Q9HAV7 (GRPE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GrpE protein homolog 1, mitochondrial

Alternative name(s):
HMGE
Mt-GrpE#1

Gene names

Name:	GRPEL1
Synonyms:	GREPEL1

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	217 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	Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
Subunit structure	Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19 By similarity. Binds to HSP70, HSC70 and HSJ1B.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the GrpE family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Chaperone
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein metabolic process Traceable author statement. Source: Reactome protein folding Inferred from electronic annotation. Source: InterPro protein import into mitochondrial matrix Non-traceable author statement. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	adenyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro unfolded protein binding Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion By similarity
	Chain	28 – 217	190	GrpE protein homolog 1, mitochondrial		PRO_0000013049
Amino acid modifications
	Modified residue	215	1	N6-acetyllysine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q9HAV7 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 40499AA3FC7E689E	FASTA	217	24,279
	10 20 30 40 50 60 MAAQCVRLAR RSLPALALSL RPSPRLLCTA TKQKNSGQNL EEDMGQSEQK ADPPATEKTL 70 80 90 100 110 120 LEEKVKLEEQ LKETVEKYKR ALADTENLRQ RSQKLVEEAK LYGIQAFCKD LLEVADVLEK 130 140 150 160 170 180 ATQCVPKEEI KDDNPHLKNL YEGLVMTEVQ IQKVFTKHGL LKLNPVGAKF DPYEHEALFH 190 200 210 TPVEGKEPGT VALVSKVGYK LHGRTLRPAL VGVVKEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Uterus.
[2]	"Identification and characterization of a human mitochondrial homologue of the bacterial co-chaperone GrpE." Choglay A.A., Chapple J.P., Blatch G.L., Cheetham M.E. Gene 267:125-134(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-117, CHARACTERIZATION. Tissue: Brain.
[3]	"Cloning and characterization of a novel human cDNA homology to R.norvegicus stress-inducible chaperone mt-GrpE#1 mRNA." Wan Y.Z., Yu L., Zhang H.L., Fu Q., Jiang J.X., Zhao S.Y. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Testis.
[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-215, 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	AK312882 mRNA. Translation: BAG35730.1. AF298592 mRNA. Translation: AAG31605.1. AF087896 mRNA. Translation: AAP97195.1. AL542571 mRNA. No translation available. CH471131 Genomic DNA. Translation: EAW82371.1. BC024242 mRNA. Translation: AAH24242.1.
IPI	IPI00029557.
RefSeq	NP_079472.1. NM_025196.2.
UniGene	Hs.443723.
3D structure databases
ProteinModelPortal	Q9HAV7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9HAV7. 6 interactions.
MINT	MINT-3069714.
STRING	9606.ENSP00000264954.
PTM databases
PhosphoSite	Q9HAV7.
Polymorphism databases
DMDM	18202951.
Proteomic databases
PaxDb	Q9HAV7.
PeptideAtlas	Q9HAV7.
PRIDE	Q9HAV7.
Protocols and materials databases
DNASU	80273.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264954; ENSP00000264954; ENSG00000109519.
GeneID	80273.
KEGG	hsa:80273.
UCSC	uc003gjy.1. human.
Organism-specific databases
CTD	80273.
GeneCards	GC04M007060.
HGNC	HGNC:19696. GRPEL1.
HPA	HPA036647.
MIM	606173. gene.
neXtProt	NX_Q9HAV7.
PharmGKB	PA134918140.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0576.
HOGENOM	HOG000252083.
HOVERGEN	HBG051846.
InParanoid	Q9HAV7.
KO	K03687.
OMA	EQLKETM.
OrthoDB	EOG437RFZ.
PhylomeDB	Q9HAV7.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9HAV7.
Bgee	Q9HAV7.
CleanEx	HS_GRPEL1.
Genevestigator	Q9HAV7.
GermOnline	ENSG00000109519. Homo sapiens.
Family and domain databases
Gene3D	2.30.22.10. 1 hit. 3.90.20.20. 1 hit.
InterPro	IPR000740. GrpE. IPR013805. GrpE_coiled_coil. IPR009012. GrpE_head. [Graphical view]
PANTHER	PTHR21237. PTHR21237. 1 hit.
Pfam	PF01025. GrpE. 1 hit. [Graphical view]
PRINTS	PR00773. GRPEPROTEIN.
SUPFAM	SSF51064. GrpE_head. 1 hit.
PROSITE	PS01071. GRPE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	80273.
NextBio	70741.
SOURCE	Search...

Entry information

Entry name

GRPE1_HUMAN

Accession

Primary (citable) accession number: Q9HAV7
Secondary accession number(s): B2R783, Q549M6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	July 11, 2001
Last modified:	May 1, 2013
This is version 104 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.