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Protein

Hsp90 co-chaperone Cdc37-like 1

Gene

CDC37L1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Hsp90 co-chaperone Cdc37-like 1
Alternative name(s):
Hsp90-associating relative of Cdc37
Gene namesi
Name:CDC37L1
Synonyms:CDC37B, HARC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17179. CDC37L1.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134982210.

Polymorphism and mutation databases

BioMutaiCDC37L1.
DMDMi182705252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Hsp90 co-chaperone Cdc37-like 1PRO_0000318521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7L3B6.
MaxQBiQ7L3B6.
PaxDbiQ7L3B6.
PRIDEiQ7L3B6.

PTM databases

iPTMnetiQ7L3B6.
PhosphoSiteiQ7L3B6.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, placenta and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ7L3B6.
CleanExiHS_CDC37L1.
ExpressionAtlasiQ7L3B6. baseline and differential.
GenevisibleiQ7L3B6. HS.

Organism-specific databases

HPAiHPA021175.

Interactioni

Subunit structurei

Self-associates. Forms complexes with Hsp70 and Hsp90. Interacts with CDC37, FKBP4, PPID and STIP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AA1P079002EBI-2841876,EBI-296047
HSP90AB1P082385EBI-2841876,EBI-352572
HSP90AB1Q6PK502EBI-2841876,EBI-9356629
STIP1P319482EBI-2841876,EBI-1054052

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120796. 27 interactions.
IntActiQ7L3B6. 23 interactions.
STRINGi9606.ENSP00000371278.

Structurei

3D structure databases

ProteinModelPortaliQ7L3B6.
SMRiQ7L3B6. Positions 156-271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 171170Self-associationAdd
BLAST
Regioni147 – 277131Self-association and interaction with Hsp90Add
BLAST
Regioni267 – 33771Interaction with Hsp70Add
BLAST
Regioni278 – 33760Required for interaction with STIP1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili84 – 12239Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the CDC37 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2260. Eukaryota.
ENOG410XTCZ. LUCA.
GeneTreeiENSGT00390000013443.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ7L3B6.
OMAiNMDAISK.
PhylomeDBiQ7L3B6.
TreeFamiTF101059.

Family and domain databases

InterProiIPR004918. Cdc37.
IPR013874. Cdc37_Hsp90-bd.
[Graphical view]
PANTHERiPTHR12800. PTHR12800. 1 hit.
PfamiPF08565. CDC37_M. 1 hit.
[Graphical view]
SMARTiSM01070. CDC37_M. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7L3B6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQPWPPPGP WSLPRAEGEA EEESDFDVFP SSPRCPQLPG GGAQMYSHGI
60 70 80 90 100
ELACQKQKEF VKSSVACKWN LAEAQQKLGS LALHNSESLD QEHAKAQTAV
110 120 130 140 150
SELRQREEEW RQKEEALVQR EKMCLWSTDA ISKDVFNKSF INQDKRKDTE
160 170 180 190 200
DEDKSESFMQ KYEQKIRHFG MLSRWDDSQR FLSDHPYLVC EETAKYLILW
210 220 230 240 250
CFHLEAEKKG ALMEQIAHQA VVMQFIMEMA KNCNVDPRGC FRLFFQKAKA
260 270 280 290 300
EEEGYFEAFK NELEAFKSRV RLYSQSQSFQ PMTVQNHVPH SGVGSIGLLE
310 320 330
SLPQNPDYLQ YSISTALCSL NSVVHKEDDE PKMMDTV
Length:337
Mass (Da):38,835
Last modified:February 5, 2008 - v1
Checksum:i46ACDDCE5D07B587
GO

Sequence cautioni

The sequence BAA91206.1 differs from that shown. Reason: Erroneous termination at position 124. Translated as Cys.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171E → G in BAA91304 (PubMed:14702039).Curated
Sequence conflicti159 – 1591M → V in BAA91206 (PubMed:14702039).Curated
Sequence conflicti305 – 3051N → S in BAA91304 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti291 – 2911S → F.
Corresponds to variant rs7036014 [ dbSNP | Ensembl ].
VAR_038755

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000497 mRNA. Translation: BAA91206.1. Sequence problems.
AK000646 mRNA. Translation: BAA91304.1.
AL136231 Genomic DNA. Translation: CAC12705.1.
CH471071 Genomic DNA. Translation: EAW58782.1.
BC014133 mRNA. Translation: AAH14133.1.
CCDSiCCDS6454.1.
RefSeqiNP_060383.2. NM_017913.3.
UniGeneiHs.666439.

Genome annotation databases

EnsembliENST00000381854; ENSP00000371278; ENSG00000106993.
GeneIDi55664.
KEGGihsa:55664.
UCSCiuc003zio.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000497 mRNA. Translation: BAA91206.1. Sequence problems.
AK000646 mRNA. Translation: BAA91304.1.
AL136231 Genomic DNA. Translation: CAC12705.1.
CH471071 Genomic DNA. Translation: EAW58782.1.
BC014133 mRNA. Translation: AAH14133.1.
CCDSiCCDS6454.1.
RefSeqiNP_060383.2. NM_017913.3.
UniGeneiHs.666439.

3D structure databases

ProteinModelPortaliQ7L3B6.
SMRiQ7L3B6. Positions 156-271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120796. 27 interactions.
IntActiQ7L3B6. 23 interactions.
STRINGi9606.ENSP00000371278.

PTM databases

iPTMnetiQ7L3B6.
PhosphoSiteiQ7L3B6.

Polymorphism and mutation databases

BioMutaiCDC37L1.
DMDMi182705252.

Proteomic databases

EPDiQ7L3B6.
MaxQBiQ7L3B6.
PaxDbiQ7L3B6.
PRIDEiQ7L3B6.

Protocols and materials databases

DNASUi55664.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381854; ENSP00000371278; ENSG00000106993.
GeneIDi55664.
KEGGihsa:55664.
UCSCiuc003zio.4. human.

Organism-specific databases

CTDi55664.
GeneCardsiCDC37L1.
HGNCiHGNC:17179. CDC37L1.
HPAiHPA021175.
MIMi610346. gene.
neXtProtiNX_Q7L3B6.
PharmGKBiPA134982210.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2260. Eukaryota.
ENOG410XTCZ. LUCA.
GeneTreeiENSGT00390000013443.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ7L3B6.
OMAiNMDAISK.
PhylomeDBiQ7L3B6.
TreeFamiTF101059.

Miscellaneous databases

GenomeRNAii55664.
NextBioi60411.
PROiQ7L3B6.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L3B6.
CleanExiHS_CDC37L1.
ExpressionAtlasiQ7L3B6. baseline and differential.
GenevisibleiQ7L3B6. HS.

Family and domain databases

InterProiIPR004918. Cdc37.
IPR013874. Cdc37_Hsp90-bd.
[Graphical view]
PANTHERiPTHR12800. PTHR12800. 1 hit.
PfamiPF08565. CDC37_M. 1 hit.
[Graphical view]
SMARTiSM01070. CDC37_M. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Signet-ring cell carcinoma.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  5. "Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37."
    Scholz G.M., Cartledge K., Hall N.E.
    J. Biol. Chem. 276:30971-30979(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP4; HSP70; HSP90; PPID AND STIP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
  6. "Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37."
    Roiniotis J., Masendycz P., Ho S., Scholz G.M.
    Biochemistry 44:6662-6669(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, INTERACTION WITH CDC37 AND HSP90.
  7. "Importance of the C-terminal domain of harc for binding to hsp70 and hop as well as its response to heat shock."
    Cartledge K., Elsegood C., Roiniotis J., Hamilton J.A., Scholz G.M.
    Biochemistry 46:15144-15152(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, INTERACTION WITH HSP70; HSP90 AND STIP1.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCD37L_HUMAN
AccessioniPrimary (citable) accession number: Q7L3B6
Secondary accession number(s): B1AL70, Q9NWS3, Q9NX16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 5, 2008
Last modified: May 11, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.