GRPE2_HUMAN
ID GRPE2_HUMAN Reviewed; 225 AA.
AC Q8TAA5; B4DFA6; Q49AJ6;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=GrpE protein homolog 2, mitochondrial;
DE AltName: Full=Mt-GrpE#2;
DE Flags: Precursor;
GN Name=GRPEL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. Seems to control the nucleotide-dependent binding of
CC mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity
CC of mt-HSP70. May also serve to modulate the interconversion of
CC oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Probable component of the PAM complex at least composed of a
CC mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and
CC TIMM14/DNAJC19. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TAA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAA5-2; Sequence=VSP_057020, VSP_057021;
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR EMBL; AK074293; BAB85040.1; -; mRNA.
DR EMBL; AK294005; BAG57367.1; -; mRNA.
DR EMBL; AC131025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036678; AAH36678.1; -; mRNA.
DR EMBL; BC070090; AAH70090.1; -; mRNA.
DR CCDS; CCDS4295.1; -. [Q8TAA5-1]
DR RefSeq; NP_689620.2; NM_152407.3. [Q8TAA5-1]
DR AlphaFoldDB; Q8TAA5; -.
DR SMR; Q8TAA5; -.
DR BioGRID; 126391; 18.
DR ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
DR ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR CORUM; Q8TAA5; -.
DR IntAct; Q8TAA5; 8.
DR STRING; 9606.ENSP00000329558; -.
DR GlyGen; Q8TAA5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TAA5; -.
DR PhosphoSitePlus; Q8TAA5; -.
DR BioMuta; GRPEL2; -.
DR EPD; Q8TAA5; -.
DR jPOST; Q8TAA5; -.
DR MassIVE; Q8TAA5; -.
DR MaxQB; Q8TAA5; -.
DR PaxDb; Q8TAA5; -.
DR PeptideAtlas; Q8TAA5; -.
DR PRIDE; Q8TAA5; -.
DR ProteomicsDB; 4019; -.
DR ProteomicsDB; 73847; -. [Q8TAA5-1]
DR Antibodypedia; 3037; 122 antibodies from 20 providers.
DR DNASU; 134266; -.
DR Ensembl; ENST00000329271.8; ENSP00000329558.3; ENSG00000164284.15. [Q8TAA5-1]
DR Ensembl; ENST00000416916.2; ENSP00000397302.2; ENSG00000164284.15. [Q8TAA5-2]
DR GeneID; 134266; -.
DR KEGG; hsa:134266; -.
DR MANE-Select; ENST00000329271.8; ENSP00000329558.3; NM_152407.4; NP_689620.2.
DR UCSC; uc003lqj.4; human. [Q8TAA5-1]
DR CTD; 134266; -.
DR DisGeNET; 134266; -.
DR GeneCards; GRPEL2; -.
DR HGNC; HGNC:21060; GRPEL2.
DR HPA; ENSG00000164284; Tissue enriched (esophagus).
DR MIM; 618545; gene.
DR neXtProt; NX_Q8TAA5; -.
DR OpenTargets; ENSG00000164284; -.
DR PharmGKB; PA134885090; -.
DR VEuPathDB; HostDB:ENSG00000164284; -.
DR eggNOG; KOG3003; Eukaryota.
DR GeneTree; ENSGT00390000005589; -.
DR HOGENOM; CLU_057217_0_1_1; -.
DR InParanoid; Q8TAA5; -.
DR OMA; ICHVPAD; -.
DR OrthoDB; 1525208at2759; -.
DR PhylomeDB; Q8TAA5; -.
DR TreeFam; TF105284; -.
DR PathwayCommons; Q8TAA5; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q8TAA5; -.
DR SIGNOR; Q8TAA5; -.
DR BioGRID-ORCS; 134266; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; GRPEL2; human.
DR GenomeRNAi; 134266; -.
DR Pharos; Q8TAA5; Tdark.
DR PRO; PR:Q8TAA5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TAA5; protein.
DR Bgee; ENSG00000164284; Expressed in lower esophagus mucosa and 191 other tissues.
DR ExpressionAtlas; Q8TAA5; baseline and differential.
DR Genevisible; Q8TAA5; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IC:ComplexPortal.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 2.30.22.10; -; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR HAMAP; MF_01151; GrpE; 1.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR PANTHER; PTHR21237; PTHR21237; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF51064; SSF51064; 1.
DR SUPFAM; SSF58014; SSF58014; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 33..225
FT /note="GrpE protein homolog 2, mitochondrial"
FT /id="PRO_0000013052"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 78..122
FT /note="VRYQRAIADCENIRRRTQRCVEDAKIFGIQSFCKDLVEVADILEK -> ESR
FT VSVRTWWRWLTFWRRLQSAFLKNRSLRTKSSLWRRSSEGCCF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057020"
FT VAR_SEQ 123..225
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057021"
SQ SEQUENCE 225 AA; 25431 MW; 8AC63CD9664593FC CRC64;
MAVRSLWAGR LRVQRLLAWS AAWESKGWPL PFSTATQRTA GEDCRSEDPP DELGPPLAER
ALRVKAVKLE KEVQDLTVRY QRAIADCENI RRRTQRCVED AKIFGIQSFC KDLVEVADIL
EKTTECISEE SEPEDQKLTL EKVFRGLLLL EAKLKSVFAK HGLEKLTPIG DKYDPHEHEL
ICHVPAGVGV QPGTVALVRQ DGYKLHGRTI RLARVEVAVE SQRRL
