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Protein

Calreticulin

Gene

CALR

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

Functioni

Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi26Calcium; via carbonyl oxygen1
Metal bindingi62Calcium; via carbonyl oxygen1
Metal bindingi64Calcium; via carbonyl oxygen1
Binding sitei109CarbohydrateBy similarity1
Binding sitei111CarbohydrateBy similarity1
Binding sitei128CarbohydrateBy similarity1
Binding sitei135CarbohydrateBy similarity1
Binding sitei317CarbohydrateBy similarity1
Metal bindingi328Calcium1

GO - Molecular functioni

  • androgen receptor binding Source: BHF-UCL
  • calcium ion binding Source: UniProtKB
  • carbohydrate binding Source: BHF-UCL
  • chaperone binding Source: BHF-UCL
  • complement component C1q binding Source: BHF-UCL
  • DNA binding Source: UniProtKB
  • glycoprotein binding Source: UniProtKB
  • hormone binding Source: Ensembl
  • integrin binding Source: BHF-UCL
  • iron ion binding Source: Ensembl
  • mRNA binding Source: BHF-UCL
  • peptide binding Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB
  • protein binding involved in protein folding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB
  • unfolded protein binding Source: BHF-UCL
  • zinc ion binding Source: BHF-UCL

GO - Biological processi

  • antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  • ATF6-mediated unfolded protein response Source: Reactome
  • cardiac muscle cell differentiation Source: Ensembl
  • cell cycle arrest Source: BHF-UCL
  • cellular calcium ion homeostasis Source: UniProtKB
  • cellular response to lithium ion Source: Ensembl
  • cellular senescence Source: BHF-UCL
  • chaperone-mediated protein folding Source: Ensembl
  • cortical actin cytoskeleton organization Source: Ensembl
  • glucocorticoid receptor signaling pathway Source: BHF-UCL
  • negative regulation of intracellular steroid hormone receptor signaling pathway Source: BHF-UCL
  • negative regulation of neuron differentiation Source: BHF-UCL
  • negative regulation of retinoic acid receptor signaling pathway Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of translation Source: BHF-UCL
  • peptide antigen assembly with MHC class I protein complex Source: BHF-UCL
  • positive regulation of cell cycle Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of dendritic cell chemotaxis Source: UniProtKB
  • positive regulation of DNA replication Source: BHF-UCL
  • positive regulation of gene expression Source: Ensembl
  • positive regulation of NIK/NF-kappaB signaling Source: Ensembl
  • positive regulation of phagocytosis Source: BHF-UCL
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • protein export from nucleus Source: UniProtKB
  • protein folding Source: BHF-UCL
  • protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
  • protein localization to nucleus Source: UniProtKB
  • protein maturation by protein folding Source: BHF-UCL
  • protein stabilization Source: UniProtKB
  • receptor-mediated endocytosis Source: Reactome
  • regulation of apoptotic process Source: UniProtKB
  • regulation of meiotic nuclear division Source: Ensembl
  • regulation of transcription, DNA-templated Source: ProtInc
  • response to drug Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to testosterone Source: Ensembl
  • sequestering of calcium ion Source: BHF-UCL
  • spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000004948-MONOMER.
ZFISH:ENSG00000179218-MONOMER.
ReactomeiR-HSA-1236974. ER-Phagosome pathway.
R-HSA-168316. Assembly of Viral Components at the Budding Site.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-3000484. Scavenging by Class F Receptors.
R-HSA-381183. ATF6 (ATF6-alpha) activates chaperone genes.
R-HSA-901042. Calnexin/calreticulin cycle.
R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Alternative name(s):
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
Short name:
ERp60
HACBP
grp60
Gene namesi
Name:CALR
Synonyms:CRTC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1455. CALR.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: Ensembl
  • cell surface Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • cytosol Source: UniProtKB
  • endocytic vesicle lumen Source: Reactome
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: UniProtKB
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  • intracellular Source: UniProtKB
  • membrane Source: UniProtKB
  • MHC class I peptide loading complex Source: BHF-UCL
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: BHF-UCL
  • polysome Source: BHF-UCL
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
  • smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Extracellular matrix, Sarcoplasmic reticulum, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi811.
MalaCardsiCALR.
OpenTargetsiENSG00000179218.
Orphaneti3318. Essential thrombocythemia.
824. Myelofibrosis with myeloid metaplasia.
PharmGKBiPA26046.

Chemistry databases

DrugBankiDB00025. Antihemophilic Factor (Recombinant).
DB01065. Melatonin.
DB00031. Tenecteplase.

Polymorphism and mutation databases

BioMutaiCALR.
DMDMi117501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Combined sources7 PublicationsAdd BLAST17
ChainiPRO_000000417318 – 417CalreticulinAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48N6-acetyllysineCombined sources1
Disulfide bondi105 ↔ 1372 Publications
Modified residuei159N6-acetyllysineCombined sources1
Modified residuei209N6-acetyllysineCombined sources1
Glycosylationi344N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

EPDiP27797.
PaxDbiP27797.
PeptideAtlasiP27797.
PRIDEiP27797.
TopDownProteomicsiP27797.

2D gel databases

DOSAC-COBS-2DPAGEP27797.
OGPiP27797.
REPRODUCTION-2DPAGEIPI00020599.
SWISS-2DPAGEP27797.
UCD-2DPAGEP27797.

PTM databases

iPTMnetiP27797.
PhosphoSitePlusiP27797.
SwissPalmiP27797.

Expressioni

Gene expression databases

BgeeiENSG00000179218.
CleanExiHS_CALR.
ExpressionAtlasiP27797. baseline and differential.
GenevisibleiP27797. HS.

Organism-specific databases

HPAiCAB001513.
CAB019952.
HPA002242.

Interactioni

Subunit structurei

Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 and SPACA9 (By similarity). Interacts with NR3C1 and TRIM21. Interacts with GABARAP. Interacts with PPIB.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050672EBI-1049597,EBI-77613
GABARAPO951664EBI-1049597,EBI-712001
HSPB1P047922EBI-1049597,EBI-352682
TAP1Q035182EBI-1049597,EBI-747259

GO - Molecular functioni

  • androgen receptor binding Source: BHF-UCL
  • chaperone binding Source: BHF-UCL
  • complement component C1q binding Source: BHF-UCL
  • integrin binding Source: BHF-UCL
  • protein binding involved in protein folding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB
  • unfolded protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107262. 125 interactors.
DIPiDIP-104N.
IntActiP27797. 41 interactors.
MINTiMINT-101756.
STRINGi9606.ENSP00000320866.

Structurei

Secondary structure

1417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 25Combined sources6
Helixi30 – 35Combined sources6
Beta strandi37 – 39Combined sources3
Beta strandi42 – 44Combined sources3
Beta strandi49 – 52Combined sources4
Turni60 – 63Combined sources4
Beta strandi65 – 68Combined sources4
Beta strandi70 – 84Combined sources15
Beta strandi91 – 98Combined sources8
Beta strandi104 – 107Combined sources4
Beta strandi110 – 113Combined sources4
Helixi119 – 121Combined sources3
Beta strandi129 – 138Combined sources10
Beta strandi142 – 150Combined sources9
Beta strandi153 – 156Combined sources4
Beta strandi166 – 176Combined sources11
Beta strandi180 – 186Combined sources7
Beta strandi189 – 195Combined sources7
Helixi196 – 199Combined sources4
Beta strandi201 – 203Combined sources3
Turni303 – 306Combined sources4
Beta strandi311 – 322Combined sources12
Beta strandi326 – 334Combined sources9
Helixi336 – 345Combined sources10
Helixi347 – 366Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CLRX-ray2.00C/F1-10[»]
3DOWX-ray2.30B195-205[»]
3POSX-ray1.65A/B/C18-204[»]
A/B/C302-368[»]
3POWX-ray1.55A18-204[»]
A302-368[»]
5LK5X-ray2.30A/B/C/D/E/F/G/H/I/J18-204[»]
A/B/C/D/E/F/G/H/I/J303-368[»]
DisProtiDP00333.
ProteinModelPortaliP27797.
SMRiP27797.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati191 – 2021-1Add BLAST12
Repeati210 – 2211-2Add BLAST12
Repeati227 – 2381-3Add BLAST12
Repeati244 – 2551-4Add BLAST12
Repeati259 – 2692-1Add BLAST11
Repeati273 – 2832-2Add BLAST11
Repeati287 – 2972-3Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 197N-domainAdd BLAST180
Regioni191 – 2554 X approximate repeatsAdd BLAST65
Regioni198 – 308P-domainAdd BLAST111
Regioni237 – 270Interaction with PPIBBy similarityAdd BLAST34
Regioni259 – 2973 X approximate repeatsAdd BLAST39
Regioni309 – 417C-domainAdd BLAST109

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi414 – 417Prevents secretion from ER4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi351 – 408Asp/Glu/Lys-richAdd BLAST58

Domaini

Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity.
The interaction with glycans occurs through a binding site in the globular lectin domain.
The zinc binding sites are localized to the N-domain.
Associates with PDIA3 through the tip of the extended arm formed by the P-domain.

Sequence similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP27797.
KOiK08057.
OMAiIANPEYV.
OrthoDBiEOG091G0AP1.
PhylomeDBiP27797.
TreeFamiTF338438.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 2 hits.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 2 hits.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSVPLLLG LLGLAVAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV
60 70 80 90 100
LSSGKFYGDE EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE
110 120 130 140 150
QNIDCGGGYV KLFPNSLDQT DMHGDSEYNI MFGPDICGPG TKKVHVIFNY
160 170 180 190 200
KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW
210 220 230 240 250
DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP
260 270 280 290 300
EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
310 320 330 340 350
PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT
360 370 380 390 400
KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED
410
KEEDEEEDVP GQAKDEL
Length:417
Mass (Da):48,142
Last modified:August 1, 1992 - v1
Checksum:iBC37C3C0F1054FB2
GO

Mass spectrometryi

Molecular mass is 46879 Da from positions 18 - 417. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32294 mRNA. Translation: AAA36582.1.
M84739 mRNA. Translation: AAA51916.1.
AY047586 mRNA. Translation: AAL13126.1.
AB451408 mRNA. Translation: BAG70222.1.
BT007448 mRNA. Translation: AAP36116.1.
CR457070 mRNA. Translation: CAG33351.1.
AD000092 Genomic DNA. Translation: AAB51176.1.
CH471106 Genomic DNA. Translation: EAW84331.1.
BC002500 mRNA. Translation: AAH02500.1.
BC007911 mRNA. Translation: AAH07911.1.
BC020493 mRNA. Translation: AAH20493.1.
CCDSiCCDS12288.1.
PIRiA42330. A37047.
RefSeqiNP_004334.1. NM_004343.3.
UniGeneiHs.515162.

Genome annotation databases

EnsembliENST00000316448; ENSP00000320866; ENSG00000179218.
GeneIDi811.
KEGGihsa:811.

Cross-referencesi

Web resourcesi

Wikipedia

Calreticulin entry

Functional Glycomics Gateway - Glycan Binding

Calreticulin

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32294 mRNA. Translation: AAA36582.1.
M84739 mRNA. Translation: AAA51916.1.
AY047586 mRNA. Translation: AAL13126.1.
AB451408 mRNA. Translation: BAG70222.1.
BT007448 mRNA. Translation: AAP36116.1.
CR457070 mRNA. Translation: CAG33351.1.
AD000092 Genomic DNA. Translation: AAB51176.1.
CH471106 Genomic DNA. Translation: EAW84331.1.
BC002500 mRNA. Translation: AAH02500.1.
BC007911 mRNA. Translation: AAH07911.1.
BC020493 mRNA. Translation: AAH20493.1.
CCDSiCCDS12288.1.
PIRiA42330. A37047.
RefSeqiNP_004334.1. NM_004343.3.
UniGeneiHs.515162.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CLRX-ray2.00C/F1-10[»]
3DOWX-ray2.30B195-205[»]
3POSX-ray1.65A/B/C18-204[»]
A/B/C302-368[»]
3POWX-ray1.55A18-204[»]
A302-368[»]
5LK5X-ray2.30A/B/C/D/E/F/G/H/I/J18-204[»]
A/B/C/D/E/F/G/H/I/J303-368[»]
DisProtiDP00333.
ProteinModelPortaliP27797.
SMRiP27797.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107262. 125 interactors.
DIPiDIP-104N.
IntActiP27797. 41 interactors.
MINTiMINT-101756.
STRINGi9606.ENSP00000320866.

Chemistry databases

DrugBankiDB00025. Antihemophilic Factor (Recombinant).
DB01065. Melatonin.
DB00031. Tenecteplase.

PTM databases

iPTMnetiP27797.
PhosphoSitePlusiP27797.
SwissPalmiP27797.

Polymorphism and mutation databases

BioMutaiCALR.
DMDMi117501.

2D gel databases

DOSAC-COBS-2DPAGEP27797.
OGPiP27797.
REPRODUCTION-2DPAGEIPI00020599.
SWISS-2DPAGEP27797.
UCD-2DPAGEP27797.

Proteomic databases

EPDiP27797.
PaxDbiP27797.
PeptideAtlasiP27797.
PRIDEiP27797.
TopDownProteomicsiP27797.

Protocols and materials databases

DNASUi811.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316448; ENSP00000320866; ENSG00000179218.
GeneIDi811.
KEGGihsa:811.

Organism-specific databases

CTDi811.
DisGeNETi811.
GeneCardsiCALR.
HGNCiHGNC:1455. CALR.
HPAiCAB001513.
CAB019952.
HPA002242.
MalaCardsiCALR.
MIMi109091. gene.
neXtProtiNX_P27797.
OpenTargetsiENSG00000179218.
Orphaneti3318. Essential thrombocythemia.
824. Myelofibrosis with myeloid metaplasia.
PharmGKBiPA26046.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP27797.
KOiK08057.
OMAiIANPEYV.
OrthoDBiEOG091G0AP1.
PhylomeDBiP27797.
TreeFamiTF338438.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000004948-MONOMER.
ZFISH:ENSG00000179218-MONOMER.
ReactomeiR-HSA-1236974. ER-Phagosome pathway.
R-HSA-168316. Assembly of Viral Components at the Budding Site.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-3000484. Scavenging by Class F Receptors.
R-HSA-381183. ATF6 (ATF6-alpha) activates chaperone genes.
R-HSA-901042. Calnexin/calreticulin cycle.
R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiCALR. human.
EvolutionaryTraceiP27797.
GeneWikiiCalreticulin.
GenomeRNAii811.
PROiP27797.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000179218.
CleanExiHS_CALR.
ExpressionAtlasiP27797. baseline and differential.
GenevisibleiP27797. HS.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 2 hits.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 2 hits.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCALR_HUMAN
AccessioniPrimary (citable) accession number: P27797
Secondary accession number(s): Q6IAT4, Q9UDG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 30, 2016
This is version 203 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

Caution

Was originally thought to be the 52 kDa Ro autoantigen.1 Publication

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

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.