Q9H477 (RBSK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribokinase
EC=2.7.1.15

Gene names

Name:	RBKS
Synonyms:	RBSK

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + D-ribose = ADP + D-ribose 5-phosphate. Ref.4
Enzyme regulation	Competitively inhibited by phosphonoacetic acid, etidronate, 2-carboxethylphosphonic acid, N-(phosphonomethyl)glycine, N-(phosphonomethyl)iminodiacetic acid and clodronate. Ref.4
Pathway	Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Sequence similarities	Belongs to the carbohydrate kinase pfkB family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	D-ribose metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribokinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 322

322

Ribokinase

PRO_0000080092

Amino acid modifications

Modified residue

160

1

Phosphoserine By similarity

Experimental info

Sequence conflict

101

1

T → A in AAT64917. Ref.2

Secondary structure

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322

Helix Strand Turn

Details...

Beta strand

17 – 21

5

Beta strand

25 – 31

7

Beta strand

41 – 43

3

Beta strand

45 – 52

8

Helix

54 – 64

11

Beta strand

69 – 78

10

Helix

79 – 89

11

Turn

90 – 92

3

Beta strand

98 – 104

7

Beta strand

107 – 113

7

Beta strand

119 – 124

6

Helix

126 – 130

5

Helix

133 – 138

6

Helix

140 – 145

6

Beta strand

147 – 151

5

Beta strand

153 – 155

3

Helix

157 – 169

13

Beta strand

173 – 176

4

Helix

188 – 191

4

Beta strand

194 – 199

6

Helix

200 – 207

8

Helix

214 – 225

12

Turn

226 – 228

3

Beta strand

230 – 235

6

Helix

237 – 239

3

Beta strand

241 – 247

7

Beta strand

252 – 254

3

Helix

267 – 281

15

Helix

287 – 302

16

Beta strand

304 – 306

3

Helix

307 – 310

4

Helix

314 – 316

3

Helix

319 – 321

3

Sequences

	Sequence		Length	Mass (Da)
	Q9H477 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 50D0E7161F33E94B	FASTA	322	34,143
	10 20 30 40 50 60 MAASGEPQRQ WQEEVAAVVV VGSCMTDLVS LTSRLPKTGE TIHGHKFFIG FGGKGANQCV 70 80 90 100 110 120 QAARLGAMTS MVCKVGKDSF GNDYIENLKQ NDISTEFTYQ TKDAATGTAS IIVNNEGQNI 130 140 150 160 170 180 IVIVAGANLL LNTEDLRAAA NVISRAKVMV CQLEITPATS LEALTMARRS GVKTLFNPAP 190 200 210 220 230 240 AIADLDPQFY TLSDVFCCNE SEAEILTGLT VGSAADAGEA ALVLLKRGCQ VVIITLGAEG 250 260 270 280 290 300 CVVLSQTEPE PKHIPTEKVK AVDTTGAGDS FVGALAFYLA YYPNLSLEDM LNRSNFIAAV 310 320 SVQAAGTQSS YPYKKDLPLT LF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Wightman P.J. Thesis (2000), University of Edinburgh, United Kingdom Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and characterization of RBS protein." Li X., Mao Y., Xie Y. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[4]	"Identification and characterization of human ribokinase and comparison of its properties with E. coli ribokinase and human adenosine kinase." Park J., van Koeverden P., Singh B., Gupta R.S. FEBS Lett. 581:3211-3216(2007) [PubMed: 17585908] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
[5]	"Crystal structure of human ribokinase." Structural genomics consortium (SGC) Submitted (JAN-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 11-322.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ404857 mRNA. Translation: CAC12877.1.
AY643715 mRNA. Translation: AAT64917.1.
BC017425 mRNA. Translation: AAH17425.1.

IPI

IPI00005487.

RefSeq

NP_071411.1. NM_022128.1.

UniGene

Hs.11916.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FV7	X-ray	2.10	A/B	11-322	[»]

ProteinModelPortal

Q9H477.

SMR

Q9H477. Positions 15-322.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9H477.

PTM databases

PhosphoSite

Q9H477.

Polymorphism databases

DMDM

20139730.

Proteomic databases

PRIDE

Q9H477.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302188; ENSP00000306817; ENSG00000171174.

GeneID

64080.

KEGG

hsa:64080.

NMPDR

fig|9606.3.peg.17687.

UCSC

uc002rlo.1. human.

Organism-specific databases

CTD

64080.

GeneCards

GC02M028004.

H-InvDB

HIX0019886.

HGNC

HGNC:30325. RBKS.

HPA

HPA019725.
HPA028285.

MIM

611132. gene.

neXtProt

NX_Q9H477.

PharmGKB

PA134951602.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000005743.

HOGENOM

HBG697973.

HOVERGEN

HBG018350.

InParanoid

Q9H477.

OMA

ETLEAPN.

OrthoDB

EOG4W9J4S.

PhylomeDB

Q9H477.

Gene expression databases

ArrayExpress

Q9H477.

Bgee

Q9H477.

Genevestigator

Q9H477.

GermOnline

ENSG00000171174. Homo sapiens.

Family and domain databases

InterPro

IPR011611. Carb/pur_kinase.
IPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011877. D_ribokin_bac.
IPR002139. Ribokinase.
[Graphical view]

KO

K00852.

Pfam

PF00294. PfkB. 1 hit.
[Graphical view]

PRINTS

PR00990. RIBOKINASE.

TIGRFAMs

TIGR02152. D_ribokin_bact. 1 hit.

PROSITE

PS00583. PFKB_KINASES_1. False negative.
PS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

65866.

SOURCE

Search...

Entry information

Entry name

RBSK_HUMAN

Accession

Primary (citable) accession number: Q9H477
Secondary accession number(s): A9UK04

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.