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O14561 (ACPM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 117. 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)
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.

Subunit structure

Mammalian complex I is composed of 45 different subunits.

Subcellular location

Mitochondrion.

Sequence similarities

Contains 1 acyl carrier domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Amino acid modifications

Modified residue921N6-acetyllysine Ref.8
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: 9878551] [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: 14702039] [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: 10493829] [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: 15489334] [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: 19892738] [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: 12611891] [Abstract]
Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
[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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, MASS SPECTROMETRY.
[9]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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.
IPIIPI00022442.
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...

Protein-protein interaction databases

IntActO14561. 4 interactions.
STRINGO14561.

PTM databases

PhosphoSiteO14561.

Proteomic databases

PeptideAtlasO14561.
PRIDEO14561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000007516; ENSP00000007516; ENSG00000004779.
GeneID4706.
KEGGhsa:4706.
NMPDRfig|9606.3.peg.11884.
UCSCuc002dlw.1. human.

Organism-specific databases

CTD4706.
GeneCardsGC16M023592.
H-InvDBHIX0202321.
HGNCHGNC:7694. NDUFAB1.
MIM603836. gene.
neXtProtNX_O14561.
PharmGKBPA31500.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08677.
GeneTreeENSGT00390000002127.
HOGENOMHBG755218.
HOVERGENHBG024318.
InParanoidO14561.
OMARVLCACV.
OrthoDBEOG41VK49.
PhylomeDBO14561.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO14561.
BgeeO14561.
CleanExHS_NDUFAB1.
GenevestigatorO14561.
GermOnlineENSG00000004779. Homo sapiens.

Family and domain databases

InterProIPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006163. Phsphopanteth-bd.
IPR006162. PPantetheine_attach_site.
[Graphical view]
Gene3DG3DSA:1.10.1200.10. ACP_like. 1 hit.
KOK03955.
PfamPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47336. ACP_like. 1 hit.
TIGRFAMsTIGR00517. Acyl_carrier. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00157. NADH.
NextBio18148.
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: January 25, 2012
This is version 117 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

Human chromosome 16

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families