B2RDU6 (B2RDU6_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Mevalonate kinase EMBL ACS13750.1

Submitted name:
Mevalonate kinase (Mevalonic aciduria), isoform CRA_c EMBL EAW97872.1
Submitted name:
Mevalonate kinase 1 EMBL ACS13751.1
Submitted name:
cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA EMBL BAG38043.1

Gene names

Name:	MVK EMBL ACS13750.1
ORF Names:	hCG_40321 EMBL EAW97872.1

Organism

Homo sapiens (Human) EMBL BAG38043.1

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Sequence similarities

Belongs to the GHMP kinase family. RuleBase RU004209

Ontologies

Keywords
Ligand	ATP-binding RuleBase RU003563 Nucleotide-binding
Molecular function	Kinase RuleBase RU003563 EMBL BAG38043.1 Transferase
Gene Ontology (GO)
Biological process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B2RDU6 [UniParc]. Last modified July 1, 2008. Version 1. Checksum: C8F6B629B58CD229	FASTA	396	42,451
	10 20 30 40 50 60 MLSEVLLVSA PGKVILHGEH AVVHGKVALA VSLNLRTFLR LQPHSNGKVD LSLPNIGIKR 70 80 90 100 110 120 AWDVARLQSL DTSFLEQGDV TTPTSEQVEK LKEVAGLPDD CAVTERLAVL AFLYLYLSIC 130 140 150 160 170 180 RKQRALPSLD IVVWSELPPG AGLGSSAAYS VCLAAALLTV CEEIPNPLKD GDCVNRWTKE 190 200 210 220 230 240 DLELINKWAF QGERMIHGNP SGVDNAVSTW GGALRYHQGK ISSLKRSPAL QILLTNTKVP 250 260 270 280 290 300 RNTRALVAGV RNRLLKFPEI VAPLLTSIDA ISLECERVLG EMGEAPAPEQ YLVLEELIDM 310 320 330 340 350 360 NQHHLNALGV GHASLDQLCQ VTRARGLHSK LTGAGGGGCG ITLLKPGLEQ PEVEATKQAL 370 380 390 TSCGFDCLET SIGAPGVSIH SATSLDSRVQ QALDGL

References

[1]	"NEDO functional analysis of protein and research application project." Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T. Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Tissue: Testis EMBL BAG38043.1.
[2]	Stockwell T.B., Busam D.A., Ferriera S.M., Brownley A.N., Strausberg R.L., Kirkness E.F., Rogers Y.-H., Levy S. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: MVK-VI-T EMBL ACS13750.1.
[3]	Mural R.J., Istrail S., Sutton 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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FJ515860 Genomic DNA. Translation: ACS13750.1. FJ515860 Genomic DNA. Translation: ACS13751.1. AK315678 mRNA. Translation: BAG38043.1. CH471054 Genomic DNA. Translation: EAW97872.1.
IPI	IPI00010717.
RefSeq	NP_000422.1. NM_000431.2. NP_001107657.1. NM_001114185.1.
UniGene	Hs.130607.
3D structure databases
ProteinModelPortal	B2RDU6.
SMR	B2RDU6. Positions 2-395.
ModBase	Search...
Protein-protein interaction databases
STRING	B2RDU6.
Proteomic databases
PRIDE	B2RDU6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4598.
KEGG	hsa:4598.
UCSC	uc001tpb.2. human.
Organism-specific databases
CTD	4598.
PharmGKB	PA31331.
Phylogenomic databases
HOVERGEN	HBG000402.
OMA	TVCEEIP.
OrthoDB	EOG4C2H9P.
PhylomeDB	B2RDU6.
Gene expression databases
Bgee	B2RDU6.
Family and domain databases
InterPro	IPR006204. GHMP_kinase. IPR013750. GHMP_kinase_C. IPR006203. GHMP_knse_ATP-bd_CS. IPR006205. Mev_gal_kin. IPR006206. Mevalonate/galactokinase. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. [Graphical view]
Gene3D	G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
KO	K00869.
Pfam	PF08544. GHMP_kinases_C. 1 hit. PF00288. GHMP_kinases_N. 1 hit. [Graphical view]
PRINTS	PR00959. MEVGALKINASE.
SUPFAM	SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMs	TIGR00549. Mevalon_kin. 1 hit.
PROSITE	PS00627. GHMP_KINASES_ATP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	17680.

Entry information

Entry name

B2RDU6_HUMAN

Accession

Primary (citable) accession number: B2RDU6

Entry history

Integrated into UniProtKB/TrEMBL:	July 1, 2008
Last sequence update:	July 1, 2008
Last modified:	November 16, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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.