HS12A_HUMAN
ID HS12A_HUMAN Reviewed; 675 AA.
AC O43301;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Heat shock 70 kDa protein 12A;
GN Name=HSPA12A; Synonyms=KIAA0417;
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].
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12552099; DOI=10.1073/pnas.252764399;
RA Han Z., Truong Q.A., Park S., Breslow J.L.;
RT "Two Hsp70 family members expressed in atherosclerotic lesions.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1256-1261(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH SORL1.
RX PubMed=30679749; DOI=10.1038/s41598-018-37336-6;
RA Madsen P., Isaksen T.J., Siupka P., Toth A.E., Nyegaard M., Gustafsen C.,
RA Nielsen M.S.;
RT "HSPA12A targets the cytoplasmic domain and affects the trafficking of the
RT Amyloid Precursor Protein receptor SorLA.";
RL Sci. Rep. 9:611-611(2019).
CC -!- FUNCTION: Adapter protein for SORL1, but not SORT1. Delays SORL1
CC internalization and affects SORL1 subcellular localization.
CC {ECO:0000269|PubMed:30679749}.
CC -!- SUBUNIT: Interacts with SORL1 (via cytosolic C-terminus); this
CC interaction affects SORL1 internalization and subcellular localization.
CC {ECO:0000269|PubMed:30679749}.
CC -!- INTERACTION:
CC O43301; Q96MM6: HSPA12B; NbExp=3; IntAct=EBI-296980, EBI-10291310;
CC O43301; Q92673: SORL1; NbExp=5; IntAct=EBI-296980, EBI-1171329;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K0U4}. Nucleus
CC {ECO:0000250|UniProtKB:Q8K0U4}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC kidney and muscle. {ECO:0000269|PubMed:12552099}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24847.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB007877; BAA24847.1; ALT_INIT; mRNA.
DR CCDS; CCDS41569.1; -.
DR PIR; T00055; T00055.
DR RefSeq; NP_079291.2; NM_025015.2.
DR AlphaFoldDB; O43301; -.
DR SMR; O43301; -.
DR BioGRID; 129226; 104.
DR IntAct; O43301; 29.
DR MINT; O43301; -.
DR STRING; 9606.ENSP00000358211; -.
DR GlyGen; O43301; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O43301; -.
DR PhosphoSitePlus; O43301; -.
DR BioMuta; HSPA12A; -.
DR EPD; O43301; -.
DR jPOST; O43301; -.
DR MassIVE; O43301; -.
DR MaxQB; O43301; -.
DR PaxDb; O43301; -.
DR PeptideAtlas; O43301; -.
DR PRIDE; O43301; -.
DR ProteomicsDB; 48876; -.
DR Antibodypedia; 2201; 105 antibodies from 22 providers.
DR DNASU; 259217; -.
DR Ensembl; ENST00000369209.8; ENSP00000358211.3; ENSG00000165868.16.
DR GeneID; 259217; -.
DR KEGG; hsa:259217; -.
DR MANE-Select; ENST00000369209.8; ENSP00000358211.3; NM_025015.3; NP_079291.2.
DR UCSC; uc001lct.3; human.
DR CTD; 259217; -.
DR DisGeNET; 259217; -.
DR GeneCards; HSPA12A; -.
DR HGNC; HGNC:19022; HSPA12A.
DR HPA; ENSG00000165868; Low tissue specificity.
DR MIM; 610701; gene.
DR neXtProt; NX_O43301; -.
DR OpenTargets; ENSG00000165868; -.
DR PharmGKB; PA38779; -.
DR VEuPathDB; HostDB:ENSG00000165868; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000154551; -.
DR HOGENOM; CLU_009958_5_3_1; -.
DR InParanoid; O43301; -.
DR OMA; TTELCKW; -.
DR PhylomeDB; O43301; -.
DR TreeFam; TF329492; -.
DR PathwayCommons; O43301; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; O43301; -.
DR BioGRID-ORCS; 259217; 6 hits in 1065 CRISPR screens.
DR ChiTaRS; HSPA12A; human.
DR GenomeRNAi; 259217; -.
DR Pharos; O43301; Tbio.
DR PRO; PR:O43301; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O43301; protein.
DR Bgee; ENSG00000165868; Expressed in lateral nuclear group of thalamus and 176 other tissues.
DR ExpressionAtlas; O43301; baseline and differential.
DR Genevisible; O43301; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR026685; HSPA12A.
DR PANTHER; PTHR14187:SF46; PTHR14187:SF46; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..675
FT /note="Heat shock 70 kDa protein 12A"
FT /id="PRO_0000078292"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 675 AA; 74978 MW; 5DF35D68F9D76437 CRC64;
MADKEAGGSD GPRETAPTSA YSSPARSLGD TGITPLSPSH IVNDTDSNVS EQQSFLVVVA
VDFGTTSSGY AYSFTKEPEC IHVMRRWEGG DPGVSNQKTP TTILLTPERK FHSFGYAARD
FYHDLDPNEA KQWLYLEKFK MKLHTTGDLT MDTDLTAANG KKVKALEIFA YALQYFKEQA
LKELSDQAGS EFENSDVRWV ITVPAIWKQP AKQFMRQAAY QAGLASPENS EQLIIALEPE
AASIYCRKLR LHQMIELSSK AAVNGYSGSD TVGAGFTQAK EHIRRNRQSR TFLVENVIGE
IWSELEEGDK YVVVDSGGGT VDLTVHQIRL PEGHLKELYK ATGGPYGSLG VDYEFEKLLY
KIFGEDFIEQ FKIKRPAAWV DLMIAFESRK RAAAPDRTNP LNITLPFSFI DYYKKFRGHS
VEHALRKSNV DFVKWSSQGM LRMSPDAMNA LFKPTIDSII EHLRDLFQKP EVSTVKFLFL
VGGFAEAPLL QQAVQAAFGD QCRIIIPQDV GLTILKGAVL FGLDPAVIKV RRSPLTYGVG
VLNRYVEGKH PPEKLLVKDG TRWCTDVFDK FISADQSVAL GELVKRSYTP AKPSQLVIVI
NIYSSEHDNV SFITDPGVKK CGTLRLDLTG TSGTAVPARR EIQTLMQFGD TEIKATAIDI
ATSKSVKVGI DFLNY
