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Protein

ATPase inhibitor, mitochondrial

Gene

ATPIF1

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

Functioni

Endogenous F1F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F1F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F1F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.4 Publications

GO - Molecular functioni

  • angiostatin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • ATPase inhibitor activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • enzyme inhibitor activity Source: ProtInc
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • erythrocyte differentiation Source: UniProtKB
  • generation of precursor metabolites and energy Source: ProtInc
  • heme biosynthetic process Source: UniProtKB
  • mitochondrial depolarization Source: ParkinsonsUK-UCL
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • negative regulation of ATPase activity Source: ParkinsonsUK-UCL
  • negative regulation of endothelial cell proliferation Source: UniProtKB
  • negative regulation of hydrolase activity Source: UniProtKB
  • positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: Ensembl
  • positive regulation of proteolysis involved in cellular protein catabolic process Source: ParkinsonsUK-UCL
  • protein homooligomerization Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • reactive oxygen species metabolic process Source: Ensembl
  • regulation of ATP metabolic process Source: ParkinsonsUK-UCL
  • regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase inhibitor, mitochondrial
Alternative name(s):
Inhibitor of F(1)F(o)-ATPase
Short name:
IF(1)
Short name:
IF1
Gene namesi
Name:ATPIF1
Synonyms:ATPI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:871. ATPIF1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25173.

Polymorphism and mutation databases

BioMutaiATPIF1.
DMDMi12585262.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionCombined sources1 PublicationAdd
BLAST
Chaini26 – 10681ATPase inhibitor, mitochondrialPRO_0000002547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031N6-succinyllysineBy similarity

Post-translational modificationi

Exhibits variability in chain length, mitochondria have distinct pools of protein cleaved after the 24th, 25th, and 26th amino acid.

Proteomic databases

EPDiQ9UII2.
MaxQBiQ9UII2.
PaxDbiQ9UII2.
PRIDEiQ9UII2.
TopDownProteomicsiQ9UII2-1. [Q9UII2-1]
Q9UII2-2. [Q9UII2-2]

PTM databases

iPTMnetiQ9UII2.
PhosphoSiteiQ9UII2.

Expressioni

Gene expression databases

BgeeiQ9UII2.
CleanExiHS_ATPIF1.
ExpressionAtlasiQ9UII2. baseline and differential.
GenevisibleiQ9UII2. HS.

Organism-specific databases

HPAiHPA027999.

Interactioni

Subunit structurei

Homodimer; represents the active form and is present at a pH value below 6.5. Homotetramer; represents the inactive form and is present at a pH value above 7.0 (By similarity).By similarity

GO - Molecular functioni

  • angiostatin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi125063. 20 interactions.
IntActiQ9UII2. 13 interactions.
MINTiMINT-1374677.
STRINGi9606.ENSP00000335203.

Structurei

3D structure databases

ProteinModelPortaliQ9UII2.
SMRiQ9UII2. Positions 45-103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 5227N-terminal inhibitory regionBy similarityAdd
BLAST
Regioni74 – 10633Antiparallel alpha-helical coiled coil regionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili63 – 10644Sequence analysisAdd
BLAST

Domaini

Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 74-106, leaving each N-terminal inhibitory region (residues 26-52) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 26-52) binds the alpha(ADP-bound)-beta(ADP-bound) (ATP5A1-ATP5B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5C1). This dimeric state is favored by pH values below 7.0, and at higher values the dimers associate to form inactive homotetramer, where the inhibitory region is occluded, masking its inhibitory activity (By similarity).By similarity

Sequence similaritiesi

Belongs to the ATPase inhibitor family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiENOG410J2TJ. Eukaryota.
ENOG41127Z5. LUCA.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiQ9UII2.
OMAiHHEDEIS.
OrthoDBiEOG7TQV31.
PhylomeDBiQ9UII2.
TreeFamiTF320659.

Family and domain databases

InterProiIPR007648. ATPase_inhibitor_mt.
[Graphical view]
PfamiPF04568. IATP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UII2-1) [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
MAVTALAART WLGVWGVRTM QARGFGSDQS ENVDRGAGSI REAGGAFGKR
60 70 80 90 100
EQAEEERYFR AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK

MLKHDD
Length:106
Mass (Da):12,249
Last modified:May 1, 2000 - v1
Checksum:iA6144431125D5A86
GO
Isoform 2 (identifier: Q9UII2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-106: AQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD → HYRLCFEISLG

Show »
Length:71
Mass (Da):7,912
Checksum:iD7E481A83975E005
GO
Isoform 3 (identifier: Q9UII2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-106: Missing.

Show »
Length:60
Mass (Da):6,592
Checksum:i151FBFCD72F13D1C
GO

Sequence cautioni

The sequence AAH04955.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601R → RR in CAI46227 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei61 – 10646AQSRE…LKHDD → HYRLCFEISLG in isoform 2. 1 PublicationVSP_041417Add
BLAST
Alternative sequencei61 – 10646Missing in isoform 3. 1 PublicationVSP_041418Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029042 mRNA. Translation: BAA88422.1.
AK316600 mRNA. Translation: BAG38187.1.
DB030607 mRNA. No translation available.
AL050386 mRNA. Translation: CAI46227.1.
AF114836 mRNA. Translation: AAP97235.1.
AY005470 Genomic DNA. Translation: AAF97495.1.
AL583540 mRNA. No translation available.
BT009849 mRNA. Translation: AAP88851.1.
CR457097 mRNA. Translation: CAG33378.1.
AL353622 Genomic DNA. Translation: CAI19134.1.
CH471059 Genomic DNA. Translation: EAX07704.1.
BC004955 mRNA. Translation: AAH04955.1. Different initiation.
BC009677 mRNA. Translation: AAH09677.1.
CCDSiCCDS319.1. [Q9UII2-1]
CCDS320.1. [Q9UII2-2]
CCDS44096.1. [Q9UII2-3]
PIRiJC7175.
RefSeqiNP_057395.1. NM_016311.4. [Q9UII2-1]
NP_835497.1. NM_178190.2. [Q9UII2-2]
NP_835498.1. NM_178191.2. [Q9UII2-3]
UniGeneiHs.744914.

Genome annotation databases

EnsembliENST00000335514; ENSP00000335203; ENSG00000130770. [Q9UII2-1]
ENST00000465645; ENSP00000437337; ENSG00000130770. [Q9UII2-3]
ENST00000497986; ENSP00000435579; ENSG00000130770. [Q9UII2-2]
GeneIDi93974.
KEGGihsa:93974.
UCSCiuc001bpp.4. human. [Q9UII2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029042 mRNA. Translation: BAA88422.1.
AK316600 mRNA. Translation: BAG38187.1.
DB030607 mRNA. No translation available.
AL050386 mRNA. Translation: CAI46227.1.
AF114836 mRNA. Translation: AAP97235.1.
AY005470 Genomic DNA. Translation: AAF97495.1.
AL583540 mRNA. No translation available.
BT009849 mRNA. Translation: AAP88851.1.
CR457097 mRNA. Translation: CAG33378.1.
AL353622 Genomic DNA. Translation: CAI19134.1.
CH471059 Genomic DNA. Translation: EAX07704.1.
BC004955 mRNA. Translation: AAH04955.1. Different initiation.
BC009677 mRNA. Translation: AAH09677.1.
CCDSiCCDS319.1. [Q9UII2-1]
CCDS320.1. [Q9UII2-2]
CCDS44096.1. [Q9UII2-3]
PIRiJC7175.
RefSeqiNP_057395.1. NM_016311.4. [Q9UII2-1]
NP_835497.1. NM_178190.2. [Q9UII2-2]
NP_835498.1. NM_178191.2. [Q9UII2-3]
UniGeneiHs.744914.

3D structure databases

ProteinModelPortaliQ9UII2.
SMRiQ9UII2. Positions 45-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125063. 20 interactions.
IntActiQ9UII2. 13 interactions.
MINTiMINT-1374677.
STRINGi9606.ENSP00000335203.

PTM databases

iPTMnetiQ9UII2.
PhosphoSiteiQ9UII2.

Polymorphism and mutation databases

BioMutaiATPIF1.
DMDMi12585262.

Proteomic databases

EPDiQ9UII2.
MaxQBiQ9UII2.
PaxDbiQ9UII2.
PRIDEiQ9UII2.
TopDownProteomicsiQ9UII2-1. [Q9UII2-1]
Q9UII2-2. [Q9UII2-2]

Protocols and materials databases

DNASUi93974.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335514; ENSP00000335203; ENSG00000130770. [Q9UII2-1]
ENST00000465645; ENSP00000437337; ENSG00000130770. [Q9UII2-3]
ENST00000497986; ENSP00000435579; ENSG00000130770. [Q9UII2-2]
GeneIDi93974.
KEGGihsa:93974.
UCSCiuc001bpp.4. human. [Q9UII2-1]

Organism-specific databases

CTDi93974.
GeneCardsiATPIF1.
HGNCiHGNC:871. ATPIF1.
HPAiHPA027999.
MIMi614981. gene.
neXtProtiNX_Q9UII2.
PharmGKBiPA25173.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J2TJ. Eukaryota.
ENOG41127Z5. LUCA.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiQ9UII2.
OMAiHHEDEIS.
OrthoDBiEOG7TQV31.
PhylomeDBiQ9UII2.
TreeFamiTF320659.

Miscellaneous databases

ChiTaRSiATPIF1. human.
GeneWikiiATPIF1.
GenomeRNAii93974.
NextBioi78232.
PROiQ9UII2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UII2.
CleanExiHS_ATPIF1.
ExpressionAtlasiQ9UII2. baseline and differential.
GenevisibleiQ9UII2. HS.

Family and domain databases

InterProiIPR007648. ATPase_inhibitor_mt.
[Graphical view]
PfamiPF04568. IATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of cDNA coding the mitochondrial precursor protein of the ATPase inhibitor from humans."
    Ichikawa N., Ushida S., Kawabata M., Masazumi Y.
    Biosci. Biotechnol. Biochem. 63:2225-2227(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  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] (ISOFORMS 1 AND 3).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Cloning and sequencing of a novel human cDNA homologous to bovine ATP synthase inhibitor protein mRNA."
    Dai F.Y., Yu L., Yang J., Zheng L.H., Wang X.K., Zhao S.Y.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Cloning and characterization of a novel human gene ASI."
    Yu L., Zhang P., Gao J.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  6. Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fetal liver.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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: Lung and Uterus.
  12. "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 26-42, VARIABILITY IN MATURE CHAIN LENGTH.
    Tissue: Leukemic T-cell.
  13. "A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies."
    Aggeler R., Coons J., Taylor S.W., Ghosh S.S., Garcia J.J., Capaldi R.A., Marusich M.F.
    J. Biol. Chem. 277:33906-33912(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "An Inhibitor of the F1 subunit of ATP synthase (IF1) modulates the activity of angiostatin on the endothelial cell surface."
    Burwick N.R., Wahl M.L., Fang J., Zhong Z., Moser T.L., Li B., Capaldi R.A., Kenan D.J., Pizzo S.V.
    J. Biol. Chem. 280:1740-1745(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: FUNCTION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: FUNCTION.
  19. Cited for: CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER PHE-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATIF1_HUMAN
AccessioniPrimary (citable) accession number: Q9UII2
Secondary accession number(s): Q5JXL8, Q6IAQ7, Q9BSL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: April 13, 2016
This is version 136 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.