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O14561 (ACPM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl carrier protein, mitochondrial

Short name=ACP
Alternative name(s):
CI-SDAP
NADH-ubiquinone oxidoreductase 9.6 kDa subunit
Gene names
Name:NDUFAB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain By similarity. HAMAP-Rule MF_01217

Subunit structure

Mammalian complex I is composed of 45 different subunits. Ref.7

Subcellular location

Mitochondrion HAMAP-Rule MF_01217.

Sequence similarities

Contains 1 acyl carrier domain.

Sequence caution

The sequence AAC05814.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processElectron transport
Fatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Respiratory chain
Transport
   Cellular componentMitochondrion
   DomainTransit peptide
   PTMAcetylation
Phosphopantetheine
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular metabolic process

Traceable author statement. Source: Reactome

fatty acid biosynthetic process

Non-traceable author statement PubMed 10234612. Source: UniProtKB

mitochondrial electron transport, NADH to ubiquinone

Non-traceable author statement Ref.1. Source: UniProtKB

protein lipoylation

Inferred from mutant phenotype PubMed 21846720. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial matrix

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial respiratory chain complex I

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process

Non-traceable author statement PubMed 10234612. Source: UniProtKB

NADH dehydrogenase (ubiquinone) activity

Non-traceable author statement Ref.1. Source: UniProtKB

calcium ion binding

Non-traceable author statement PubMed 10234612. Source: UniProtKB

fatty acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6868Mitochondrion Ref.6
Chain69 – 15688Acyl carrier protein, mitochondrial HAMAP-Rule MF_01217
PRO_0000000561

Amino acid modifications

Modified residue881N6-acetyllysine By similarity
Modified residue1121O-(pantetheine 4'-phosphoryl)serine Potential

Experimental info

Sequence conflict1321D → Y in AAH58920. Ref.5

Secondary structure

............. 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O14561 [UniParc].

Last modified July 11, 2002. Version 3.
Checksum: 0FCE3C3EC6D97AE2

FASTA15617,417
        10         20         30         40         50         60 
MASRVLSAYV SRLPAAFAPL PRVRMLAVAR PLSTALCSAG TQTRLGTLQP ALVLAQVPGR 

        70         80         90        100        110        120 
VTQLCRQYSD MPPLTLEGIQ DRVLYVLKLY DKIDPEKLSV NSHFMKDLGL DSLDQVEIIM 

       130        140        150 
AMEDEFGFEI PDIDAEKLMC PQEIVDYIAD KKDVYE 

« Hide

References

« Hide 'large scale' references
[1]"cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed."
Loeffen J.L.C.M., Triepels R.H., van den Heuvel L.P., Schuelke M., Buskens C.A.F., Smeets R.J.P., Trijbels J.M.F., Smeitink J.A.M.
Biochem. Biophys. Res. Commun. 253:415-422(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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].
[3]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Skin.
[6]"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
Xu G., Shin S.B., Jaffrey S.R.
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 69-83.
Tissue: Leukemic T-cell.
[7]"The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification."
Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., Ghosh S.S., Capaldi R.A.
J. Biol. Chem. 278:13619-13622(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Solution structure of RSGI RUH-059, an ACP domain of acyl carrier protein, mitochondrial from human."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 69-156.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087660 mRNA. Translation: AAD23566.1.
AK311877 mRNA. Translation: BAG34818.1.
AC002400 Genomic DNA. Translation: AAC05814.1. Different initiation.
CH471145 Genomic DNA. Translation: EAW55816.1.
BC058920 mRNA. Translation: AAH58920.1.
CCDSCCDS10614.1.
PIRT00741.
RefSeqNP_004994.1. NM_005003.2.
UniGeneHs.189716.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNWNMR-A71-156[»]
ProteinModelPortalO14561.
SMRO14561. Positions 69-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110786. 5 interactions.
IntActO14561. 4 interactions.
STRING9606.ENSP00000007516.

Chemistry

ChEMBLCHEMBL2363065.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteO14561.

Proteomic databases

MaxQBO14561.
PaxDbO14561.
PeptideAtlasO14561.
PRIDEO14561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000007516; ENSP00000007516; ENSG00000004779.
ENST00000570319; ENSP00000458770; ENSG00000004779.
GeneID4706.
KEGGhsa:4706.
UCSCuc002dlw.3. human.

Organism-specific databases

CTD4706.
GeneCardsGC16M023592.
HGNCHGNC:7694. NDUFAB1.
HPAHPA054364.
MIM603836. gene.
neXtProtNX_O14561.
PharmGKBPA31500.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0236.
HOGENOMHOG000178184.
HOVERGENHBG024318.
InParanoidO14561.
KOK03955.
OMATHLCRQY.
OrthoDBEOG77HDGQ.
PhylomeDBO14561.
TreeFamTF314361.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO14561.
BgeeO14561.
CleanExHS_NDUFAB1.
GenevestigatorO14561.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
HAMAPMF_01217. Acyl_carrier.
InterProIPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006162. PPantetheine_attach_site.
[Graphical view]
PfamPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47336. SSF47336. 1 hit.
TIGRFAMsTIGR00517. acyl_carrier. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO14561.
GenomeRNAi4706.
NextBio18148.
PROO14561.
SOURCESearch...

Entry information

Entry nameACPM_HUMAN
AccessionPrimary (citable) accession number: O14561
Secondary accession number(s): B2R4M1, Q9UNV1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 11, 2002
Last modified: July 9, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM