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Protein

Hsc70-interacting protein 1

Gene

HIP

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

One HIP oligomer binds the ATPase domains of at least two Hsc70 molecules dependent on activation of the Hsc70 ATPase by Hsp40. Stabilizes the ADP state of Hsc70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of Hsc70 with various target proteins (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Hsc70-interacting protein 11 Publication
Gene namesi
Name:HIP1 Publication
ORF Names:CG32789
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0260484. HIP.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosol Source: FlyBase
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Hsc70-interacting protein 1PRO_0000393584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiC4NYP8.

PTM databases

iPTMnetiC4NYP8.

Expressioni

Gene expression databases

GenevisibleiC4NYP8. DM.

Interactioni

Subunit structurei

Homotetramer. Interacts with Hsc70 as well as DNAJ homologs and Hsp90 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi57855. 50 interactions.
76808. 1 interaction.
STRINGi7227.FBpp0070575.

Structurei

3D structure databases

ProteinModelPortaliC4NYP8.
SMRiC4NYP8. Positions 90-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati126 – 15934TPR 1Sequence analysisAdd
BLAST
Repeati161 – 19333TPR 2Sequence analysisAdd
BLAST
Repeati195 – 22733TPR 3Sequence analysisAdd
BLAST
Domaini294 – 33643STI1Sequence analysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili239 – 27638Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the FAM10 family.Sequence analysis
Contains 1 STI1 domain.Sequence analysis
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiENOG410IN5Q. Eukaryota.
COG0457. LUCA.
InParanoidiC4NYP8.
KOiK09560.
OrthoDBiEOG77M8P3.
PhylomeDBiC4NYP8.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13414. TPR_11. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C4NYP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFTMQTGDL KKLKYFIDFA LENPTFLNMP QLQFVKDFVE KFGGTVPPGQ
60 70 80 90 100
FNGGSAGGKC PFGGVAGAKA NEPANAPEDS EDEKSLSDPE SDVELDMEGV
110 120 130 140 150
IEADSDPAQP MGNYSKKATE EEVEQASELR AQAASAYGQQ KFDEAIALYT
160 170 180 190 200
KAIELSPGNA LFHAKRGQAF LKLKKPNACI RDCDVALELN SDLAAGYKFR
210 220 230 240 250
GRARRLLGDF ELAAHDLRQA CKLDFDEETD EWLKEVTPNA KKIEQHRLKQ
260 270 280 290 300
ERRQAERKIK ERQRDQRRAR KEQEKHNASS GGSSGEFSGG NPGNGNMSDI
310 320 330 340 350
LGAMSDPEVS AAIQDILSNP GNITKYASNP KIYNLIKKIV PGGDVGAAFG
360 370
QAGEKAGKPS EPKPKKDSAD FVDDGLD
Length:377
Mass (Da):41,037
Last modified:April 20, 2010 - v2
Checksum:iD62D41198348A786
GO

Sequence cautioni

The sequence ACX32977.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051S → N in strain: XCPA112. 1 Publication
Natural varianti227 – 2271E → D in strain: XCPA25. 1 Publication
Natural varianti290 – 2901G → A in strain: XCPA77, XCPA93 and XCPA126. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ686088 Genomic DNA. Translation: ACQ66626.1.
FJ686092 Genomic DNA. Translation: ACQ66627.1.
FJ686093 Genomic DNA. Translation: ACQ66628.1.
FJ686094 Genomic DNA. Translation: ACQ66629.1.
FJ686095 Genomic DNA. Translation: ACQ66630.1.
AE014298 Genomic DNA. Translation: AAN09108.2.
BT099906 mRNA. Translation: ACX32977.1. Different initiation.
RefSeqiNP_001014719.2. NM_001014719.2.
NP_570074.3. NM_130718.5.
NP_726885.1. NM_166988.4.
NP_726886.1. NM_166989.5.
UniGeneiDm.33464.

Genome annotation databases

EnsemblMetazoaiFBtr0070597; FBpp0070572; FBgn0029676.
FBtr0070598; FBpp0070573; FBgn0029676.
FBtr0070600; FBpp0070575; FBgn0260484.
FBtr0333764; FBpp0305905; FBgn0029676.
GeneIDi31335.
318211.
KEGGidme:Dmel_CG2947.
dme:Dmel_CG32789.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ686088 Genomic DNA. Translation: ACQ66626.1.
FJ686092 Genomic DNA. Translation: ACQ66627.1.
FJ686093 Genomic DNA. Translation: ACQ66628.1.
FJ686094 Genomic DNA. Translation: ACQ66629.1.
FJ686095 Genomic DNA. Translation: ACQ66630.1.
AE014298 Genomic DNA. Translation: AAN09108.2.
BT099906 mRNA. Translation: ACX32977.1. Different initiation.
RefSeqiNP_001014719.2. NM_001014719.2.
NP_570074.3. NM_130718.5.
NP_726885.1. NM_166988.4.
NP_726886.1. NM_166989.5.
UniGeneiDm.33464.

3D structure databases

ProteinModelPortaliC4NYP8.
SMRiC4NYP8. Positions 90-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57855. 50 interactions.
76808. 1 interaction.
STRINGi7227.FBpp0070575.

PTM databases

iPTMnetiC4NYP8.

Proteomic databases

PaxDbiC4NYP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070597; FBpp0070572; FBgn0029676.
FBtr0070598; FBpp0070573; FBgn0029676.
FBtr0070600; FBpp0070575; FBgn0260484.
FBtr0333764; FBpp0305905; FBgn0029676.
GeneIDi31335.
318211.
KEGGidme:Dmel_CG2947.
dme:Dmel_CG32789.

Organism-specific databases

CTDi31335.
318211.
FlyBaseiFBgn0260484. HIP.

Phylogenomic databases

eggNOGiENOG410IN5Q. Eukaryota.
COG0457. LUCA.
InParanoidiC4NYP8.
KOiK09560.
OrthoDBiEOG77M8P3.
PhylomeDBiC4NYP8.

Miscellaneous databases

NextBioi773101.
PROiC4NYP8.

Gene expression databases

GenevisibleiC4NYP8. DM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13414. TPR_11. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Duplicate gene evolution toward multiple fates at the Drosophila melanogaster HIP/HIP-Replacement locus."
    Hogan C.C., Bettencourt B.R.
    J. Mol. Evol. 68:337-350(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-105; ASP-227 AND ALA-290.
    Strain: XCPA112Imported, XCPA126Imported, XCPA25Imported, XCPA77Imported and XCPA93Imported.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    Tissue: Embryo.
  5. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiF10A1_DROME
AccessioniPrimary (citable) accession number: C4NYP8
Secondary accession number(s): C0L9I4
, C0L9I8, C9QP24, Q8IRT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: May 11, 2016
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.