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Mascot Search Results
Protein View
ID HSP7C_MOUSE Reviewed; 646 AA. AC P63017; P08109; P12225; Q3U6R0; Q3U764; Q3U7D7; Q3U7E2; Q3U9B4; AC Q3U9G0; Q3UGM0; Q5FWJ6; Q62373; Q62374; Q62375; Q6NZD0; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 15-DEC-2009, entry version 72. DE RecName: Full=Heat shock cognate 71 kDa protein; DE AltName: Full=Heat shock 70 kDa protein 8; GN Name=Hspa8; Synonyms=Hsc70, Hsc73; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88055872; PubMed=3334718; DOI=10.1016/0012-1606(88)90073-5; RA Giebel L.B., Dworniczak B.P., Bautz E.K.F.; RT "Developmental regulation of a constitutively expressed mouse mRNA RT encoding a 72-kDa heat shock-like protein."; RL Dev. Biol. 125:200-207(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129; TISSUE=Mammary gland; RX PubMed=8682318; DOI=10.1016/0378-1119(96)00169-2; RA Soulier S., Vilotte J.-L., L'Huillier P.J., Mercier J.-C.; RT "Developmental regulation of murine integrin beta 1 subunit- and RT Hsc73-encoding genes in mammary gland: sequence of a new mouse Hsc73 RT cDNA."; RL Gene 172:285-289(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX PubMed=10095055; DOI=10.1016/S0167-4781(98)00285-1; RA Hunt C.R., Parsian A.J., Goswami P.C., Kozak C.A.; RT "Characterization and expression of the mouse Hsc70 gene."; RL Biochim. Biophys. Acta 1444:315-325(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2; RC TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, Stomach, Thymus, and RC Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and FVB/N; RC TISSUE=Brain, Embryo, Embryonic germ cell, Eye, and Mammary gland; 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 [6] RP PROTEIN SEQUENCE OF 4-49; 57-71; 77-102; 113-155; 160-188; 221-246; RP 300-319; 326-342; 349-357; 362-384; 424-447; 540-550 AND 584-597, AND RP MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-383; 438-452 AND 580-587. RX MEDLINE=91067440; PubMed=2251119; DOI=10.1093/nar/18.22.6565; RA Liu J., Maxwell E.S.; RT "Mouse U14 snRNA is encoded in an intron of the mouse cognate hsc70 RT heat shock gene."; RL Nucleic Acids Res. 18:6565-6571(1990). RN [8] RP INTERACTION WITH HSPH1. RX PubMed=9675148; DOI=10.1006/bbrc.1998.8979; RA Hatayama T., Yasuda K., Yasuda K.; RT "Association of HSP105 with HSC70 in high molecular mass complexes in RT mouse FM3A cells."; RL Biochem. Biophys. Res. Commun. 248:395-401(1998). RN [9] RP INTERACTION WITH HSPH1. RX PubMed=15292236; DOI=10.1074/jbc.M407947200; RA Yamagishi N., Ishihara K., Hatayama T.; RT "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 RT ATPase activity."; RL J. Biol. Chem. 279:41727-41733(2004). RN [10] RP INTERACTION WITH IRAK1BP1, AND MASS SPECTROMETRY. RX PubMed=17233114; DOI=10.1089/dna.2006.25.704; RA Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.; RT "The disordered amino-terminus of SIMPL interacts with members of the RT 70-kDa heat-shock protein family."; RL DNA Cell Biol. 25:704-714(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-41, AND MASS RP SPECTROMETRY. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). CC -!- FUNCTION: Chaperone. CC -!- SUBUNIT: Identified in a mRNP granule complex, at least composed CC of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, CC HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, CC NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, CC RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with CC PACRG and BAG1 (By similarity). Interacts with HSPH1/HSP105 and CC IRAK1BP1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). Note=Localized in cytoplasmic mRNP granules CC containing untranslated mRNAs. Translocates rapidly from the CC cytoplasm to the nuclei, and especially to the nucleoli, upon heat CC shock (By similarity). CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- INDUCTION: Constitutively synthesized. CC -!- DOMAIN: The N-terminal 1-386 residues constitute the ATPase CC domain, while residues 387-646 form the peptide-binding domain (By CC similarity). CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By CC similarity). CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC -!- SEQUENCE CAUTION: CC Sequence=BAE31508.1; Type=Frameshift; Positions=256, 269; 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; M19141; AAA37869.1; -; mRNA. DR EMBL; U27129; AAC52836.1; -; mRNA. DR EMBL; U73744; AAB18391.1; -; Genomic_DNA. DR EMBL; AK035286; BAC29016.1; -; mRNA. DR EMBL; AK075935; BAC36065.1; -; mRNA. DR EMBL; AK145579; BAE26523.1; -; mRNA. DR EMBL; AK146708; BAE27374.1; -; mRNA. DR EMBL; AK146985; BAE27588.1; -; mRNA. DR EMBL; AK147864; BAE28187.1; -; mRNA. DR EMBL; AK150474; BAE29591.1; -; mRNA. DR EMBL; AK150498; BAE29612.1; -; mRNA. DR EMBL; AK150701; BAE29780.1; -; mRNA. DR EMBL; AK150958; BAE29990.1; -; mRNA. DR EMBL; AK151065; BAE30081.1; -; mRNA. DR EMBL; AK151127; BAE30135.1; -; mRNA. DR EMBL; AK151287; BAE30272.1; -; mRNA. DR EMBL; AK151435; BAE30398.1; -; mRNA. DR EMBL; AK151516; BAE30465.1; -; mRNA. DR EMBL; AK151537; BAE30484.1; -; mRNA. DR EMBL; AK151775; BAE30681.1; -; mRNA. DR EMBL; AK151808; BAE30707.1; -; mRNA. DR EMBL; AK151865; BAE30753.1; -; mRNA. DR EMBL; AK151892; BAE30776.1; -; mRNA. DR EMBL; AK151948; BAE30822.1; -; mRNA. DR EMBL; AK151997; BAE30861.1; -; mRNA. DR EMBL; AK152598; BAE31346.1; -; mRNA. DR EMBL; AK152697; BAE31427.1; -; mRNA. DR EMBL; AK152703; BAE31432.1; -; mRNA. DR EMBL; AK152803; BAE31508.1; ALT_FRAME; mRNA. DR EMBL; AK153032; BAE31664.1; -; mRNA. DR EMBL; AK153834; BAE32204.1; -; mRNA. DR EMBL; AK159479; BAE35116.1; -; mRNA. DR EMBL; AK164000; BAE37581.1; -; mRNA. DR EMBL; AK166643; BAE38912.1; -; mRNA. DR EMBL; AK166721; BAE38970.1; -; mRNA. DR EMBL; AK166767; BAE39005.1; -; mRNA. DR EMBL; AK166776; BAE39012.1; -; mRNA. DR EMBL; AK166808; BAE39036.1; -; mRNA. DR EMBL; AK166830; BAE39053.1; -; mRNA. DR EMBL; AK166846; BAE39065.1; -; mRNA. DR EMBL; AK166861; BAE39076.1; -; mRNA. DR EMBL; AK166873; BAE39084.1; -; mRNA. DR EMBL; AK166908; BAE39109.1; -; mRNA. DR EMBL; AK166910; BAE39111.1; -; mRNA. DR EMBL; AK166913; BAE39113.1; -; mRNA. DR EMBL; AK166933; BAE39127.1; -; mRNA. DR EMBL; AK167043; BAE39211.1; -; mRNA. DR EMBL; AK167121; BAE39269.1; -; mRNA. DR EMBL; AK167122; BAE39270.1; -; mRNA. DR EMBL; AK167134; BAE39280.1; -; mRNA. DR EMBL; AK167163; BAE39304.1; -; mRNA. DR EMBL; AK167218; BAE39344.1; -; mRNA. DR EMBL; AK167229; BAE39353.1; -; mRNA. DR EMBL; AK167845; BAE39865.1; -; mRNA. DR EMBL; AK167910; BAE39917.1; -; mRNA. DR EMBL; AK168492; BAE40379.1; -; mRNA. DR EMBL; AK168519; BAE40398.1; -; mRNA. DR EMBL; AK168542; BAE40419.1; -; mRNA. DR EMBL; AK168711; BAE40553.1; -; mRNA. DR EMBL; AK168750; BAE40590.1; -; mRNA. DR EMBL; AK168776; BAE40612.1; -; mRNA. DR EMBL; AK168887; BAE40704.1; -; mRNA. DR EMBL; AK168934; BAE40745.1; -; mRNA. DR EMBL; AK169093; BAE40876.1; -; mRNA. DR EMBL; AK169179; BAE40957.1; -; mRNA. DR EMBL; AK169236; BAE41004.1; -; mRNA. DR EMBL; AK169293; BAE41049.1; -; mRNA. DR EMBL; BC006722; AAH06722.1; -; mRNA. DR EMBL; BC066191; AAH66191.1; -; mRNA. DR EMBL; BC085486; AAH85486.1; -; mRNA. DR EMBL; BC089322; AAH89322.1; -; mRNA. DR EMBL; BC089457; AAH89457.1; -; mRNA. DR EMBL; BC106193; AAI06194.1; -; mRNA. DR EMBL; X54401; CAA38267.1; -; Genomic_DNA. DR EMBL; X54402; CAA38268.1; -; Genomic_DNA. DR EMBL; X54403; CAA38269.1; -; Genomic_DNA. DR IPI; IPI00323357; -. DR PIR; A45935; A45935. DR PIR; JC4853; JC4853. DR RefSeq; NP_112442.2; -. DR UniGene; Mm.290774; -. DR UniGene; Mm.336743; -. DR UniGene; Mm.351377; -. DR UniGene; Mm.412745; -. DR PDB; 3CQX; X-ray; 2.30 A; A/B=1-381. DR PDBsum; 3CQX; -. DR SMR; P63017; 1-554. DR IntAct; P63017; 8. DR STRING; P63017; -. DR SWISS-2DPAGE; P63017; -. DR REPRODUCTION-2DPAGE; P63017; -. DR REPRODUCTION-2DPAGE; Q6NZD0; -. DR PRIDE; P63017; -. DR Ensembl; ENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656; Mus musculus. DR GeneID; 15481; -. DR KEGG; mmu:15481; -. DR UCSC; uc009ozx.1; mouse. DR CTD; 15481; -. DR MGI; MGI:105384; Hspa8. DR HOVERGEN; P63017; -. DR InParanoid; P63017; -. DR OMA; EKYKADD; -. DR NextBio; 288328; -. DR Bgee; P63017; -. DR CleanEx; MM_HSPA8; -. DR Genevestigator; P63017; -. DR GermOnline; ENSMUSG00000015656; Mus musculus. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR001023; Hsp70. DR InterPro; IPR013126; Hsp_70. DR PANTHER; PTHR19375; Hsp70; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm; KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein; KW Stress response. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 646 Heat shock cognate 71 kDa protein. FT /FTId=PRO_0000078271. FT REGION 186 377 Interaction with BAG1 (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 15 15 Phosphotyrosine. FT MOD_RES 41 41 Phosphotyrosine. FT MOD_RES 88 88 N6-acetyllysine (By similarity). FT MOD_RES 107 107 Phosphotyrosine (By similarity). FT MOD_RES 108 108 N6-acetyllysine (By similarity). FT MOD_RES 113 113 Phosphoserine (By similarity). FT MOD_RES 115 115 Phosphotyrosine (By similarity). FT MOD_RES 120 120 Phosphoserine (By similarity). FT MOD_RES 121 121 Phosphoserine (By similarity). FT MOD_RES 153 153 Phosphoserine (By similarity). FT MOD_RES 246 246 N6-acetyllysine (By similarity). FT MOD_RES 319 319 N6-acetyllysine (By similarity). FT MOD_RES 348 348 N6-acetyllysine (By similarity). FT MOD_RES 477 477 Phosphothreonine (By similarity). FT MOD_RES 512 512 N6-acetyllysine (By similarity). FT MOD_RES 524 524 N6-acetyllysine (By similarity). FT MOD_RES 541 541 Phosphoserine (By similarity). FT MOD_RES 589 589 N6-acetyllysine (By similarity). FT MOD_RES 597 597 N6-acetyllysine (By similarity). FT MOD_RES 601 601 N6-acetyllysine (By similarity). FT MOD_RES 637 637 Phosphoserine (By similarity). FT MOD_RES 638 638 Phosphoserine (By similarity). FT CONFLICT 9 9 I -> V (in Ref. 4; BAE28187). FT CONFLICT 35 35 N -> K (in Ref. 4; BAE30081/BAE30861/ FT BAE30753). FT CONFLICT 268 268 E -> G (in Ref. 4; BAE31432/BAE31346). FT CONFLICT 269 269 R -> G (in Ref. 4; BAE31508). FT CONFLICT 353 353 F -> C (in Ref. 4; BAE31664). FT CONFLICT 428 428 F -> L (in Ref. 1; AAA37869 and 3; FT AAB18391). FT CONFLICT 432 432 S -> Y (in Ref. 4; BAE30707). FT CONFLICT 589 589 K -> E (in Ref. 5; AAH66191). FT CONFLICT 645 645 V -> M (in Ref. 4; BAE30272/BAE31427). FT STRAND 15 17 FT STRAND 37 39 FT STRAND 42 44 FT HELIX 54 57 FT TURN 58 61 FT HELIX 63 65 FT HELIX 70 72 FT HELIX 81 86 FT TURN 87 89 FT STRAND 91 96 FT STRAND 101 106 FT STRAND 111 114 FT HELIX 116 134 FT STRAND 141 146 FT HELIX 152 160 FT STRAND 168 174 FT HELIX 175 182 FT STRAND 193 199 FT STRAND 206 212 FT STRAND 217 223 FT HELIX 232 249 FT HELIX 257 273 FT TURN 274 276 FT STRAND 278 284 FT STRAND 293 298 FT HELIX 299 310 FT HELIX 314 324 FT HELIX 328 330 FT STRAND 333 337 FT HELIX 344 353 FT TURN 365 370 FT HELIX 374 380 SQ SEQUENCE 646 AA; 70871 MW; 03A27B30E6C076ED CRC64; MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
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