Full text data of HSPA4
HSPA4
(APG2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Heat shock 70 kDa protein 4 (HSP70RY; Heat shock 70-related protein APG-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heat shock 70 kDa protein 4 (HSP70RY; Heat shock 70-related protein APG-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00002966
IPI00002966 Heat shock 70 kDa protein 4 response to unfolded proteins, lymphoctytes, ATP binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00002966 Heat shock 70 kDa protein 4 response to unfolded proteins, lymphoctytes, ATP binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P34932
ID HSP74_HUMAN Reviewed; 840 AA.
AC P34932; O95756; Q2TAL4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 4.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Heat shock 70 kDa protein 4;
DE AltName: Full=HSP70RY;
DE AltName: Full=Heat shock 70-related protein APG-2;
GN Name=HSPA4; Synonyms=APG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nonoguchi K., Fujita J.;
RT "Cloning and characterization of human apg-1 and apg-2, members of the
RT hsp110 family, cDNAs and chromosomal assignment of the genes.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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].
RC TISSUE=Brain, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-749.
RC TISSUE=Lymphocyte;
RX PubMed=8335910;
RA Fathallah D.M., Cherif D., Dellagi K., Arnaout M.A.;
RT "Molecular cloning of a novel human hsp70 from a B cell line and its
RT assignment to chromosome 5.";
RL J. Immunol. 151:810-813(1993).
RN [5]
RP PROTEIN SEQUENCE OF 20-33; 111-124; 170-185; 222-234; 333-346; 361-374
RP AND 391-422, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-336, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538, AND MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND TYR-336, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430 AND LYS-679, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-546, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBUNIT: Interacts with TJP1/ZO-1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA02807.1; Type=Frameshift; Positions=567, 586, 697, 715, 722;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB023420; BAA75062.1; -; mRNA.
DR EMBL; AC113410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110861; AAI10862.1; -; mRNA.
DR EMBL; BC126122; AAI26123.1; -; mRNA.
DR EMBL; BC126124; AAI26125.1; -; mRNA.
DR EMBL; L12723; AAA02807.1; ALT_FRAME; mRNA.
DR PIR; I56208; I56208.
DR RefSeq; NP_002145.3; NM_002154.3.
DR UniGene; Hs.90093; -.
DR ProteinModelPortal; P34932; -.
DR SMR; P34932; 5-697.
DR DIP; DIP-460N; -.
DR IntAct; P34932; 19.
DR MINT; MINT-1159519; -.
DR STRING; 9606.ENSP00000302961; -.
DR PhosphoSite; P34932; -.
DR DMDM; 206729934; -.
DR DOSAC-COBS-2DPAGE; P34932; -.
DR REPRODUCTION-2DPAGE; IPI00002966; -.
DR REPRODUCTION-2DPAGE; P34932; -.
DR PaxDb; P34932; -.
DR PRIDE; P34932; -.
DR DNASU; 3308; -.
DR Ensembl; ENST00000304858; ENSP00000302961; ENSG00000170606.
DR GeneID; 3308; -.
DR KEGG; hsa:3308; -.
DR UCSC; uc003kyj.3; human.
DR CTD; 3308; -.
DR GeneCards; GC05P132415; -.
DR HGNC; HGNC:5237; HSPA4.
DR HPA; CAB025529; -.
DR HPA; HPA010023; -.
DR MIM; 601113; gene.
DR neXtProt; NX_P34932; -.
DR PharmGKB; PA29503; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228138; -.
DR HOVERGEN; HBG047955; -.
DR InParanoid; P34932; -.
DR KO; K09489; -.
DR OMA; KVKYMEE; -.
DR OrthoDB; EOG77M8N0; -.
DR PhylomeDB; P34932; -.
DR ChiTaRS; HSPA4; human.
DR GeneWiki; HSPA4; -.
DR GenomeRNAi; 3308; -.
DR NextBio; 13119; -.
DR PRO; PR:P34932; -.
DR ArrayExpress; P34932; -.
DR Bgee; P34932; -.
DR CleanEx; HS_HSPA4; -.
DR Genevestigator; P34932; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:BHF-UCL.
DR GO; GO:0045040; P:protein import into mitochondrial outer membrane; IDA:BHF-UCL.
DR GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1 840 Heat shock 70 kDa protein 4.
FT /FTId=PRO_0000078262.
FT MOD_RES 76 76 Phosphoserine.
FT MOD_RES 89 89 Phosphotyrosine.
FT MOD_RES 336 336 Phosphotyrosine.
FT MOD_RES 430 430 N6-acetyllysine.
FT MOD_RES 538 538 Phosphothreonine.
FT MOD_RES 546 546 Phosphoserine.
FT MOD_RES 660 660 Phosphotyrosine (By similarity).
FT MOD_RES 679 679 N6-acetyllysine.
FT CONFLICT 94 94 L -> W (in Ref. 4; AAA02807).
FT CONFLICT 190 190 A -> R (in Ref. 4; AAA02807).
FT CONFLICT 583 586 NQLL -> ESAI (in Ref. 4; AAA02807).
FT CONFLICT 622 622 E -> R (in Ref. 1; BAA75062).
FT CONFLICT 644 644 D -> G (in Ref. 1; BAA75062).
FT CONFLICT 746 749 NNKL -> EVTP (in Ref. 4; AAA02807).
SQ SEQUENCE 840 AA; 94331 MW; 8B690A52A0729C2A CRC64;
MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA AAKSQVISNA
KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVTYMEEER NFTTEQVTAM
LLSKLKETAE SVLKKPVVDC VVSVPCFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL
VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT
MNRGKFLEMC NDLLARVEPP LRSVLEQTKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGSSDCEVF
SKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
KVRVNVHGIF SVSSASLVEV HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA
ENKAESEEME TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN
EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL KLEDTENWLY
EDGEDQPKQV YVDKLAELKN LGQPIKIRFQ ESEERPKLFE ELGKQIQQYM KIISSFKNKE
DQYDHLDAAD MTKVEKSTNE AMEWMNNKLN LQNKQSLTMD PVVKSKEIEA KIKELTSTCS
PIISKPKPKV EPPKEEQKNA EQNGPVDGQG DNPGPQAAEQ GTDTAVPSDS DKKLPEMDID
//
ID HSP74_HUMAN Reviewed; 840 AA.
AC P34932; O95756; Q2TAL4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 4.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Heat shock 70 kDa protein 4;
DE AltName: Full=HSP70RY;
DE AltName: Full=Heat shock 70-related protein APG-2;
GN Name=HSPA4; Synonyms=APG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nonoguchi K., Fujita J.;
RT "Cloning and characterization of human apg-1 and apg-2, members of the
RT hsp110 family, cDNAs and chromosomal assignment of the genes.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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].
RC TISSUE=Brain, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-749.
RC TISSUE=Lymphocyte;
RX PubMed=8335910;
RA Fathallah D.M., Cherif D., Dellagi K., Arnaout M.A.;
RT "Molecular cloning of a novel human hsp70 from a B cell line and its
RT assignment to chromosome 5.";
RL J. Immunol. 151:810-813(1993).
RN [5]
RP PROTEIN SEQUENCE OF 20-33; 111-124; 170-185; 222-234; 333-346; 361-374
RP AND 391-422, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-336, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538, AND MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND TYR-336, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430 AND LYS-679, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-546, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBUNIT: Interacts with TJP1/ZO-1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA02807.1; Type=Frameshift; Positions=567, 586, 697, 715, 722;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB023420; BAA75062.1; -; mRNA.
DR EMBL; AC113410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110861; AAI10862.1; -; mRNA.
DR EMBL; BC126122; AAI26123.1; -; mRNA.
DR EMBL; BC126124; AAI26125.1; -; mRNA.
DR EMBL; L12723; AAA02807.1; ALT_FRAME; mRNA.
DR PIR; I56208; I56208.
DR RefSeq; NP_002145.3; NM_002154.3.
DR UniGene; Hs.90093; -.
DR ProteinModelPortal; P34932; -.
DR SMR; P34932; 5-697.
DR DIP; DIP-460N; -.
DR IntAct; P34932; 19.
DR MINT; MINT-1159519; -.
DR STRING; 9606.ENSP00000302961; -.
DR PhosphoSite; P34932; -.
DR DMDM; 206729934; -.
DR DOSAC-COBS-2DPAGE; P34932; -.
DR REPRODUCTION-2DPAGE; IPI00002966; -.
DR REPRODUCTION-2DPAGE; P34932; -.
DR PaxDb; P34932; -.
DR PRIDE; P34932; -.
DR DNASU; 3308; -.
DR Ensembl; ENST00000304858; ENSP00000302961; ENSG00000170606.
DR GeneID; 3308; -.
DR KEGG; hsa:3308; -.
DR UCSC; uc003kyj.3; human.
DR CTD; 3308; -.
DR GeneCards; GC05P132415; -.
DR HGNC; HGNC:5237; HSPA4.
DR HPA; CAB025529; -.
DR HPA; HPA010023; -.
DR MIM; 601113; gene.
DR neXtProt; NX_P34932; -.
DR PharmGKB; PA29503; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228138; -.
DR HOVERGEN; HBG047955; -.
DR InParanoid; P34932; -.
DR KO; K09489; -.
DR OMA; KVKYMEE; -.
DR OrthoDB; EOG77M8N0; -.
DR PhylomeDB; P34932; -.
DR ChiTaRS; HSPA4; human.
DR GeneWiki; HSPA4; -.
DR GenomeRNAi; 3308; -.
DR NextBio; 13119; -.
DR PRO; PR:P34932; -.
DR ArrayExpress; P34932; -.
DR Bgee; P34932; -.
DR CleanEx; HS_HSPA4; -.
DR Genevestigator; P34932; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:BHF-UCL.
DR GO; GO:0045040; P:protein import into mitochondrial outer membrane; IDA:BHF-UCL.
DR GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1 840 Heat shock 70 kDa protein 4.
FT /FTId=PRO_0000078262.
FT MOD_RES 76 76 Phosphoserine.
FT MOD_RES 89 89 Phosphotyrosine.
FT MOD_RES 336 336 Phosphotyrosine.
FT MOD_RES 430 430 N6-acetyllysine.
FT MOD_RES 538 538 Phosphothreonine.
FT MOD_RES 546 546 Phosphoserine.
FT MOD_RES 660 660 Phosphotyrosine (By similarity).
FT MOD_RES 679 679 N6-acetyllysine.
FT CONFLICT 94 94 L -> W (in Ref. 4; AAA02807).
FT CONFLICT 190 190 A -> R (in Ref. 4; AAA02807).
FT CONFLICT 583 586 NQLL -> ESAI (in Ref. 4; AAA02807).
FT CONFLICT 622 622 E -> R (in Ref. 1; BAA75062).
FT CONFLICT 644 644 D -> G (in Ref. 1; BAA75062).
FT CONFLICT 746 749 NNKL -> EVTP (in Ref. 4; AAA02807).
SQ SEQUENCE 840 AA; 94331 MW; 8B690A52A0729C2A CRC64;
MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA AAKSQVISNA
KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVTYMEEER NFTTEQVTAM
LLSKLKETAE SVLKKPVVDC VVSVPCFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL
VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT
MNRGKFLEMC NDLLARVEPP LRSVLEQTKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGSSDCEVF
SKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
KVRVNVHGIF SVSSASLVEV HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA
ENKAESEEME TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN
EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL KLEDTENWLY
EDGEDQPKQV YVDKLAELKN LGQPIKIRFQ ESEERPKLFE ELGKQIQQYM KIISSFKNKE
DQYDHLDAAD MTKVEKSTNE AMEWMNNKLN LQNKQSLTMD PVVKSKEIEA KIKELTSTCS
PIISKPKPKV EPPKEEQKNA EQNGPVDGQG DNPGPQAAEQ GTDTAVPSDS DKKLPEMDID
//
MIM
601113
*RECORD*
*FIELD* NO
601113
*FIELD* TI
*601113 HEAT-SHOCK 70-KD PROTEIN 4; HSPA4
;;HSP70
*FIELD* TX
CLONING
Fathallah et al. (1993) reported the cloning of a human heat-shock
read moreprotein (hsp), which they designated hsp70 RY. The cDNA was isolated
from an EBV-transformed B-cell line from a patient with leukocyte
adhesion molecule deficiency. The predicted 701-amino acid protein has
an N-terminal ATP-binding domain and a C-terminal peptide-binding domain
characteristic of hsp proteins. Northern blot analysis detected a 3.0-kb
RNA in the patient's EBV cell line.
MAPPING
Fathallah et al. (1993) used in situ hybridization to map the HSPA4 gene
to chromosome 5q31.1-q31.2.
*FIELD* RF
1. Fathallah, D. M.; Cherif, D.; Dellagi, K.; Arnaout, M. A.: Molecular
cloning of a novel human hsp70 from a B cell line and its assignment
to chromosome 5. J. Immun. 151: 810-813, 1993. Note: Erratum: J.
Immun. 151: 6616 only, 1993.
*FIELD* CD
Alan F. Scott: 3/10/1996
*FIELD* ED
carol: 11/05/2010
tkritzer: 6/21/2004
psherman: 12/13/1999
psherman: 6/22/1999
terry: 7/24/1998
dholmes: 5/12/1998
terry: 7/9/1997
mark: 3/10/1996
*RECORD*
*FIELD* NO
601113
*FIELD* TI
*601113 HEAT-SHOCK 70-KD PROTEIN 4; HSPA4
;;HSP70
*FIELD* TX
CLONING
Fathallah et al. (1993) reported the cloning of a human heat-shock
read moreprotein (hsp), which they designated hsp70 RY. The cDNA was isolated
from an EBV-transformed B-cell line from a patient with leukocyte
adhesion molecule deficiency. The predicted 701-amino acid protein has
an N-terminal ATP-binding domain and a C-terminal peptide-binding domain
characteristic of hsp proteins. Northern blot analysis detected a 3.0-kb
RNA in the patient's EBV cell line.
MAPPING
Fathallah et al. (1993) used in situ hybridization to map the HSPA4 gene
to chromosome 5q31.1-q31.2.
*FIELD* RF
1. Fathallah, D. M.; Cherif, D.; Dellagi, K.; Arnaout, M. A.: Molecular
cloning of a novel human hsp70 from a B cell line and its assignment
to chromosome 5. J. Immun. 151: 810-813, 1993. Note: Erratum: J.
Immun. 151: 6616 only, 1993.
*FIELD* CD
Alan F. Scott: 3/10/1996
*FIELD* ED
carol: 11/05/2010
tkritzer: 6/21/2004
psherman: 12/13/1999
psherman: 6/22/1999
terry: 7/24/1998
dholmes: 5/12/1998
terry: 7/9/1997
mark: 3/10/1996