SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

F4JMJ1

- HSP7R_ARATH

UniProt

F4JMJ1 - HSP7R_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Heat shock 70 kDa protein 17
Gene
HSP70-17, At4g16660, dl4355w, FCAALL.64
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_187630. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 17
Alternative name(s):
Heat shock protein 70-17
Short name:
AtHsp70-17
Gene namesi
Name:HSP70-17
Ordered Locus Names:At4g16660
ORF Names:dl4355w, FCAALL.64
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G16660.

Subcellular locationi

Endoplasmic reticulum lumen Reviewed prediction

GO - Cellular componenti

  1. Golgi apparatus Source: TAIR
  2. chloroplast Source: TAIR
  3. endoplasmic reticulum Source: TAIR
  4. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  5. vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed prediction
Add
BLAST
Chaini25 – 867843Heat shock 70 kDa protein 17
PRO_0000415435Add
BLAST

Proteomic databases

PRIDEiF4JMJ1.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G16660.1-P.

Structurei

3D structure databases

ProteinModelPortaliF4JMJ1.
SMRiF4JMJ1. Positions 22-734.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi865 – 8673Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000239402.
KOiK09486.
OMAiHFADEFN.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

F4JMJ1-1 [UniParc]FASTAAdd to Basket

« Hide

MGKIFSWLVV LLSLISLVPV PSESAVLSVD LGSEWVKVAV VNLKRGQSPI    50
SVAINEMSKR KSPALVAFQS GDRLLGEEAA GITARYPNKV YSQLRDMVGK 100
PFKHVKDFID SVYLPFDIVE DSRGAVGIKI DDGSTVYSVE ELLAMILGYA 150
SNLAEFHAKI PVKDMVVSVP PYFGQAERRG LIQASQLAGV NVLSLVNEHS 200
GAALQYGIDK DFANGSRHVI FYDMGSSSTY AALVYYSAYS EKEYGKTVSV 250
NQFQVKDVRW DLGLGGQSME MRLVEHFADE FNKQLGNGVD VRKFPKAMAK 300
LKKQVKRTKE ILSANTAAPI SVESLHDDRD FRSTITREKF EELCKDLWER 350
SLTPLKDVLK HSGLKIDDIS AVELIGGATR VPKLQSTIQE FIGKQQLDKH 400
LDADEAIVLG SALHAANLSD GIKLKRRLGI VDGSPYGFLV ELEGPNVKKD 450
ESTKQQLVPR MKKLPSKMFR SFVLDKDFDV SLAYESEGIL PPGTTSPVFA 500
QYSVSGLADA SEKYSSRNLS APIKANLHFS LSRSGILSLD RGDAVIEITE 550
WVDVPKKNVT IDSNTTTSTG NATDENSQEN KEDLQTDAEN STASNTTAEE 600
PAVASLGTEK KLKKRTFRIP LKVVEKTVGP GAPFSKESLA EAKIKLEALD 650
KKDRERRRTA ELKNNLESYI YATKEKLETP EFEKISTQEE RKAFVEKLDE 700
VQDWLYMDGE DANATEFEKR LDSLKAIGSP ISFRSEELTA RPVAIEYARK 750
YLTELKEIIK EWETNKTWLP KEKIDEVSKE AEKVKSWLDK NVAEQEKTSL 800
WSKPVFTSTE VYAKVFTLQD KVTKVNKIPK PKPKIEKVTK TENTTKEEEQ 850
SKSSDEAAKE EESHDEL 867
Length:867
Mass (Da):96,725
Last modified:June 28, 2011 - v1
Checksum:iB62D427C39CAB87A
GO

Sequence cautioni

The sequence CAB46039.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB78708.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti413 – 4131L → I in BAF01805. 1 Publication
Sequence conflicti741 – 7411R → Q in AAK93685. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z97341 Genomic DNA. Translation: CAB46039.1. Sequence problems.
AL161544 Genomic DNA. Translation: CAB78708.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83781.1.
AY051008 mRNA. Translation: AAK93685.1.
AK229980 mRNA. Translation: BAF01805.1.
PIRiE85185.
G71433.
RefSeqiNP_567510.1. NM_117767.3.
UniGeneiAt.22039.

Genome annotation databases

EnsemblPlantsiAT4G16660.1; AT4G16660.1; AT4G16660.
GeneIDi827367.
KEGGiath:AT4G16660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z97341 Genomic DNA. Translation: CAB46039.1 . Sequence problems.
AL161544 Genomic DNA. Translation: CAB78708.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE83781.1 .
AY051008 mRNA. Translation: AAK93685.1 .
AK229980 mRNA. Translation: BAF01805.1 .
PIRi E85185.
G71433.
RefSeqi NP_567510.1. NM_117767.3.
UniGenei At.22039.

3D structure databases

ProteinModelPortali F4JMJ1.
SMRi F4JMJ1. Positions 22-734.
ModBasei Search...

Protein-protein interaction databases

STRINGi 3702.AT4G16660.1-P.

Proteomic databases

PRIDEi F4JMJ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G16660.1 ; AT4G16660.1 ; AT4G16660 .
GeneIDi 827367.
KEGGi ath:AT4G16660.

Organism-specific databases

TAIRi AT4G16660.

Phylogenomic databases

eggNOGi COG0443.
HOGENOMi HOG000239402.
KOi K09486.
OMAi HFADEFN.

Enzyme and pathway databases

Reactomei REACT_187630. XBP1(S) activates chaperone genes.

Miscellaneous databases

PROi F4JMJ1.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100934. SSF100934. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-867.
    Strain: cv. Columbia.
  6. "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana."
    Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.
    Cell Stress Chaperones 6:201-208(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiHSP7R_ARATH
AccessioniPrimary (citable) accession number: F4JMJ1
Secondary accession number(s): O23509, Q0WM51, Q949M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: June 28, 2011
Last modified: September 3, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi