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.

Q9NWU1

- OXSM_HUMAN

UniProt

Q9NWU1 - OXSM_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

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

Gene
OXSM
Organism
Homo sapiens (Human)
Status
Reviewed - 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]
  3. KM=10.9 µM for C8-[acyl-carrier-protein]
  4. KM=1.8 µM for C10-[acyl-carrier-protein]
  5. KM=9.5 µM for C12-[acyl-carrier-protein]
  6. KM=50.8 µM for C14-[acyl-carrier-protein]

Vmax=129 nmol/min/mg enzyme toward C4-[acyl-carrier-protein]

Vmax=241 nmol/min/mg enzyme toward C6-[acyl-carrier-protein]

Vmax=271 nmol/min/mg enzyme toward C8-[acyl-carrier-protein]

Vmax=364 nmol/min/mg enzyme toward C10-[acyl-carrier-protein]

Vmax=1045 nmol/min/mg enzyme toward C12-[acyl-carrier-protein]

Vmax=115 nmol/min/mg enzyme toward C14-[acyl-carrier-protein]

Pathwayi

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: HGNC

GO - Biological processi

  1. acyl-CoA metabolic process Source: HGNC
  2. medium-chain fatty acid biosynthetic process Source: HGNC
  3. 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: Chromosome 3

Organism-specific databases

HGNCiHGNC:26063. OXSM.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671214.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

ArrayExpressiQ9NWU1.
BgeeiQ9NWU1.
CleanExiHS_OXSM.
GenevestigatoriQ9NWU1.

Organism-specific databases

HPAiHPA021293.
HPA021300.
HPA021337.

Interactioni

Protein-protein interaction databases

BioGridi120328. 2 interactions.
STRINGi9606.ENSP00000280701.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9NWU1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0304.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ9NWU1.
KOiK09458.
OMAiHAQKRNA.
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. Align

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

MSNCLQNFLK ITSTRLLCSR LCQQLRSKRK FFGTVPISRL HRRVVITGIG    50
LVTPLGVGTH LVWDRLIGGE SGIVSLVGEE YKSIPCSVAA YVPRGSDEGQ 100
FNEQNFVSKS DIKSMSSPTI MAIGAAELAM KDSGWHPQSE ADQVATGVAI 150
GMGMIPLEVV SETALNFQTK GYNKVSPFFV PKILVNMAAG QVSIRYKLKG 200
PNHAVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI SPLSLAGFSR 250
ARALSTNSDP KLACRPFHPK RDGFVMGEGA AVLVLEEYEH AVQRRARIYA 300
EVLGYGLSGD AGHITAPDPE GEGALRCMAA ALKDAGVQPE EISYINAHAT 350
STPLGDAAEN KAIKHLFKDH AYALAVSSTK GATGHLLGAA GAVEAAFTTL 400
ACYYQKLPPT LNLDCSEPEF DLNYVPLKAQ EWKTEKRFIG LTNSFGFGGT 450
NATLCIAGL 459
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. VSP_041671Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006713216.1. [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]

Polymorphism databases

DMDMi74753030.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK000611 mRNA. Translation: BAA91286.1 .
AK225260 mRNA. No translation available.
AC092798 Genomic DNA. No translation available.
BC008202 mRNA. Translation: AAH08202.1 .
CCDSi CCDS2643.1. [Q9NWU1-1 ]
CCDS46780.1. [Q9NWU1-2 ]
RefSeqi NP_001138863.1. NM_001145391.1. [Q9NWU1-2 ]
NP_060367.1. NM_017897.2. [Q9NWU1-1 ]
XP_006713279.1. XM_006713216.1. [Q9NWU1-1 ]
UniGenei Hs.55781.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C9H X-ray 1.80 A 39-459 [» ]
2IWY X-ray 2.06 A/B 38-459 [» ]
2IWZ X-ray 1.65 A/B 38-459 [» ]
ProteinModelPortali Q9NWU1.
SMRi Q9NWU1. Positions 38-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120328. 2 interactions.
STRINGi 9606.ENSP00000280701.

PTM databases

PhosphoSitei Q9NWU1.

Polymorphism databases

DMDMi 74753030.

Proteomic databases

MaxQBi Q9NWU1.
PaxDbi Q9NWU1.
PeptideAtlasi Q9NWU1.
PRIDEi Q9NWU1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000280701 ; ENSP00000280701 ; ENSG00000151093 . [Q9NWU1-1 ]
ENST00000420173 ; ENSP00000411303 ; ENSG00000151093 . [Q9NWU1-2 ]
GeneIDi 54995.
KEGGi hsa:54995.
UCSCi uc003cdn.3. human. [Q9NWU1-1 ]
uc010hfh.3. human. [Q9NWU1-2 ]

Organism-specific databases

CTDi 54995.
GeneCardsi GC03P025824.
HGNCi HGNC:26063. OXSM.
HPAi HPA021293.
HPA021300.
HPA021337.
MIMi 610324. gene.
neXtProti NX_Q9NWU1.
PharmGKBi PA142671214.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0304.
HOGENOMi HOG000060166.
HOVERGENi HBG082096.
InParanoidi Q9NWU1.
KOi K09458.
OMAi HAQKRNA.
PhylomeDBi Q9NWU1.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BRENDAi 2.3.1.41. 2681.
SABIO-RK Q9NWU1.

Miscellaneous databases

EvolutionaryTracei Q9NWU1.
GenomeRNAii 54995.
NextBioi 58306.
PROi Q9NWU1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NWU1.
Bgeei Q9NWU1.
CleanExi HS_OXSM.
Genevestigatori Q9NWU1.

Family and domain databases

Gene3Di 3.40.47.10. 2 hits.
InterProi IPR017568. 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 ]
Pfami PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000447. KAS_II. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR03150. fabF. 1 hit.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 110 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