Reviewed, UniProtKB/Swiss-Prot Q9BSD7 (CA057_HUMAN)

Names and origin

Protein names

Recommended name:
    Nucleoside-triphosphatase C1orf57
      Short name=NTPase
    EC=3.6.1.15
Alternative name(s):
    Nucleoside triphosphate phosphohydrolase

Gene names

Name:

C1orf57

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency. Ref.5
Catalytic activity	NTP + H2O = NDP + phosphate.
Subunit structure	Monomer. Ref.5
Sequence similarities	Belongs to the THEP1 NTPase family.
Biophysicochemical properties	Kinetic parameters: KM=5 µM for ATP KM=46 µM for ADP KM=4 µM for GTP KM=6 µM for CTP KM=7 µM for TTP

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: EC transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 190

190

Nucleoside-triphosphatase C1orf57

PRO_0000146711

Regions

Nucleotide binding

9 – 16

8

ATP Probable

Nucleotide binding

109 – 116

8

ATP Probable

Amino acid modifications

Modified residue

21

1

N6-acetyllysine Ref.4

Modified residue

165

1

N6-acetyllysine Ref.4

Natural variations

Natural variant

106

1

G → E: dbSNP rs12123482.

VAR_053071

Experimental info

Mutagenesis

114

1

E → T: Reduced activity, especially towards ATP, GTP and TTP. Ref.5

Mutagenesis

116

1

G → H: Reduced activity, especially towards ATP, GTP and TTP. Ref.5

Secondary structure

1

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190

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

15 – 28

14

Beta strand

34 – 37

4

Beta strand

40 – 42

3

Beta strand

45 – 54

10

Beta strand

59 – 64

6

Beta strand

71 – 73

3

Beta strand

76 – 83

8

Helix

85 – 89

5

Turn

90 – 96

7

Beta strand

110 – 112

3

Turn

117 – 121

5

Helix

124 – 134

11

Beta strand

140 – 143

4

Helix

155 – 159

5

Beta strand

164 – 168

5

Beta strand

171 – 173

3

Helix

174 – 176

3

Helix

177 – 185

9

Sequences

	Sequence		Length	Mass (Da)
	Q9BSD7-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: B4B753F95796A210	FASTA	190	20,713
	10 20 30 40 50 60 MARHVFLTGP PGVGKTTLIH KASEVLKSSG VPVDGFYTEE VRQGGRRIGF DVVTLSGTRG 70 80 90 100 110 120 PLSRVGLEPP PGKRECRVGQ YVVDLTSFEQ LALPVLRNAD CSSGPGQRVC VIDEIGKMEL 130 140 150 160 170 180 FSQLFIQAVR QTLSTPGTII LGTIPVPKGK PLALVEEIRN RKDVKVFNVT KENRNHLLPD 190 IVTCVQSSRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Kang L., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"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.
[3]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[4]	"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-21 AND LYS-165, MASS SPECTROMETRY.
[5]	"NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase." Placzek W.J., Almeida M.S., Wuethrich K. J. Mol. Biol. 367:788-801(2007) [PubMed: 17291528] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH THE ATP ANALOG ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLU-114 AND GLY-116.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF416713 mRNA. Translation: AAL16807.1.
BC005102 mRNA. Translation: AAH05102.1.

IPI

IPI00031570.

RefSeq

NP_115700.1.

UniGene

Hs.642715

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I3B	NMR	-	A	2-190	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9BSD7.

Proteomic databases

PeptideAtlas

Q9BSD7.

PRIDE

Q9BSD7.

Genome annotation databases

Ensembl

ENST00000366627; ENSP00000355586; ENSG00000135778; Homo sapiens. [Genome view]
ENST00000366628; ENSP00000355587; ENSG00000135778; Homo sapiens. [Genome view]

GeneID

84284.

KEGG

hsa:84284.

UCSC

uc001hvj.1. human.

Organism-specific databases

CTD

84284.

GeneCards

GC01P231152.

HGNC

HGNC:28204. C1orf57.

PharmGKB

PA142672508.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9BSD7.

OMA

EIGPMEY.

Gene expression databases

ArrayExpress

Q9BSD7.

Bgee

Q9BSD7.

CleanEx

HS_C1orf57.

Genevestigator

Q9BSD7.

GermOnline

ENSG00000135778. Homo sapiens.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR004948. DUF265.
[Graphical view]

Pfam

PF03266. DUF265. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

73894.

Entry information

Entry name

CA057_HUMAN

Accession

Primary (citable) accession number: Q9BSD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.