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Protein

DnaJ homolog subfamily B member 1

Gene

DNAJB1

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

Functioni

Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.

GO - Molecular functioni

  1. ATPase activator activity Source: BHF-UCL
  2. ATPase binding Source: BHF-UCL
  3. chaperone binding Source: UniProtKB
  4. Hsp70 protein binding Source: BHF-UCL
  5. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. chaperone cofactor-dependent protein refolding Source: UniProtKB
  2. chaperone mediated protein folding requiring cofactor Source: Ensembl
  3. negative regulation of inclusion body assembly Source: UniProtKB
  4. positive regulation of ATPase activity Source: BHF-UCL
  5. response to unfolded protein Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

ReactomeiREACT_200624. Attenuation phase.
REACT_200775. HSF1-dependent transactivation.
REACT_200780. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily B member 1
Alternative name(s):
DnaJ protein homolog 1
Heat shock 40 kDa protein 1
Short name:
HSP40
Short name:
Heat shock protein 40
Human DnaJ protein 1
Short name:
hDj-1
Gene namesi
Name:DNAJB1
Synonyms:DNAJ1, HDJ1, HSPF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:5270. DNAJB1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. Nucleusnucleolus 1 Publication
Note: Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti401920. Fibrolamellar hepatocellular carcinoma.
PharmGKBiPA27412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 340339DnaJ homolog subfamily B member 1PRO_0000071016Add
BLAST

Proteomic databases

MaxQBiP25685.
PaxDbiP25685.
PeptideAtlasiP25685.
PRIDEiP25685.

2D gel databases

REPRODUCTION-2DPAGEIPI00015947.

PTM databases

PhosphoSiteiP25685.

Expressioni

Inductioni

By heat shock.1 Publication

Gene expression databases

BgeeiP25685.
CleanExiHS_DNAJB1.
ExpressionAtlasiP25685. baseline and differential.
GenevestigatoriP25685.

Organism-specific databases

HPAiCAB017450.

Interactioni

Subunit structurei

Interacts with DNAJC3. Interacts with SRPK1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Phlda1Q623922EBI-357034,EBI-309727From a different organism.

Protein-protein interaction databases

BioGridi109569. 61 interactions.
DIPiDIP-41180N.
IntActiP25685. 30 interactions.
MINTiMINT-204558.
STRINGi9606.ENSP00000254322.

Structurei

Secondary structure

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi166 – 1705Combined sources
Helixi172 – 1776Combined sources
Beta strandi179 – 19012Combined sources
Turni191 – 1933Combined sources
Beta strandi197 – 20812Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi235 – 2417Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi253 – 2619Combined sources
Helixi262 – 2676Combined sources
Beta strandi269 – 2746Combined sources
Beta strandi280 – 2856Combined sources
Beta strandi294 – 2974Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi314 – 3218Combined sources
Helixi328 – 33710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDJNMR-A1-76[»]
2QLDX-ray2.70A158-340[»]
3AGXX-ray1.85A/B161-340[»]
3AGYX-ray1.85A/B161-340[»]
3AGZX-ray2.51A/B151-340[»]
ProteinModelPortaliP25685.
SMRiP25685. Positions 1-340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25685.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7069JPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2214.
GeneTreeiENSGT00760000118947.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiP25685.
KOiK09507.
OMAiGLPMGMG.
OrthoDBiEOG7TF79F.
PhylomeDBiP25685.
TreeFamiTF105141.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamiPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 2 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 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. Align

Isoform 1 (identifier: P25685-1) [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
MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE
60 70 80 90 100
AYDVLSDPRK REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHA
110 120 130 140 150
MFAEFFGGRN PFDTFFGQRN GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR
160 170 180 190 200
SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT KKMKISHKRL NPDGKSIRNE
210 220 230 240 250
DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK DKPHNIFKRD
260 270 280 290 300
GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE
310 320 330 340
GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI
Length:340
Mass (Da):38,044
Last modified:January 23, 2007 - v4
Checksum:i17545098B0C196DF
GO
Isoform 2 (identifier: P25685-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Note: No experimental confirmation available.

Show »
Length:240
Mass (Da):27,016
Checksum:i760FFA819B48174B
GO

Sequence cautioni

The sequence CAA44287.1 differs from that shown. Reason: Frameshift at positions 11, 28, 81 and 136. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681G → L in CAA44287. (PubMed:1754405)Curated
Sequence conflicti150 – 1501R → C in CAA44287. (PubMed:1754405)Curated
Sequence conflicti183 – 1831M → T in CAA44287. (PubMed:1754405)Curated
Sequence conflicti320 – 3201V → A in CAA44287. (PubMed:1754405)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_056414Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62421 mRNA. Translation: CAA44287.1. Frameshift.
D49547 mRNA. Translation: BAA08495.1.
D85429 Genomic DNA. Translation: BAA12819.1.
AK301817 mRNA. Translation: BAG63264.1.
AC009004 Genomic DNA. No translation available.
AC012318 Genomic DNA. No translation available.
BC002352 mRNA. Translation: AAH02352.1.
BC019827 mRNA. Translation: AAH19827.1.
CCDSiCCDS12312.1. [P25685-1]
CCDS74295.1. [P25685-2]
PIRiJN0912.
S20062.
RefSeqiNP_001287843.1. NM_001300914.1. [P25685-2]
NP_006136.1. NM_006145.2. [P25685-1]
XP_006722796.1. XM_006722733.1. [P25685-2]
XP_006722797.1. XM_006722734.1. [P25685-2]
XP_006722798.1. XM_006722735.1. [P25685-2]
UniGeneiHs.515210.

Genome annotation databases

EnsembliENST00000254322; ENSP00000254322; ENSG00000132002. [P25685-1]
ENST00000396969; ENSP00000444212; ENSG00000132002. [P25685-2]
GeneIDi3337.
KEGGihsa:3337.
UCSCiuc002myz.1. human. [P25685-1]

Polymorphism databases

DMDMi1706473.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62421 mRNA. Translation: CAA44287.1. Frameshift.
D49547 mRNA. Translation: BAA08495.1.
D85429 Genomic DNA. Translation: BAA12819.1.
AK301817 mRNA. Translation: BAG63264.1.
AC009004 Genomic DNA. No translation available.
AC012318 Genomic DNA. No translation available.
BC002352 mRNA. Translation: AAH02352.1.
BC019827 mRNA. Translation: AAH19827.1.
CCDSiCCDS12312.1. [P25685-1]
CCDS74295.1. [P25685-2]
PIRiJN0912.
S20062.
RefSeqiNP_001287843.1. NM_001300914.1. [P25685-2]
NP_006136.1. NM_006145.2. [P25685-1]
XP_006722796.1. XM_006722733.1. [P25685-2]
XP_006722797.1. XM_006722734.1. [P25685-2]
XP_006722798.1. XM_006722735.1. [P25685-2]
UniGeneiHs.515210.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDJNMR-A1-76[»]
2QLDX-ray2.70A158-340[»]
3AGXX-ray1.85A/B161-340[»]
3AGYX-ray1.85A/B161-340[»]
3AGZX-ray2.51A/B151-340[»]
ProteinModelPortaliP25685.
SMRiP25685. Positions 1-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109569. 61 interactions.
DIPiDIP-41180N.
IntActiP25685. 30 interactions.
MINTiMINT-204558.
STRINGi9606.ENSP00000254322.

PTM databases

PhosphoSiteiP25685.

Polymorphism databases

DMDMi1706473.

2D gel databases

REPRODUCTION-2DPAGEIPI00015947.

Proteomic databases

MaxQBiP25685.
PaxDbiP25685.
PeptideAtlasiP25685.
PRIDEiP25685.

Protocols and materials databases

DNASUi3337.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254322; ENSP00000254322; ENSG00000132002. [P25685-1]
ENST00000396969; ENSP00000444212; ENSG00000132002. [P25685-2]
GeneIDi3337.
KEGGihsa:3337.
UCSCiuc002myz.1. human. [P25685-1]

Organism-specific databases

CTDi3337.
GeneCardsiGC19M014625.
H-InvDBHIX0014838.
HGNCiHGNC:5270. DNAJB1.
HPAiCAB017450.
MIMi604572. gene.
neXtProtiNX_P25685.
Orphaneti401920. Fibrolamellar hepatocellular carcinoma.
PharmGKBiPA27412.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2214.
GeneTreeiENSGT00760000118947.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiP25685.
KOiK09507.
OMAiGLPMGMG.
OrthoDBiEOG7TF79F.
PhylomeDBiP25685.
TreeFamiTF105141.

Enzyme and pathway databases

ReactomeiREACT_200624. Attenuation phase.
REACT_200775. HSF1-dependent transactivation.
REACT_200780. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

ChiTaRSiDNAJB1. human.
EvolutionaryTraceiP25685.
GeneWikiiDNAJB1.
GenomeRNAii3337.
NextBioi13208.
PROiP25685.
SOURCEiSearch...

Gene expression databases

BgeeiP25685.
CleanExiHS_DNAJB1.
ExpressionAtlasiP25685. baseline and differential.
GenevestigatoriP25685.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamiPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 2 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human homologue of the Escherichia coli DnaJ heat-shock protein."
    Raabe T., Manley J.L.
    Nucleic Acids Res. 19:6645-6645(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ."
    Ohtsuka K.
    Biochem. Biophys. Res. Commun. 197:235-240(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-48.
    Tissue: Placenta.
  3. "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2."
    Hata M., Okumura K., Seto M., Ohtsuka K.
    Genomics 38:446-449(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  4. "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: Testis.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain and Lung.
  7. "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells."
    Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.
    Cell Struct. Funct. 17:77-86(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-49, INDUCTION, SUBCELLULAR LOCATION.
  8. "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity."
    Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.
    J. Biol. Chem. 274:3797-3803(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNAJC3.
  9. "Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones."
    Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.
    Genes Dev. 23:482-495(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRPK1.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain."
    Qian Y.Q., Patel D., Hartl F.-U., McColl D.J.
    J. Mol. Biol. 260:224-235(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-76.

Entry informationi

Entry nameiDNJB1_HUMAN
AccessioniPrimary (citable) accession number: P25685
Secondary accession number(s): B4DX52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 158 of the entry and version 4 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.