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Protein

Hsp70-Hsp90 organizing protein 2

Gene

HOP2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the association of the molecular chaperones HSP70 and HSP90. Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • chaperone-mediated protein complex assembly Source: UniProtKB
  • response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Hsp70-Hsp90 organizing protein 2
Short name:
AtHop2
Gene namesi
Name:HOP2
Ordered Locus Names:At1g62740
ORF Names:F23N19.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G62740.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • nucleus Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Hsp70-Hsp90 organizing protein 2PRO_0000426702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated.By similarity
Acetylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5XEP2.
PRIDEiQ5XEP2.

PTM databases

iPTMnetiQ5XEP2.

Expressioni

Gene expression databases

GenevisibleiQ5XEP2. AT.

Interactioni

Subunit structurei

Co-chaperone that forms a complex with HSP70 and HSP90 and preproteins (e.g. chloroplast preproteins) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi27793. 1 interaction.
STRINGi3702.AT1G62740.1.

Structurei

3D structure databases

ProteinModelPortaliQ5XEP2.
SMRiQ5XEP2. Positions 3-115, 237-499, 506-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 3534TPR 1Add
BLAST
Repeati37 – 6933TPR 2Add
BLAST
Repeati70 – 10334TPR 3Add
BLAST
Domaini134 – 17340STI1 1Add
BLAST
Repeati243 – 27634TPR 4Add
BLAST
Repeati278 – 31033TPR 5Add
BLAST
Repeati322 – 35534TPR 6Add
BLAST
Repeati382 – 41534TPR 7Add
BLAST
Repeati417 – 44933TPR 8Add
BLAST
Repeati450 – 48334TPR 9Add
BLAST
Domaini520 – 55940STI1 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi240 – 25718Bipartite nuclear localization signalSequence analysisAdd
BLAST

Domaini

The tetratricopeptide repeat (TPR) domain, forming a carboxylate clamp (CC), mediates interaction with the highly conserved 'EEVD' motif at the C-terminal ends of HSP90 and HSP70.By similarity

Sequence similaritiesi

Contains 2 STI1 domains.Curated
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0548. Eukaryota.
ENOG410XTCJ. LUCA.
HOGENOMiHOG000186562.
InParanoidiQ5XEP2.
KOiK09553.
OMAiLDACNEA.
PhylomeDBiQ5XEP2.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 2 hits.
PF13414. TPR_11. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5XEP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEAKAKGN AAFSSGDFNS AVNHFTDAIN LTPTNHVLFS NRSAAHASLN
60 70 80 90 100
HYDEALSDAK KTVELKPDWG KGYSRLGAAH LGLNQFDEAV EAYSKGLEID
110 120 130 140 150
PSNEGLKSGL ADAKASASRS RASAPNPFGD AFQGPEMWSK LTADPSTRGL
160 170 180 190 200
LKQPDFVNMM KEIQRNPSNL NLYLQDQRVM QALGVLLNIQ IRTQQAGDDM
210 220 230 240 250
EIGEEEMAVP SRKEPEVEKK RKPEPEPEPE PEFGEEKQKK LKAQKEKELG
260 270 280 290 300
NAAYKKKDFE TAIQHYSTAM EIDDEDISYI TNRAAVHLEM GKYDECIKDC
310 320 330 340 350
DKAVERGREL RSDYKMVAKA LTRKGTALGK MAKVSKDYEP VIQTYQKALT
360 370 380 390 400
EHRNPETLKR LNEAERAKKE LEQQEYYDPN IGDEEREKGN DFFKEQKYPD
410 420 430 440 450
AVRHYTEAIK RNPKDPRAYS NRAACYTKLG AMPEGLKDAE KCIELDPTFL
460 470 480 490 500
KGYSRKGAVQ FFMKEYDNAM ETYQKGLEHD PNNQELLDGV KRCVQQINKA
510 520 530 540 550
NRGDLTPEEL KERQAKGMQD PEIQNILTDP VMRQVLSDLQ ENPAAAQKHM
560 570
QNPMIMNKIQ KLISSGIVQM K
Length:571
Mass (Da):64,520
Last modified:November 23, 2004 - v1
Checksum:i0AB71C7433DF1CFB
GO

Sequence cautioni

The sequence AAF19538.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti349 – 3491L → I in AAO64147 (PubMed:14593172).Curated
Sequence conflicti349 – 3491L → I in BAF00546 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007190 Genomic DNA. Translation: AAF19538.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33999.1.
BT005735 mRNA. Translation: AAO64147.1.
BT015924 mRNA. Translation: AAU95460.1.
BT020538 mRNA. Translation: AAW70384.1.
AK228637 mRNA. Translation: BAF00546.1.
RefSeqiNP_176461.1. NM_104951.3.
UniGeneiAt.21185.
At.48334.

Genome annotation databases

EnsemblPlantsiAT1G62740.1; AT1G62740.1; AT1G62740.
GeneIDi842572.
GrameneiAT1G62740.1; AT1G62740.1; AT1G62740.
KEGGiath:AT1G62740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007190 Genomic DNA. Translation: AAF19538.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33999.1.
BT005735 mRNA. Translation: AAO64147.1.
BT015924 mRNA. Translation: AAU95460.1.
BT020538 mRNA. Translation: AAW70384.1.
AK228637 mRNA. Translation: BAF00546.1.
RefSeqiNP_176461.1. NM_104951.3.
UniGeneiAt.21185.
At.48334.

3D structure databases

ProteinModelPortaliQ5XEP2.
SMRiQ5XEP2. Positions 3-115, 237-499, 506-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27793. 1 interaction.
STRINGi3702.AT1G62740.1.

PTM databases

iPTMnetiQ5XEP2.

Proteomic databases

PaxDbiQ5XEP2.
PRIDEiQ5XEP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G62740.1; AT1G62740.1; AT1G62740.
GeneIDi842572.
GrameneiAT1G62740.1; AT1G62740.1; AT1G62740.
KEGGiath:AT1G62740.

Organism-specific databases

TAIRiAT1G62740.

Phylogenomic databases

eggNOGiKOG0548. Eukaryota.
ENOG410XTCJ. LUCA.
HOGENOMiHOG000186562.
InParanoidiQ5XEP2.
KOiK09553.
OMAiLDACNEA.
PhylomeDBiQ5XEP2.

Miscellaneous databases

PROiQ5XEP2.

Gene expression databases

GenevisibleiQ5XEP2. AT.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 2 hits.
PF13414. TPR_11. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "Arabidopsis ORF clones."
    Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    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].
    Strain: cv. Columbia.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  7. "In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70."
    Prasad B.D., Goel S., Krishna P.
    PLoS ONE 5:E12761-E12761(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiHSOP2_ARATH
AccessioniPrimary (citable) accession number: Q5XEP2
Secondary accession number(s): Q84TJ2, Q9SI76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: November 23, 2004
Last modified: May 11, 2016
This is version 104 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.