O76031 (CLPX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial

Gene names

Name:

CLPX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	633 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of clpP By similarity.
Subunit structure	Heterodimer of clpP and clpX By similarity.
Subcellular location	Mitochondrion Ref.1.
Tissue specificity	Higher expression in skeletal muscle and heart and to a lesser extent in liver, brain, placenta, lung, kidney and pancreas. Ref.1
Sequence similarities	Belongs to the ClpX chaperone family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: InterPro proteolysis involved in cellular protein catabolic process Inferred from direct assay PubMed 16115876. Source: UniProtKB
Cellular_component	mitochondrial endopeptidase Clp complex Inferred from direct assay PubMed 16115876. Source: UniProtKB mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptidase activator activity Inferred from direct assay PubMed 11923310PubMed 16115876. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 56	56	Mitochondrion Potential
	Chain	57 – 633	577	ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial		PRO_0000005518
Regions
	Zinc finger	105 – 130	26	C4-type
	Nucleotide binding	293 – 300	8	ATP Potential
Amino acid modifications
	Modified residue	437	1	N6-acetyllysine Ref.7
	Modified residue	617	1	Phosphoserine Ref.6
Natural variations
	Natural variant	488	1	I → T. Corresponds to variant rs35754835 [ dbSNP | Ensembl ].		VAR_048826
Experimental info
	Sequence conflict	21	1	L → P in BAF85005. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O76031 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: CF46A6DC0DDBF022	FASTA	633	69,224
	10 20 30 40 50 60 MPSCGACTCG AAAVRLITSS LASAQRGISG GRIHMSVLGR LGTFETQILQ RAPLRSFTET 70 80 90 100 110 120 PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG NQLRCPKCGD LCTHVETFVS 130 140 150 160 170 180 STRFVKCEKC HHFFVVLSEA DSKKSIIKEP ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV 190 200 210 220 230 240 VGQSFAKKVL SVAVYNHYKR IYNNIPANLR QQAEVEKQTS LTPRELEIRR REDEYRFTKL 250 260 270 280 290 300 LQIAGISPHG NALGASMQQQ VNQQIPQEKR GGEVLDSSHD DIKLEKSNIL LLGPTGSGKT 310 320 330 340 350 360 LLAQTLAKCL DVPFAICDCT TLTQAGYVGE DIESVIAKLL QDANYNVEKA QQGIVFLDEV 370 380 390 400 410 420 DKIGSVPGIH QLRDVGGEGV QQGLLKLLEG TIVNVPEKNS RKLRGETVQV DTTNILFVAS 430 440 450 460 470 480 GAFNGLDRII SRRKNEKYLG FGTPSNLGKG RRAAAAADLA NRSGESNTHQ DIEEKDRLLR 490 500 510 520 530 540 HVEARDLIEF GMIPEFVGRL PVVVPLHSLD EKTLVQILTE PRNAVIPQYQ ALFSMDKCEL 550 560 570 580 590 600 NVTEDALKAI ARLALERKTG ARGLRSIMEK LLLEPMFEVP NSDIVCVEVD KEVVEGKKEP 610 620 630 GYIRAPTKES SEEEYDSGVE EEGWPRQADA ANS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human and mouse mitochondrial orthologs of bacterial ClpX." Corydon T.J., Wilsbech M., Jespersgaard C., Andresen B.S., Borglum A.D., Pedersen S., Bolund L., Gregersen N., Bross P. Mamm. Genome 11:899-905(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Skeletal muscle.
[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]. Tissue: Testis.
[3]	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. , 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 [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Brain and Testis.
[5]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-437, MASS SPECTROMETRY.
[8]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ006267 mRNA. Translation: CAA06933.2. AJ276980 , AJ276981, AJ276966, AJ276967, AJ276968, AJ276969, AJ276970, AJ276971, AJ276972, AJ276973, AJ276974, AJ276975, AJ276976, AJ276977 Genomic DNA. Translation: CAC01291.1. AK292316 mRNA. Translation: BAF85005.1. CH471082 Genomic DNA. Translation: EAW77715.1. BC130373 mRNA. Translation: AAI30374.1. BC136487 mRNA. Translation: AAI36488.1.
IPI	IPI00008728.
RefSeq	NP_006651.2. NM_006660.3.
UniGene	Hs.113823.
3D structure databases
ProteinModelPortal	O76031.
ModBase	Search...
Protein-protein interaction databases
IntAct	O76031. 10 interactions.
MINT	MINT-3002168.
STRING	9606.ENSP00000300107.
PTM databases
PhosphoSite	O76031.
Proteomic databases
PaxDb	O76031.
PeptideAtlas	O76031.
PRIDE	O76031.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000300107; ENSP00000300107; ENSG00000166855.
GeneID	10845.
KEGG	hsa:10845.
UCSC	uc002aom.3. human.
Organism-specific databases
CTD	10845.
GeneCards	GC15M065440.
HGNC	HGNC:2088. CLPX.
HPA	HPA040262.
neXtProt	NX_O76031.
PharmGKB	PA26614.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1219.
HOGENOM	HOG000010093.
HOVERGEN	HBG004940.
InParanoid	O76031.
KO	K03544.
OMA	KSIIKEP.
OrthoDB	EOG46DM2G.
PhylomeDB	O76031.
Gene expression databases
ArrayExpress	O76031.
Bgee	O76031.
CleanEx	HS_CLPX.
Genevestigator	O76031.
GermOnline	ENSG00000166855. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR013093. ATPase_AAA-2. IPR019489. Clp_ATPase_C. IPR004487. Clp_protease_ATP-bd_su_ClpX. IPR027417. P-loop_NTPase. [Graphical view]
PANTHER	PTHR11262:SF4. PTHR11262:SF4. 1 hit.
Pfam	PF07724. AAA_2. 1 hit. PF10431. ClpB_D2-small. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. SM01086. ClpB_D2-small. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00382. clpX. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10845.
NextBio	41174.

Entry information

Entry name

CLPX_HUMAN

Accession

Primary (citable) accession number: O76031
Secondary accession number(s): A1L428 , A8K8F1, B9EGI8, Q9H4D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 11, 2001
Last modified:	May 29, 2013
This is version 112 of the entry and version 2 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.