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Protein

DnaJ homolog subfamily A member 3, mitochondrial

Gene

DNAJA3

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

Functioni

Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi236Zinc 1Combined sources1 Publication1
Metal bindingi239Zinc 1Combined sources1 Publication1
Metal bindingi253Zinc 2Combined sources1 Publication1
Metal bindingi256Zinc 2Combined sources1 Publication1
Metal bindingi275Zinc 2Combined sources1 Publication1
Metal bindingi278Zinc 2Combined sources1 Publication1
Metal bindingi289Zinc 1Combined sources1 Publication1
Metal bindingi292Zinc 1Combined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri223 – 301CR-typeAdd BLAST79

GO - Molecular functioni

  • ATP binding Source: InterPro
  • GTPase regulator activity Source: Ensembl
  • interferon-gamma receptor binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • NF-kappaB binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • activation-induced cell death of T cells Source: Ensembl
  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • cell aging Source: Ensembl
  • mitochondrial DNA replication Source: Ensembl
  • mitochondrion organization Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of interferon-gamma-mediated signaling pathway Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of programmed cell death Source: Ensembl
  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • neuromuscular junction development Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of protein ubiquitination Source: UniProtKB
  • positive regulation of T cell proliferation Source: Ensembl
  • protein folding Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • response to heat Source: InterPro
  • response to interferon-gamma Source: UniProtKB
  • skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
  • small GTPase mediated signal transduction Source: Ensembl
  • T cell differentiation in thymus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily A member 3, mitochondrial
Alternative name(s):
DnaJ protein Tid-1
Short name:
hTid-1
Hepatocellular carcinoma-associated antigen 57
Tumorous imaginal discs protein Tid56 homolog
Gene namesi
Name:DNAJA3
Synonyms:HCA57, TID1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11808. DNAJA3.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extrinsic component of plasma membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • mitochondrial matrix Source: UniProtKB
  • mitochondrial nucleoid Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • neuromuscular junction Source: UniProtKB
  • nucleus Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Mitochondrion, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121H → Q: Loss of modulation of apoptosis. 1 Publication1

Organism-specific databases

DisGeNETi9093.
OpenTargetsiENSG00000103423.
ENSG00000276726.
PharmGKBiPA27410.

Polymorphism and mutation databases

BioMutaiDNAJA3.
DMDMi311033374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000007256? – 480DnaJ homolog subfamily A member 3, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei58Omega-N-methylarginine; by CARM11 Publication1
Modified residuei134N6-acetyllysineBy similarity1
Modified residuei238Omega-N-methylarginine; by CARM11 Publication1
Modified residuei293Omega-N-methylarginine; by CARM11 Publication1
Modified residuei398PhosphoserineCombined sources1

Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ96EY1.
MaxQBiQ96EY1.
PaxDbiQ96EY1.
PeptideAtlasiQ96EY1.
PRIDEiQ96EY1.

PTM databases

iPTMnetiQ96EY1.
PhosphoSitePlusiQ96EY1.

Expressioni

Tissue specificityi

Widely expressed with highest levels in heart, liver, lung and skeletal muscles. Also expressed in keratinocytes.1 Publication

Gene expression databases

BgeeiENSG00000103423.
CleanExiHS_DNAJA3.
ExpressionAtlasiQ96EY1. baseline and differential.
GenevisibleiQ96EY1. HS.

Organism-specific databases

HPAiCAB016095.
HPA040875.
HPA044229.

Interactioni

Subunit structurei

Interacts with JAK2, HSPA9B and IFN-gammaR2 chain. Interacts with Ras GTPase-activating protein 1 (RASA1). Isoform 2 interacts with MUSK (via the cytoplasmic domain) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9H6143EBI-3952284,EBI-10249899
ALS2CR11Q53TS83EBI-3952284,EBI-739879
CARM1Q86X552EBI-356767,EBI-2339854
FAM214BQ7L5A33EBI-3952284,EBI-745689
FOSL2P154083EBI-3952284,EBI-3893419
FRMD6Q96NE93EBI-3952284,EBI-741729
GCC1Q96CN93EBI-3952284,EBI-746252
INPP5JQ157353EBI-3952284,EBI-10236940
KDM1AO603412EBI-356767,EBI-710124
METP085812EBI-3952284,EBI-1039152
NOC4LQ9BVI43EBI-3952284,EBI-395927
OSGIN1Q9UJX03EBI-3952284,EBI-9057006
PRMT6Q96LA82EBI-356767,EBI-912440
STAT5BP516922EBI-356767,EBI-1186119
Stat5bP422323EBI-356767,EBI-617454From a different organism.
STK16O757163EBI-3952284,EBI-749295
TCF19D2IYK53EBI-3952284,EBI-10176552

GO - Molecular functioni

  • interferon-gamma receptor binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114547. 78 interactors.
DIPiDIP-33870N.
IntActiQ96EY1. 62 interactors.
MINTiMINT-1151431.
STRINGi9606.ENSP00000262375.

Structurei

Secondary structure

1480
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi94 – 98Combined sources5
Helixi106 – 119Combined sources14
Turni122 – 124Combined sources3
Helixi131 – 146Combined sources16
Helixi148 – 156Combined sources9
Beta strandi222 – 224Combined sources3
Beta strandi237 – 244Combined sources8
Beta strandi254 – 259Combined sources6
Beta strandi261 – 266Combined sources6
Beta strandi269 – 274Combined sources6
Beta strandi276 – 284Combined sources9
Beta strandi290 – 294Combined sources5
Beta strandi296 – 298Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CTTNMR-A213-303[»]
2DN9NMR-A93-158[»]
ProteinModelPortaliQ96EY1.
SMRiQ96EY1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96EY1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini93 – 158JAdd BLAST66
Repeati236 – 243CXXCXGXG motif8
Repeati253 – 260CXXCXGXG motif8
Repeati275 – 282CXXCXGXG motif8
Repeati289 – 296CXXCXGXG motif8

Domaini

Modulation of apoptosis, i.e. proapoptotic activity of isoform 1 and antiapoptotic activity of isoform 2, is J domain-dependent.

Sequence similaritiesi

Contains 1 CR-type zinc finger.Curated
Contains 1 J domain.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri223 – 301CR-typeAdd BLAST79

Keywords - Domaini

Repeat, Transit peptide, Zinc-finger

Phylogenomic databases

eggNOGiKOG0715. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00860000133735.
HOGENOMiHOG000203530.
HOVERGENiHBG051371.
InParanoidiQ96EY1.
KOiK09504.
OMAiGPEGFSQ.
OrthoDBiEOG091G09C7.
PhylomeDBiQ96EY1.
TreeFamiTF105152.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ. 1 hit.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 1 hit.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96EY1-1) [UniParc]FASTAAdd to basket
Also known as: Tid-1(L)

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
MAARCSTRWL LVVVGTPRLP AISGRGARPP REGVVGAWLS RKLSVPAFAS
60 70 80 90 100
SLTSCGPRAL LTLRPGVSLT GTKHNPFICT ASFHTSAPLA KEDYYQILGV
110 120 130 140 150
PRNASQKEIK KAYYQLAKKY HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK
160 170 180 190 200
RKQYDAYGSA GFDPGASGSQ HSYWKGGPTV DPEELFRKIF GEFSSSSFGD
210 220 230 240 250
FQTVFDQPQE YFMELTFNQA AKGVNKEFTV NIMDTCERCN GKGNEPGTKV
260 270 280 290 300
QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIIISPCV VCRGAGQAKQ
310 320 330 340 350
KKRVMIPVPA GVEDGQTVRM PVGKREIFIT FRVQKSPVFR RDGADIHSDL
360 370 380 390 400
FISIAQALLG GTARAQGLYE TINVTIPPGT QTDQKIRMGG KGIPRINSYG
410 420 430 440 450
YGDHYIHIKI RVPKRLTSRQ QSLILSYAED ETDVEGTVNG VTLTSSGGST
460 470 480
MDSSAGSKAR REAGEDEEGF LSKLKKMFTS
Length:480
Mass (Da):52,489
Last modified:November 2, 2010 - v2
Checksum:i5A57B9020992CF59
GO
Isoform 2 (identifier: Q96EY1-2) [UniParc]FASTAAdd to basket
Also known as: Tid-1(S)

The sequence of this isoform differs from the canonical sequence as follows:
     448-453: GSTMDS → KRSTGN
     454-480: Missing.

Show »
Length:453
Mass (Da):49,611
Checksum:iE235B8DC1DB99FBC
GO
Isoform 3 (identifier: Q96EY1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-186: ARCSTRWLLV...GPTVDPEELF → EPQAERPRLCVFPDLLRPPSAADIETWCQPY
     448-453: GSTMDS → KRSTGN
     454-480: Missing.

Show »
Length:300
Mass (Da):33,082
Checksum:i36D883E568E8ECC8
GO

Sequence cautioni

The sequence AAF66245 differs from that shown. Reason: Frameshift at positions 408 and 411.Curated
The sequence AAF66245 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH12343 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti320M → W in AAF66245 (PubMed:12097419).Curated1
Isoform 3 (identifier: Q96EY1-3)
Sequence conflicti33Y → H in BAG58345 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02796575N → Y.4 PublicationsCorresponds to variant rs4785963dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0557283 – 186ARCST…PEELF → EPQAERPRLCVFPDLLRPPS AADIETWCQPY in isoform 3. 1 PublicationAdd BLAST184
Alternative sequenceiVSP_007425448 – 453GSTMDS → KRSTGN in isoform 2 and isoform 3. 4 Publications6
Alternative sequenceiVSP_007426454 – 480Missing in isoform 2 and isoform 3. 4 PublicationsAdd BLAST27

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061749 mRNA. Translation: AAC29066.1.
AF411044 mRNA. Translation: AAL35323.1.
AK295391 mRNA. Translation: BAG58345.1.
AK314218 mRNA. Translation: BAG36892.1.
AC012676 Genomic DNA. No translation available.
BC007225 mRNA. Translation: AAH07225.1.
BC011855 mRNA. Translation: AAH11855.1.
BC012343 mRNA. Translation: AAH12343.1. Different initiation.
BC014062 mRNA. Translation: AAH14062.1.
BC020248 mRNA. Translation: AAH20248.1.
BC030145 mRNA. Translation: AAH30145.1.
BC032100 mRNA. Translation: AAH32100.1.
AF244136 mRNA. Translation: AAF66245.1. Sequence problems.
CCDSiCCDS10515.1. [Q96EY1-1]
CCDS45400.1. [Q96EY1-2]
CCDS66930.1. [Q96EY1-3]
RefSeqiNP_001128582.1. NM_001135110.2. [Q96EY1-2]
NP_001273445.1. NM_001286516.1. [Q96EY1-3]
NP_005138.3. NM_005147.5. [Q96EY1-1]
UniGeneiHs.459779.

Genome annotation databases

EnsembliENST00000262375; ENSP00000262375; ENSG00000103423. [Q96EY1-1]
ENST00000355296; ENSP00000347445; ENSG00000103423. [Q96EY1-2]
ENST00000431375; ENSP00000393970; ENSG00000103423. [Q96EY1-3]
ENST00000612103; ENSP00000477570; ENSG00000276726. [Q96EY1-1]
ENST00000614397; ENSP00000479815; ENSG00000276726. [Q96EY1-2]
GeneIDi9093.
KEGGihsa:9093.
UCSCiuc002cwk.4. human. [Q96EY1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061749 mRNA. Translation: AAC29066.1.
AF411044 mRNA. Translation: AAL35323.1.
AK295391 mRNA. Translation: BAG58345.1.
AK314218 mRNA. Translation: BAG36892.1.
AC012676 Genomic DNA. No translation available.
BC007225 mRNA. Translation: AAH07225.1.
BC011855 mRNA. Translation: AAH11855.1.
BC012343 mRNA. Translation: AAH12343.1. Different initiation.
BC014062 mRNA. Translation: AAH14062.1.
BC020248 mRNA. Translation: AAH20248.1.
BC030145 mRNA. Translation: AAH30145.1.
BC032100 mRNA. Translation: AAH32100.1.
AF244136 mRNA. Translation: AAF66245.1. Sequence problems.
CCDSiCCDS10515.1. [Q96EY1-1]
CCDS45400.1. [Q96EY1-2]
CCDS66930.1. [Q96EY1-3]
RefSeqiNP_001128582.1. NM_001135110.2. [Q96EY1-2]
NP_001273445.1. NM_001286516.1. [Q96EY1-3]
NP_005138.3. NM_005147.5. [Q96EY1-1]
UniGeneiHs.459779.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CTTNMR-A213-303[»]
2DN9NMR-A93-158[»]
ProteinModelPortaliQ96EY1.
SMRiQ96EY1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114547. 78 interactors.
DIPiDIP-33870N.
IntActiQ96EY1. 62 interactors.
MINTiMINT-1151431.
STRINGi9606.ENSP00000262375.

PTM databases

iPTMnetiQ96EY1.
PhosphoSitePlusiQ96EY1.

Polymorphism and mutation databases

BioMutaiDNAJA3.
DMDMi311033374.

Proteomic databases

EPDiQ96EY1.
MaxQBiQ96EY1.
PaxDbiQ96EY1.
PeptideAtlasiQ96EY1.
PRIDEiQ96EY1.

Protocols and materials databases

DNASUi9093.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262375; ENSP00000262375; ENSG00000103423. [Q96EY1-1]
ENST00000355296; ENSP00000347445; ENSG00000103423. [Q96EY1-2]
ENST00000431375; ENSP00000393970; ENSG00000103423. [Q96EY1-3]
ENST00000612103; ENSP00000477570; ENSG00000276726. [Q96EY1-1]
ENST00000614397; ENSP00000479815; ENSG00000276726. [Q96EY1-2]
GeneIDi9093.
KEGGihsa:9093.
UCSCiuc002cwk.4. human. [Q96EY1-1]

Organism-specific databases

CTDi9093.
DisGeNETi9093.
GeneCardsiDNAJA3.
H-InvDBHIX0012782.
HGNCiHGNC:11808. DNAJA3.
HPAiCAB016095.
HPA040875.
HPA044229.
MIMi608382. gene.
neXtProtiNX_Q96EY1.
OpenTargetsiENSG00000103423.
ENSG00000276726.
PharmGKBiPA27410.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0715. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00860000133735.
HOGENOMiHOG000203530.
HOVERGENiHBG051371.
InParanoidiQ96EY1.
KOiK09504.
OMAiGPEGFSQ.
OrthoDBiEOG091G09C7.
PhylomeDBiQ96EY1.
TreeFamiTF105152.

Miscellaneous databases

ChiTaRSiDNAJA3. human.
EvolutionaryTraceiQ96EY1.
GeneWikiiDNAJA3.
GenomeRNAii9093.
PROiQ96EY1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103423.
CleanExiHS_DNAJA3.
ExpressionAtlasiQ96EY1. baseline and differential.
GenevisibleiQ96EY1. HS.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ. 1 hit.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 1 hit.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNJA3_HUMAN
AccessioniPrimary (citable) accession number: Q96EY1
Secondary accession number(s): B2RAJ5
, B4DI33, E7ES32, O75472, Q8WUJ6, Q8WXJ3, Q96D76, Q96IV1, Q9NYH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: November 2, 2010
Last modified: November 30, 2016
This is version 160 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.