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Protein

DnaJ homolog subfamily C member 7

Gene

DNAJC7

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

Functioni

Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity).By similarity

GO - Molecular functioni

  • heat shock protein binding Source: UniProtKB

GO - Biological processi

  • cellular response to heat Source: Reactome
  • chaperone cofactor-dependent protein refolding Source: UniProtKB
  • protein folding Source: ProtInc
  • regulation of cellular response to heat Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_264487. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily C member 7
Alternative name(s):
Tetratricopeptide repeat protein 2
Short name:
TPR repeat protein 2
Gene namesi
Name:DNAJC7
Synonyms:TPR2, TTC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12392. DNAJC7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011R → A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-333 and A-409. 1 Publication
Mutagenesisi333 – 3331R → A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-409. 1 Publication
Mutagenesisi409 – 4091H → A: Predominantly nuclear localization. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-333. 2 Publications

Organism-specific databases

PharmGKBiPA27424.

Polymorphism and mutation databases

BioMutaiDNAJC7.
DMDMi46397879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 494493DnaJ homolog subfamily C member 7PRO_0000071058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99615.
PaxDbiQ99615.
PeptideAtlasiQ99615.
PRIDEiQ99615.

PTM databases

PhosphoSiteiQ99615.

Miscellaneous databases

PMAP-CutDBQ99615.

Expressioni

Gene expression databases

BgeeiQ99615.
CleanExiHS_DNAJC7.
ExpressionAtlasiQ99615. baseline and differential.
GenevisibleiQ99615. HS.

Organism-specific databases

HPAiHPA023015.
HPA052395.

Interactioni

Subunit structurei

Associates with complexes containing chaperones HSP70 and HSP90. Interacts with the GAP domain of NF1. Interacts with HSP90AA1. Interacts with HSPA1A/B; the interaction is enhanced by ATP. Interacts with HSP90AB1. Interacts with PGR. Interacts with RAD9A; the interaction is interrupted by UV and heat shock treatments. Interacts with HUS1 and RAD1. Interacts with NR1I3. The DNAJC7-NR1I3 complex may also include HSP90 (By similarity). Interacts with HSPA8.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BAG4O954292EBI-357552,EBI-2949658
vifP125043EBI-357552,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi113117. 38 interactions.
IntActiQ99615. 18 interactions.
MINTiMINT-1143801.

Structurei

3D structure databases

ProteinModelPortaliQ99615.
SMRiQ99615. Positions 27-476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati28 – 6134TPR 1Add
BLAST
Repeati62 – 9534TPR 2Add
BLAST
Repeati96 – 12934TPR 3Add
BLAST
Repeati142 – 17534TPR 4Add
BLAST
Repeati177 – 20933TPR 5Add
BLAST
Repeati210 – 24334TPR 6Add
BLAST
Repeati256 – 28934TPR 7Add
BLAST
Repeati294 – 32734TPR 8Add
BLAST
Repeati328 – 36134TPR 9Add
BLAST
Domaini381 – 45171JPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00760000118947.
HOGENOMiHOG000210360.
HOVERGENiHBG051376.
InParanoidiQ99615.
KOiK09527.
OMAiCFQRVLE.
PhylomeDBiQ99615.
TreeFamiTF105166.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProiIPR001623. DnaJ_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00515. TPR_1. 5 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99615-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAECDVV MAATEPELLD DQEAKREAET FKEQGNAYYA KKDYNEAYNY
60 70 80 90 100
YTKAIDMCPK NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL
110 120 130 140 150
REGKCHLSLG NAMAACRSFQ RALELDHKNA QAQQEFKNAN AVMEYEKIAE
160 170 180 190 200
TDFEKRDFRK VVFCMDRALE FAPACHRFKI LKAECLAMLG RYPEAQSVAS
210 220 230 240 250
DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA PDHEKACIAC
260 270 280 290 300
RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR
310 320 330 340 350
GTVNSKLRKL DDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQYEEAVRD
360 370 380 390 400
YEKVYQTEKT KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA
410 420 430 440 450
YRKRALMHHP DRHSGASAEV QKEEEKKFKE VGEAFTILSD PKKKTRYDSG
460 470 480 490
QDLDEEGMNM GDFDPNNIFK AFFGGPGGFS FEASGPGNFF FQFG
Length:494
Mass (Da):56,441
Last modified:April 13, 2004 - v2
Checksum:i81C60CF71BFE951D
GO
Isoform 2 (identifier: Q99615-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.

Show »
Length:438
Mass (Da):50,097
Checksum:iC1C5BF7A49DF56B0
GO

Sequence cautioni

The sequence AAB36872.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH33772.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti375 – 3751K → R in BX647209 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5656Missing in isoform 2. 2 PublicationsVSP_044279Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK298860 mRNA. Translation: BAG60982.1.
BX647209 mRNA. No translation available.
AC105024 Genomic DNA. No translation available.
AC125257 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60788.1.
BC003601 mRNA. Translation: AAH03601.1.
BC011837 mRNA. Translation: AAH11837.2.
BC033772 mRNA. Translation: AAH33772.1. Different initiation.
U46571 mRNA. Translation: AAB36872.1. Different initiation.
CCDSiCCDS45677.1. [Q99615-1]
CCDS45678.1. [Q99615-2]
RefSeqiNP_001138238.1. NM_001144766.2. [Q99615-2]
NP_003306.3. NM_003315.3. [Q99615-1]
UniGeneiHs.500156.

Genome annotation databases

EnsembliENST00000316603; ENSP00000313311; ENSG00000168259. [Q99615-2]
ENST00000426588; ENSP00000394327; ENSG00000168259. [Q99615-2]
ENST00000457167; ENSP00000406463; ENSG00000168259. [Q99615-1]
GeneIDi7266.
KEGGihsa:7266.
UCSCiuc002hyo.3. human. [Q99615-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK298860 mRNA. Translation: BAG60982.1.
BX647209 mRNA. No translation available.
AC105024 Genomic DNA. No translation available.
AC125257 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60788.1.
BC003601 mRNA. Translation: AAH03601.1.
BC011837 mRNA. Translation: AAH11837.2.
BC033772 mRNA. Translation: AAH33772.1. Different initiation.
U46571 mRNA. Translation: AAB36872.1. Different initiation.
CCDSiCCDS45677.1. [Q99615-1]
CCDS45678.1. [Q99615-2]
RefSeqiNP_001138238.1. NM_001144766.2. [Q99615-2]
NP_003306.3. NM_003315.3. [Q99615-1]
UniGeneiHs.500156.

3D structure databases

ProteinModelPortaliQ99615.
SMRiQ99615. Positions 27-476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113117. 38 interactions.
IntActiQ99615. 18 interactions.
MINTiMINT-1143801.

PTM databases

PhosphoSiteiQ99615.

Polymorphism and mutation databases

BioMutaiDNAJC7.
DMDMi46397879.

Proteomic databases

MaxQBiQ99615.
PaxDbiQ99615.
PeptideAtlasiQ99615.
PRIDEiQ99615.

Protocols and materials databases

DNASUi7266.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316603; ENSP00000313311; ENSG00000168259. [Q99615-2]
ENST00000426588; ENSP00000394327; ENSG00000168259. [Q99615-2]
ENST00000457167; ENSP00000406463; ENSG00000168259. [Q99615-1]
GeneIDi7266.
KEGGihsa:7266.
UCSCiuc002hyo.3. human. [Q99615-1]

Organism-specific databases

CTDi7266.
GeneCardsiGC17M040128.
HGNCiHGNC:12392. DNAJC7.
HPAiHPA023015.
HPA052395.
MIMi601964. gene.
neXtProtiNX_Q99615.
PharmGKBiPA27424.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00760000118947.
HOGENOMiHOG000210360.
HOVERGENiHBG051376.
InParanoidiQ99615.
KOiK09527.
OMAiCFQRVLE.
PhylomeDBiQ99615.
TreeFamiTF105166.

Enzyme and pathway databases

ReactomeiREACT_264487. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

ChiTaRSiDNAJC7. human.
GeneWikiiDNAJC7.
GenomeRNAii7266.
NextBioi28407.
PMAP-CutDBQ99615.
PROiQ99615.
SOURCEiSearch...

Gene expression databases

BgeeiQ99615.
CleanExiHS_DNAJC7.
ExpressionAtlasiQ99615. baseline and differential.
GenevisibleiQ99615. HS.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProiIPR001623. DnaJ_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00515. TPR_1. 5 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 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] (ISOFORM 2).
    Tissue: Salivary gland.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Salivary gland.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Lung and Skin.
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-26; 69-77; 80-90; 138-156; 192-238; 274-291 AND 430-442 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  7. "Identification and characterization of two novel tetratricopeptide repeat-containing genes."
    Murthy A.E., Bernards A., Church D., Wasmuth J., Gusella J.F.
    DNA Cell Biol. 15:727-735(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-494 (ISOFORM 1).
  8. "Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats."
    Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.
    J. Biol. Chem. 274:34425-34432(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPA8.
  9. "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9."
    Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C.
    Biochem. Biophys. Res. Commun. 287:932-940(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD9A; HUS1 AND RAD1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-409.
  10. "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system."
    Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M.
    EMBO J. 22:3613-3623(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA1A/B, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-101; ARG-333 AND HIS-409.
  11. "Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells."
    Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.
    Mol. Pharmacol. 64:1069-1075(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR1I3.
  12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: FUNCTION, INTERACTION WITH HSP90AB1; HSPA1A/B AND PGR.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDNJC7_HUMAN
AccessioniPrimary (citable) accession number: Q99615
Secondary accession number(s): Q7Z784
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 13, 2004
Last modified: June 24, 2015
This is version 147 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.