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Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Gene

PPP1CC

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

Functioni

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).4 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Cofactori

Mn2+2 PublicationsNote: Binds 2 manganese ions per subunit.2 Publications

Enzyme regulationi

Inactivated by binding to URI1. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Manganese 12 Publications1
Metal bindingi66Manganese 12 Publications1
Metal bindingi92Manganese 12 Publications1
Metal bindingi92Manganese 22 Publications1
Metal bindingi124Manganese 22 Publications1
Active sitei125Proton donor1 Publication1
Metal bindingi173Manganese 22 Publications1
Metal bindingi248Manganese 22 Publications1
Sitei273Inhibition by microcystin toxin binding1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphatase activity Source: UniProtKB
  • phosphoprotein phosphatase activity Source: Reactome
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: MGI
  • protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS07713-MONOMER.
BRENDAi3.1.3.16. 2681.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-400253. Circadian Clock.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiP36873.
SIGNORiP36873.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (EC:3.1.3.16)
Short name:
PP-1G
Alternative name(s):
Protein phosphatase 1C catalytic subunit
Gene namesi
Name:PPP1CC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9283. PPP1CC.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • Nucleusnucleolus
  • Nucleusnucleoplasm
  • Nucleus speckle
  • Chromosomecentromerekinetochore
  • Cleavage furrow
  • Midbody
  • Mitochondrion

  • Note: Colocalizes with SPZ1 in the nucleus (By similarity). Colocalizes with URI1 at mitochondrion. Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments. Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles. Shows a dynamic targeting to specific sites throughout the cell cycle. Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis. Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase. Also accumulates at the cleavage furrow and midbody by telophase.By similarity

GO - Cellular componenti

  • cleavage furrow Source: UniProtKB-SubCell
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • dendritic spine Source: Ensembl
  • focal adhesion Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • mitochondrial outer membrane Source: Ensembl
  • mitochondrion Source: UniProtKB
  • MLL5-L complex Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
  • PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125H → A: Loss of activity. 1 Publication1
Mutagenesisi273C → A, S or L: Abolishes interaction with microcystin toxin. 1 Publication1

Organism-specific databases

DisGeNETi5501.
OpenTargetsiENSG00000186298.
PharmGKBiPA33611.

Chemistry databases

ChEMBLiCHEMBL4438.

Polymorphism and mutation databases

BioMutaiPPP1CC.
DMDMi548573.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00000587872 – 323Serine/threonine-protein phosphatase PP1-gamma catalytic subunitAdd BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei307PhosphothreonineCombined sources1
Modified residuei311PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated by NEK2.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP36873.
MaxQBiP36873.
PaxDbiP36873.
PeptideAtlasiP36873.
PRIDEiP36873.
TopDownProteomicsiP36873-1. [P36873-1]
P36873-2. [P36873-2]

PTM databases

DEPODiP36873.
iPTMnetiP36873.
PhosphoSitePlusiP36873.
SwissPalmiP36873.

Expressioni

Inductioni

Up-regulated in synovial fluid mononuclear cells and peripheral blood mononuclear cells from patients with rheumatoid arthritis.1 Publication

Gene expression databases

BgeeiENSG00000186298.
CleanExiHS_PPP1CC.
ExpressionAtlasiP36873. baseline and differential.
GenevisibleiP36873. HS.

Organism-specific databases

HPAiCAB022645.
HPA013661.

Interactioni

Subunit structurei

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with cyanobacterial toxin microcystin; disulfide-linked. Interacts with PPP1R3B and PPP1R7. Isoform gamma-2 interacts with SPZ1 (By similarity). Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with CDCA2. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with PPP1R42; the interaction is direct (By similarity). Interacts with NOM1 and PPP1R8. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with isoform 1 and isoform 4 NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner. Interacts with FOXP3. Interacts with TMEM225 (via RVxF motif) (By similarity). Interacts with MKI67 (PubMed:24867636).By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A1DRY32EBI-3964623,EBI-4311408
BRCA1P383982EBI-356283,EBI-349905
CD2BP2O954003EBI-356283,EBI-768015
ClockO087852EBI-356283,EBI-79859From a different organism.
CSRNP1Q96S653EBI-356283,EBI-4311573
CSRNP2Q9H1755EBI-356283,EBI-5235958
PPP1R2P412365EBI-356283,EBI-1056517
PPP1R32Q7Z5V64EBI-3964623,EBI-4311771
PPP1R7Q154353EBI-356283,EBI-1024281
RANBP9Q96S593EBI-3964623,EBI-636085
TCTEX1D4Q5JR983EBI-3964623,EBI-4311709
TP53P046372EBI-356289,EBI-366083
TP53BP2Q136256EBI-356283,EBI-77642
TP53BP2Q13625-33EBI-356283,EBI-10175039
URI1O947637EBI-356283,EBI-357067
ZFYVE9O954055EBI-356283,EBI-296817

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: MGI

Protein-protein interaction databases

BioGridi111495. 292 interactors.
DIPiDIP-749N.
IntActiP36873. 200 interactors.
MINTiMINT-190765.
STRINGi9606.ENSP00000335084.

Chemistry databases

BindingDBiP36873.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 17Combined sources9
Turni18 – 21Combined sources4
Helixi32 – 48Combined sources17
Beta strandi51 – 55Combined sources5
Beta strandi57 – 62Combined sources6
Helixi69 – 79Combined sources11
Beta strandi87 – 89Combined sources3
Beta strandi94 – 98Combined sources5
Helixi100 – 113Combined sources14
Turni115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Helixi128 – 131Combined sources4
Turni132 – 135Combined sources4
Helixi136 – 143Combined sources8
Helixi146 – 156Combined sources11
Beta strandi162 – 165Combined sources4
Turni166 – 168Combined sources3
Beta strandi169 – 174Combined sources6
Helixi183 – 187Combined sources5
Beta strandi197 – 199Combined sources3
Helixi200 – 206Combined sources7
Beta strandi214 – 218Combined sources5
Beta strandi222 – 227Combined sources6
Helixi229 – 238Combined sources10
Beta strandi242 – 246Combined sources5
Beta strandi254 – 258Combined sources5
Turni259 – 262Combined sources4
Beta strandi263 – 267Combined sources5
Helixi272 – 274Combined sources3
Beta strandi280 – 285Combined sources6
Beta strandi291 – 296Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IT6X-ray2.00A/B1-323[»]
1JK7X-ray1.90A1-323[»]
1U32X-ray2.00A6-298[»]
2BCDX-ray2.10A1-323[»]
2BDXX-ray2.30A1-323[»]
4UT2X-ray1.96A/B1-323[»]
4UT3X-ray2.19A/B1-323[»]
5INBX-ray1.30A7-308[»]
5J28X-ray2.00A/B7-308[»]
ProteinModelPortaliP36873.
SMRiP36873.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36873.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP36873.
KOiK06269.
OMAiIQRLLEX.
OrthoDBiEOG091G0EKF.
PhylomeDBiP36873.
TreeFamiTF354243.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 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 Gamma-1 (identifier: P36873-1) [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
MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
310 320
KKKPNATRPV TPPRGMITKQ AKK
Length:323
Mass (Da):36,984
Last modified:June 1, 1994 - v1
Checksum:i0EEEF0E842188536
GO
Isoform Gamma-2 (identifier: P36873-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     315-323: GMITKQAKK → VASGLNPSIQKASNYRNNTVLYE

Show »
Length:337
Mass (Da):38,518
Checksum:i9731E5A6C8EEBF46
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051734152F → S.Corresponds to variant rs11558237dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005094315 – 323GMITKQAKK → VASGLNPSIQKASNYRNNTV LYE in isoform Gamma-2. 1 Publication9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74008 mRNA. Translation: CAA52169.1.
BC014073 mRNA. Translation: AAH14073.1.
L07395 mRNA. Translation: AAA19823.1.
CCDSiCCDS58279.1. [P36873-2]
CCDS9150.1. [P36873-1]
PIRiS35699.
S35700.
RefSeqiNP_001231903.1. NM_001244974.1. [P36873-2]
NP_002701.1. NM_002710.3. [P36873-1]
UniGeneiHs.79081.

Genome annotation databases

EnsembliENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1]
ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2]
GeneIDi5501.
KEGGihsa:5501.
UCSCiuc001tru.4. human. [P36873-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74008 mRNA. Translation: CAA52169.1.
BC014073 mRNA. Translation: AAH14073.1.
L07395 mRNA. Translation: AAA19823.1.
CCDSiCCDS58279.1. [P36873-2]
CCDS9150.1. [P36873-1]
PIRiS35699.
S35700.
RefSeqiNP_001231903.1. NM_001244974.1. [P36873-2]
NP_002701.1. NM_002710.3. [P36873-1]
UniGeneiHs.79081.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IT6X-ray2.00A/B1-323[»]
1JK7X-ray1.90A1-323[»]
1U32X-ray2.00A6-298[»]
2BCDX-ray2.10A1-323[»]
2BDXX-ray2.30A1-323[»]
4UT2X-ray1.96A/B1-323[»]
4UT3X-ray2.19A/B1-323[»]
5INBX-ray1.30A7-308[»]
5J28X-ray2.00A/B7-308[»]
ProteinModelPortaliP36873.
SMRiP36873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111495. 292 interactors.
DIPiDIP-749N.
IntActiP36873. 200 interactors.
MINTiMINT-190765.
STRINGi9606.ENSP00000335084.

Chemistry databases

BindingDBiP36873.
ChEMBLiCHEMBL4438.

PTM databases

DEPODiP36873.
iPTMnetiP36873.
PhosphoSitePlusiP36873.
SwissPalmiP36873.

Polymorphism and mutation databases

BioMutaiPPP1CC.
DMDMi548573.

Proteomic databases

EPDiP36873.
MaxQBiP36873.
PaxDbiP36873.
PeptideAtlasiP36873.
PRIDEiP36873.
TopDownProteomicsiP36873-1. [P36873-1]
P36873-2. [P36873-2]

Protocols and materials databases

DNASUi5501.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1]
ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2]
GeneIDi5501.
KEGGihsa:5501.
UCSCiuc001tru.4. human. [P36873-1]

Organism-specific databases

CTDi5501.
DisGeNETi5501.
GeneCardsiPPP1CC.
HGNCiHGNC:9283. PPP1CC.
HPAiCAB022645.
HPA013661.
MIMi176914. gene.
neXtProtiNX_P36873.
OpenTargetsiENSG00000186298.
PharmGKBiPA33611.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP36873.
KOiK06269.
OMAiIQRLLEX.
OrthoDBiEOG091G0EKF.
PhylomeDBiP36873.
TreeFamiTF354243.

Enzyme and pathway databases

BioCyciZFISH:HS07713-MONOMER.
BRENDAi3.1.3.16. 2681.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-400253. Circadian Clock.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiP36873.
SIGNORiP36873.

Miscellaneous databases

ChiTaRSiPPP1CC. human.
EvolutionaryTraceiP36873.
GeneWikiiPPP1CC.
GenomeRNAii5501.
PROiP36873.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000186298.
CleanExiHS_PPP1CC.
ExpressionAtlasiP36873. baseline and differential.
GenevisibleiP36873. HS.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPP1G_HUMAN
AccessioniPrimary (citable) accession number: P36873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 199 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

Miscellaneous

Microcystin toxin is bound to Cys-273 through a thioether bond.

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. 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.