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Protein

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

Gene

OXSM

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

Functioni

May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.1 Publication

Catalytic activityi

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Enzyme regulationi

Inhibited by cerulenin.1 Publication

Kineticsi

The highest catalytic efficiency is observed for C10-[acyl-carrier-protein].

  1. KM=3.9 µM for C4-[acyl-carrier-protein]1 Publication
  2. KM=1.9 µM for C6-[acyl-carrier-protein]1 Publication
  3. KM=10.9 µM for C8-[acyl-carrier-protein]1 Publication
  4. KM=1.8 µM for C10-[acyl-carrier-protein]1 Publication
  5. KM=9.5 µM for C12-[acyl-carrier-protein]1 Publication
  6. KM=50.8 µM for C14-[acyl-carrier-protein]1 Publication
  1. Vmax=129 nmol/min/mg enzyme toward C4-[acyl-carrier-protein]1 Publication
  2. Vmax=241 nmol/min/mg enzyme toward C6-[acyl-carrier-protein]1 Publication
  3. Vmax=271 nmol/min/mg enzyme toward C8-[acyl-carrier-protein]1 Publication
  4. Vmax=364 nmol/min/mg enzyme toward C10-[acyl-carrier-protein]1 Publication
  5. Vmax=1045 nmol/min/mg enzyme toward C12-[acyl-carrier-protein]1 Publication
  6. Vmax=115 nmol/min/mg enzyme toward C14-[acyl-carrier-protein]1 Publication

Pathway: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: HGNC

GO - Biological processi

  • acyl-CoA metabolic process Source: HGNC
  • medium-chain fatty acid biosynthetic process Source: HGNC
  • short-chain fatty acid biosynthetic process Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

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

Enzyme and pathway databases

BRENDAi2.3.1.41. 2681.
SABIO-RKQ9NWU1.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (EC:2.3.1.41)
Alternative name(s):
Beta-ketoacyl-ACP synthase
Gene namesi
Name:OXSM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:26063. OXSM.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671214.

Polymorphism and mutation databases

BioMutaiOXSM.
DMDMi74753030.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
BLAST
Chaini28 – 4594323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrialPRO_0000232660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-acetyllysine; alternateBy similarity
Modified residuei109 – 1091N6-succinyllysine; alternateBy similarity
Modified residuei113 – 1131N6-succinyllysineBy similarity
Modified residuei174 – 1741N6-acetyllysine; alternate1 Publication
Modified residuei174 – 1741N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NWU1.
PaxDbiQ9NWU1.
PeptideAtlasiQ9NWU1.
PRIDEiQ9NWU1.

PTM databases

PhosphoSiteiQ9NWU1.

Expressioni

Tissue specificityi

Widely expressed. Higher expression in heart, skeletal muscle, liver and kidney which contain high levels of active mitochondria.1 Publication

Gene expression databases

BgeeiQ9NWU1.
CleanExiHS_OXSM.
ExpressionAtlasiQ9NWU1. baseline and differential.
GenevisibleiQ9NWU1. HS.

Organism-specific databases

HPAiHPA021293.
HPA021300.
HPA021337.

Interactioni

Protein-protein interaction databases

BioGridi120328. 5 interactions.
STRINGi9606.ENSP00000280701.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 414Combined sources
Beta strandi44 – 5310Combined sources
Beta strandi56 – 583Combined sources
Helixi59 – 679Combined sources
Beta strandi73 – 753Combined sources
Helixi79 – 813Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 974Combined sources
Helixi103 – 1053Combined sources
Helixi109 – 1124Combined sources
Helixi117 – 13317Combined sources
Helixi140 – 1445Combined sources
Beta strandi146 – 1538Combined sources
Helixi157 – 17014Combined sources
Helixi172 – 1743Combined sources
Helixi179 – 1824Combined sources
Helixi187 – 19610Combined sources
Helixi208 – 2103Combined sources
Helixi211 – 22515Combined sources
Beta strandi229 – 2379Combined sources
Helixi242 – 2509Combined sources
Turni260 – 2623Combined sources
Beta strandi279 – 2879Combined sources
Helixi288 – 2936Combined sources
Beta strandi300 – 30910Combined sources
Beta strandi314 – 3163Combined sources
Helixi322 – 33514Combined sources
Helixi339 – 3413Combined sources
Beta strandi344 – 3463Combined sources
Helixi353 – 36715Combined sources
Helixi368 – 3725Combined sources
Beta strandi374 – 3774Combined sources
Helixi380 – 3834Combined sources
Helixi387 – 3893Combined sources
Helixi390 – 40415Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi439 – 4468Combined sources
Turni447 – 4493Combined sources
Beta strandi450 – 4578Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9HX-ray1.80A39-459[»]
2IWYX-ray2.06A/B38-459[»]
2IWZX-ray1.65A/B38-459[»]
ProteinModelPortaliQ9NWU1.
SMRiQ9NWU1. Positions 38-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NWU1.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-ketoacyl-ACP synthases family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0304.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ9NWU1.
KOiK09458.
OMAiQKASRPY.
PhylomeDBiQ9NWU1.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR017568. 3-oxoacyl-ACP_synth-2.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000447. KAS_II. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR03150. fabF. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 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. AlignAdd to basket

Isoform 1 (identifier: Q9NWU1-1) [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
MSNCLQNFLK ITSTRLLCSR LCQQLRSKRK FFGTVPISRL HRRVVITGIG
60 70 80 90 100
LVTPLGVGTH LVWDRLIGGE SGIVSLVGEE YKSIPCSVAA YVPRGSDEGQ
110 120 130 140 150
FNEQNFVSKS DIKSMSSPTI MAIGAAELAM KDSGWHPQSE ADQVATGVAI
160 170 180 190 200
GMGMIPLEVV SETALNFQTK GYNKVSPFFV PKILVNMAAG QVSIRYKLKG
210 220 230 240 250
PNHAVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI SPLSLAGFSR
260 270 280 290 300
ARALSTNSDP KLACRPFHPK RDGFVMGEGA AVLVLEEYEH AVQRRARIYA
310 320 330 340 350
EVLGYGLSGD AGHITAPDPE GEGALRCMAA ALKDAGVQPE EISYINAHAT
360 370 380 390 400
STPLGDAAEN KAIKHLFKDH AYALAVSSTK GATGHLLGAA GAVEAAFTTL
410 420 430 440 450
ACYYQKLPPT LNLDCSEPEF DLNYVPLKAQ EWKTEKRFIG LTNSFGFGGT

NATLCIAGL
Length:459
Mass (Da):48,843
Last modified:October 1, 2000 - v1
Checksum:iB2EF550CD354F18C
GO
Isoform 2 (identifier: Q9NWU1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-311: Missing.

Show »
Length:376
Mass (Da):40,035
Checksum:iB9470D089DE7CF7D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061F → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_036064

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei229 – 31183Missing in isoform 2. 1 PublicationVSP_041671Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000611 mRNA. Translation: BAA91286.1.
AK225260 mRNA. No translation available.
AC092798 Genomic DNA. No translation available.
BC008202 mRNA. Translation: AAH08202.1.
CCDSiCCDS2643.1. [Q9NWU1-1]
CCDS46780.1. [Q9NWU1-2]
RefSeqiNP_001138863.1. NM_001145391.1. [Q9NWU1-2]
NP_060367.1. NM_017897.2. [Q9NWU1-1]
XP_006713279.1. XM_006713216.2. [Q9NWU1-1]
UniGeneiHs.55781.

Genome annotation databases

EnsembliENST00000280701; ENSP00000280701; ENSG00000151093. [Q9NWU1-1]
ENST00000420173; ENSP00000411303; ENSG00000151093. [Q9NWU1-2]
GeneIDi54995.
KEGGihsa:54995.
UCSCiuc003cdn.3. human. [Q9NWU1-1]
uc010hfh.3. human. [Q9NWU1-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000611 mRNA. Translation: BAA91286.1.
AK225260 mRNA. No translation available.
AC092798 Genomic DNA. No translation available.
BC008202 mRNA. Translation: AAH08202.1.
CCDSiCCDS2643.1. [Q9NWU1-1]
CCDS46780.1. [Q9NWU1-2]
RefSeqiNP_001138863.1. NM_001145391.1. [Q9NWU1-2]
NP_060367.1. NM_017897.2. [Q9NWU1-1]
XP_006713279.1. XM_006713216.2. [Q9NWU1-1]
UniGeneiHs.55781.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9HX-ray1.80A39-459[»]
2IWYX-ray2.06A/B38-459[»]
2IWZX-ray1.65A/B38-459[»]
ProteinModelPortaliQ9NWU1.
SMRiQ9NWU1. Positions 38-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120328. 5 interactions.
STRINGi9606.ENSP00000280701.

PTM databases

PhosphoSiteiQ9NWU1.

Polymorphism and mutation databases

BioMutaiOXSM.
DMDMi74753030.

Proteomic databases

MaxQBiQ9NWU1.
PaxDbiQ9NWU1.
PeptideAtlasiQ9NWU1.
PRIDEiQ9NWU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280701; ENSP00000280701; ENSG00000151093. [Q9NWU1-1]
ENST00000420173; ENSP00000411303; ENSG00000151093. [Q9NWU1-2]
GeneIDi54995.
KEGGihsa:54995.
UCSCiuc003cdn.3. human. [Q9NWU1-1]
uc010hfh.3. human. [Q9NWU1-2]

Organism-specific databases

CTDi54995.
GeneCardsiGC03P025824.
HGNCiHGNC:26063. OXSM.
HPAiHPA021293.
HPA021300.
HPA021337.
MIMi610324. gene.
neXtProtiNX_Q9NWU1.
PharmGKBiPA142671214.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0304.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ9NWU1.
KOiK09458.
OMAiQKASRPY.
PhylomeDBiQ9NWU1.

Enzyme and pathway databases

UniPathwayiUPA00094.
BRENDAi2.3.1.41. 2681.
SABIO-RKQ9NWU1.

Miscellaneous databases

EvolutionaryTraceiQ9NWU1.
GenomeRNAii54995.
NextBioi58306.
PROiQ9NWU1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NWU1.
CleanExiHS_OXSM.
ExpressionAtlasiQ9NWU1. baseline and differential.
GenevisibleiQ9NWU1. HS.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR017568. 3-oxoacyl-ACP_synth-2.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000447. KAS_II. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR03150. fabF. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 AND 2).
    Tissue: Carcinoma.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Placenta.
  4. "Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain."
    Zhang L., Joshi A.K., Hofmann J., Schweizer E., Smith S.
    J. Biol. Chem. 280:12422-12429(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "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-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structure of mitochondrial beta-ketoacyl synthase."
    Bunkoczi G., Wu X., Smee C., Gileadi O., Arrowsmith C., Edwards A., Sundstrom M., Weigelt J., von Delft F., Oppermann U.
    Submitted (DEC-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-459.
  8. "Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase."
    Christensen C.E., Kragelund B.B., von Wettstein-Knowles P., Henriksen A.
    Protein Sci. 16:261-272(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-459.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-106.

Entry informationi

Entry nameiOXSM_HUMAN
AccessioniPrimary (citable) accession number: Q9NWU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 118 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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.