417Combined sources
Helixi242 – 2509Combined sources
Helixi252 – 2554Combined sources
Beta strandi259 – 2624Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 28612Combined sources
Beta strandi294 – 2985Combined sources
Turni300 – 3023Combined sources
Beta strandi303 – 3053Combined sources
Helixi309 – 3113Combined sources
Helixi312 – 3198Combined sources
Helixi326 – 3338Combined sources
Beta strandi344 – 3529Combined sources
Helixi353 – 3619Combined sources
Helixi363 – 3664Combined sources
Beta strandi369 – 3724Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C2NX-ray1.55A/B60-375[»]
ProteinModelPortaliQ8IVS2.
SMRiQ8IVS2. Positions 60-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IVS2.

Family & Domainsi

Sequence similaritiesi

Belongs to the type II malonyltransferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0331.
GeneTreeiENSGT00390000013715.
HOGENOMiHOG000036504.
HOVERGENiHBG051540.
InParanoidiQ8IVS2.
KOiK00645.
OMAiNEAYHNK.
OrthoDBiEOG7D85X6.
PhylomeDBiQ8IVS2.
TreeFamiTF313401.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.

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. AlignAdd to basket

Isoform 1 (identifier: Q8IVS2-1) [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
MSVRVARVAW VRGLGASYRR GASSFPVPPP GAQGVAELLR DATGAEEEAP
60 70 80 90 100
WAATERRMPG QCSVLLFPGQ GSQVVGMGRG LLNYPRVREL YAAARRVLGY
110 120 130 140 150
DLLELSLHGP QETLDRTVHC QPAIFVASLA AVEKLHHLQP SVIENCVAAA
160 170 180 190 200
GFSVGEFAAL VFAGAMEFAE GLYAVKIRAE AMQEASEAVP SGMLSVLGQP
210 220 230 240 250
QSKFNFACLE AREHCKSLGI ENPVCEVSNY LFPDCRVISG HQEALRFLQK
260 270 280 290 300
NSSKFHFRRT RMLPVSGAFH TRLMEPAVEP LTQALKAVDI KKPLVSVYSN
310 320 330 340 350
VHAHRYRHPG HIHKLLAQQL VSPVKWEQTM HAIYERKKGR GFPQTFEVGP
360 370 380 390
GRQLGAILKS CNMQAWKSYS AVDVLQTLEH VDLDPQEPPR
Length:390
Mass (Da):42,962
Last modified:June 7, 2004 - v2
Checksum:i5CAF7AE9DFF36A21
GO
Isoform 2 (identifier: Q8IVS2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     172-180: LYAVKIRAE → STVSPEEFL
     181-390: Missing.

Show »
Length:180
Mass (Da):19,176
Checksum:i8DA3FDA905D219C7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031A → G.1 Publication
Corresponds to variant rs13815 [ dbSNP | Ensembl ].
VAR_048183

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei172 – 1809LYAVKIRAE → STVSPEEFL in isoform 2. 3 PublicationsVSP_010517
Alternative sequencei181 – 390210Missing in isoform 2. 3 PublicationsVSP_010518Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359401 mRNA. Translation: CAB94789.1.
AL359403 mRNA. Translation: CAB94790.1.
AK314059 mRNA. Translation: BAG36765.1.
AL022237 Genomic DNA. Translation: CAQ07851.1.
AL022237 Genomic DNA. Translation: CAA18261.1.
CH471138 Genomic DNA. Translation: EAW73286.1.
BC030985 mRNA. Translation: AAH30985.1.
BC042195 mRNA. Translation: AAH42195.2.
CCDSiCCDS14045.1. [Q8IVS2-2]
CCDS33660.1. [Q8IVS2-1]
RefSeqiNP_055322.1. NM_014507.3. [Q8IVS2-2]
NP_775738.3. NM_173467.4. [Q8IVS2-1]
UniGeneiHs.349111.

Genome annotation databases

EnsembliENST00000290429; ENSP00000290429; ENSG00000100294. [Q8IVS2-1]
ENST00000327555; ENSP00000331306; ENSG00000100294. [Q8IVS2-2]
GeneIDi27349.
KEGGihsa:27349.
UCSCiuc003bdl.1. human. [Q8IVS2-1]
uc003bdm.1. human.

Polymorphism databases

DMDMi48428076.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359401 mRNA. Translation: CAB94789.1.
AL359403 mRNA. Translation: CAB94790.1.
AK314059 mRNA. Translation: BAG36765.1.
AL022237 Genomic DNA. Translation: CAQ07851.1.
AL022237 Genomic DNA. Translation: CAA18261.1.
CH471138 Genomic DNA. Translation: EAW73286.1.
BC030985 mRNA. Translation: AAH30985.1.
BC042195 mRNA. Translation: AAH42195.2.
CCDSiCCDS14045.1. [Q8IVS2-2]
CCDS33660.1. [Q8IVS2-1]
RefSeqiNP_055322.1. NM_014507.3. [Q8IVS2-2]
NP_775738.3. NM_173467.4. [Q8IVS2-1]
UniGeneiHs.349111.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C2NX-ray1.55A/B60-375[»]
ProteinModelPortaliQ8IVS2.
SMRiQ8IVS2. Positions 60-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118161. 22 interactions.
IntActiQ8IVS2. 2 interactions.
MINTiMINT-4828919.
STRINGi9606.ENSP00000290429.

PTM databases

PhosphoSiteiQ8IVS2.

Polymorphism databases

DMDMi48428076.

Proteomic databases

MaxQBiQ8IVS2.
PaxDbiQ8IVS2.
PeptideAtlasiQ8IVS2.
PRIDEiQ8IVS2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290429; ENSP00000290429; ENSG00000100294. [Q8IVS2-1]
ENST00000327555; ENSP00000331306; ENSG00000100294. [Q8IVS2-2]
GeneIDi27349.
KEGGihsa:27349.
UCSCiuc003bdl.1. human. [Q8IVS2-1]
uc003bdm.1. human.

Organism-specific databases

CTDi27349.
GeneCardsiGC22M043528.
HGNCiHGNC:29622. MCAT.
HPAiHPA035471.
MIMi614479. gene.
neXtProtiNX_Q8IVS2.
PharmGKBiPA162395058.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0331.
GeneTreeiENSGT00390000013715.
HOGENOMiHOG000036504.
HOVERGENiHBG051540.
InParanoidiQ8IVS2.
KOiK00645.
OMAiNEAYHNK.
OrthoDBiEOG7D85X6.
PhylomeDBiQ8IVS2.
TreeFamiTF313401.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:HS02028-MONOMER.

Miscellaneous databases

ChiTaRSiMCAT. human.
EvolutionaryTraceiQ8IVS2.
GeneWikiiMCAT_(gene).
GenomeRNAii27349.
NextBioi50446.
PROiQ8IVS2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IVS2.
CleanExiHS_MCAT.
ExpressionAtlasiQ8IVS2. baseline and differential.
GenevestigatoriQ8IVS2.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  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).
    Tissue: Caudate nucleus.
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 2), VARIANT GLY-303.
    Tissue: Testis.
  6. "Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein."
    Zhang L., Joshi A.K., Smith S.
    J. Biol. Chem. 278:40067-40074(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Structure of human mitochondrial malonyltransferase."
    Structural genomics consortium (SGC)
    Submitted (SEP-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 60-375.

Entry informationi

Entry nameiFABD_HUMAN
AccessioniPrimary (citable) accession number: Q8IVS2
Secondary accession number(s): B0QY72, O95510, O95511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: March 4, 2015
This is version 113 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 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.