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Protein

E3 ubiquitin-protein ligase CHFR

Gene

CHFR

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

Functioni

E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.7 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri304 – 343RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri633 – 655PBZ-typeAdd BLAST23

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • nucleotide binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: Ensembl
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase CHFR (EC:6.3.2.-)
Alternative name(s):
Checkpoint with forkhead and RING finger domains protein
RING finger protein 196
Gene namesi
Name:CHFR
Synonyms:RNF196
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20455. CHFR.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39T → A: Abolishes phosphorylation but not autoubiquitination; when associated with A-205. 1 Publication1
Mutagenesisi205S → A: Abolishes phosphorylation but not autoubiquitination; when associated with A-39. 1 Publication1
Mutagenesisi306I → A: Abolishes autoubiquitination. Does not affect phosphorylation. 2 Publications1
Mutagenesisi332W → A: Abolishes autoubiquitination in vitro. 1 Publication1
Mutagenesisi632R → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1. 1 Publication1
Mutagenesisi635C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-641. 1 Publication1
Mutagenesisi641C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-635. 1 Publication1
Mutagenesisi642R → A: Impairs poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1. 1 Publication1
Mutagenesisi644Q → A: Impairs poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1. 1 Publication1

Organism-specific databases

DisGeNETi55743.
OpenTargetsiENSG00000072609.
PharmGKBiPA134898949.

Polymorphism and mutation databases

BioMutaiCHFR.
DMDMi41688511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000558721 – 664E3 ubiquitin-protein ligase CHFRAdd BLAST664

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei244PhosphoserineCombined sources1
Modified residuei386PhosphothreonineBy similarity1

Post-translational modificationi

Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc finger, the protein is also covalently poly-ADP-ribosylated by PARP1.
Autoubiquitinated; may regulate its cellular level.3 Publications
Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity.2 Publications

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96EP1.
MaxQBiQ96EP1.
PaxDbiQ96EP1.
PeptideAtlasiQ96EP1.
PRIDEiQ96EP1.

PTM databases

iPTMnetiQ96EP1.
PhosphoSitePlusiQ96EP1.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Developmental stagei

Weakly expressed in G1 phase, and highly expressed during S phase.1 Publication

Gene expression databases

BgeeiENSG00000072609.
CleanExiHS_CHFR.
ExpressionAtlasiQ96EP1. baseline and differential.
GenevisibleiQ96EP1. HS.

Interactioni

Subunit structurei

Interacts with HDAC1 and HDAC2. Interacts with PML (with sumoylated form of PML).3 Publications

Protein-protein interaction databases

BioGridi120861. 45 interactors.
DIPiDIP-40098N.
IntActiQ96EP1. 19 interactors.
MINTiMINT-1381330.
STRINGi9606.ENSP00000392395.

Structurei

Secondary structure

1664
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 19Combined sources3
Beta strandi26 – 28Combined sources3
Beta strandi31 – 33Combined sources3
Beta strandi35 – 43Combined sources9
Beta strandi46 – 49Combined sources4
Beta strandi61 – 65Combined sources5
Turni67 – 69Combined sources3
Beta strandi72 – 76Combined sources5
Beta strandi78 – 80Combined sources3
Beta strandi82 – 90Combined sources9
Beta strandi92 – 96Combined sources5
Beta strandi102 – 106Combined sources5
Helixi112 – 114Combined sources3
Beta strandi116 – 119Combined sources4
Helixi433 – 436Combined sources4
Beta strandi482 – 484Combined sources3
Turni486 – 488Combined sources3
Beta strandi491 – 493Combined sources3
Helixi496 – 500Combined sources5
Turni511 – 513Combined sources3
Helixi519 – 522Combined sources4
Beta strandi532 – 535Combined sources4
Helixi536 – 538Combined sources3
Turni543 – 552Combined sources10
Helixi554 – 566Combined sources13
Helixi571 – 583Combined sources13
Beta strandi599 – 601Combined sources3
Helixi602 – 618Combined sources17
Helixi622 – 624Combined sources3
Helixi627 – 630Combined sources4
Helixi638 – 640Combined sources3
Helixi643 – 645Combined sources3
Helixi647 – 652Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LGPX-ray2.00A14-128[»]
1LGQX-ray2.10A/B14-124[»]
2XOCX-ray1.89A/B407-664[»]
2XOYX-ray2.60A/B407-664[»]
2XOZX-ray2.37A/B407-664[»]
2XP0X-ray1.98A/B394-664[»]
ProteinModelPortaliQ96EP1.
SMRiQ96EP1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96EP1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 89FHAPROSITE-ProRule annotationAdd BLAST52

Domaini

The PBZ-type zinc finger (also named CYR) mediates non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and is required for its function in antephase checkpoint.
The FHA domain plays a key role in the anti-proliferative properties of the protein and is involved in initiating a cell cycle arrest at G2/M. The FHA domain may be required to interact with phosphorylated proteins.

Sequence similaritiesi

Belongs to the CHFR family.Curated
Contains 1 FHA domain.PROSITE-ProRule annotation
Contains 1 PBZ-type zinc finger.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri304 – 343RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri633 – 655PBZ-typeAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00400000022306.
HOVERGENiHBG048005.
InParanoidiQ96EP1.
KOiK10644.
OMAiELAYQYR.
OrthoDBiEOG091G03AR.
PhylomeDBiQ96EP1.
TreeFamiTF330957.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96EP1-1) [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
MERPEEGKQS PPPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF
60 70 80 90 100
PSNKLVSGDH CRIVVDEKSG QVTLEDTSTS GTVINKLKVV KKQTCPLQTG
110 120 130 140 150
DVIYLVYRKN EPEHNVAYLY ESLSEKQGMT QESFEANKEN VFHGTKDTSG
160 170 180 190 200
AGAGRGADPR VPPSSPATQV CFEEPQPSTS TSDLFPTASA SSTEPSPAGR
210 220 230 240 250
ERSSSCGSGG GGISPKGSGP SVASDEVSSF ASALPDRKTA SFSSLEPQDQ
260 270 280 290 300
EDLEPVKKKM RGDGDLDLNG QLLVAQPRRN AQTVHEDVRA AAGKPDKMEE
310 320 330 340 350
TLTCIICQDL LHDCVSLQPC MHTFCAACYS GWMERSSLCP TCRCPVERIC
360 370 380 390 400
KNHILNNLVE AYLIQHPDKS RSEEDVQSMD ARNKITQDML QPKVRRSFSD
410 420 430 440 450
EEGSSEDLLE LSDVDSESSD ISQPYVVCRQ CPEYRRQAAQ PPHCPAPEGE
460 470 480 490 500
PGAPQALGDA PSTSVSLTTA VQDYVCPLQG SHALCTCCFQ PMPDRRAERE
510 520 530 540 550
QDPRVAPQQC AVCLQPFCHL YWGCTRTGCY GCLAPFCELN LGDKCLDGVL
560 570 580 590 600
NNNSYESDIL KNYLATRGLT WKNMLTESLV ALQRGVFLLS DYRVTGDTVL
610 620 630 640 650
CYCCGLRSFR ELTYQYRQNI PASELPVAVT SRPDCYWGRN CRTQVKAHHA
660
MKFNHICEQT RFKN
Length:664
Mass (Da):73,386
Last modified:February 2, 2004 - v2
Checksum:i141A1E7FEFAE36A2
GO
Isoform 2 (identifier: Q96EP1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-146: Missing.

Show »
Length:652
Mass (Da):72,031
Checksum:i572F2CE6D1743D80
GO
Isoform 3 (identifier: Q96EP1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-206: ANKENVFHGT...PAGRERSSSC → MVPCCVAQAGLKLLGSSDPPTLASQSIVIT

Show »
Length:623
Mass (Da):69,192
Checksum:iB747CD23B74368E7
GO
Isoform 4 (identifier: Q96EP1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     470-470: Missing.

Show »
Length:663
Mass (Da):73,315
Checksum:i302207777755B60C
GO
Isoform 5 (identifier: Q96EP1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-207: NVAYLYESLS...AGRERSSSCG → R

Note: No experimental confirmation available.
Show »
Length:572
Mass (Da):63,873
Checksum:iC3CFDEF89A9C85B7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti256V → E in BAA91817 (PubMed:14702039).Curated1
Sequence conflicti462S → P in BAA91817 (PubMed:14702039).Curated1
Sequence conflicti599V → A in BAG65178 (PubMed:14702039).Curated1
Sequence conflicti617R → Q in BAA91817 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017582166P → L in a patient with non small cell lung carcinomas; homozygous. 1 Publication1
Natural variantiVAR_017583202R → P in a patient with non small cell lung carcinomas. 1 Publication1
Natural variantiVAR_017584270G → R.1 PublicationCorresponds to variant rs115096950dbSNPEnsembl.1
Natural variantiVAR_017585497A → V Common polymorphism. 2 PublicationsCorresponds to variant rs2306541dbSNPEnsembl.1
Natural variantiVAR_017586536F → S in a patient with non small cell lung carcinomas. 1 Publication1
Natural variantiVAR_017587580V → M Common polymorphism. 3 PublicationsCorresponds to variant rs2306536dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_038126115 – 207NVAYL…SSSCG → R in isoform 5. CuratedAdd BLAST93
Alternative sequenceiVSP_009349135 – 146Missing in isoform 2. 2 PublicationsAdd BLAST12
Alternative sequenceiVSP_009350136 – 206ANKEN…RSSSC → MVPCCVAQAGLKLLGSSDPP TLASQSIVIT in isoform 3. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_038127470Missing in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170724 mRNA. Translation: AAF91084.1.
AK001658 mRNA. Translation: BAA91817.1.
AK027687 mRNA. Translation: BAB55297.1.
AK302785 mRNA. Translation: BAG63989.1.
AK304333 mRNA. Translation: BAG65178.1.
AC127070 Genomic DNA. No translation available.
BC012072 mRNA. Translation: AAH12072.1.
AL137561 mRNA. Translation: CAB70812.1.
CCDSiCCDS31937.1. [Q96EP1-3]
CCDS53847.1. [Q96EP1-5]
CCDS53848.1. [Q96EP1-2]
CCDS53849.1. [Q96EP1-1]
PIRiT46399.
RefSeqiNP_001154816.1. NM_001161344.1. [Q96EP1-1]
NP_001154817.1. NM_001161345.1. [Q96EP1-4]
NP_001154818.1. NM_001161346.1. [Q96EP1-2]
NP_001154819.1. NM_001161347.1. [Q96EP1-5]
NP_060693.2. NM_018223.2. [Q96EP1-3]
UniGeneiHs.720197.

Genome annotation databases

EnsembliENST00000266880; ENSP00000266880; ENSG00000072609. [Q96EP1-3]
ENST00000432561; ENSP00000392395; ENSG00000072609. [Q96EP1-1]
ENST00000443047; ENSP00000416431; ENSG00000072609. [Q96EP1-5]
ENST00000450056; ENSP00000398735; ENSG00000072609. [Q96EP1-2]
GeneIDi55743.
KEGGihsa:55743.
UCSCiuc001uld.3. human. [Q96EP1-1]

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
AF170724 mRNA. Translation: AAF91084.1.
AK001658 mRNA. Translation: BAA91817.1.
AK027687 mRNA. Translation: BAB55297.1.
AK302785 mRNA. Translation: BAG63989.1.
AK304333 mRNA. Translation: BAG65178.1.
AC127070 Genomic DNA. No translation available.
BC012072 mRNA. Translation: AAH12072.1.
AL137561 mRNA. Translation: CAB70812.1.
CCDSiCCDS31937.1. [Q96EP1-3]
CCDS53847.1. [Q96EP1-5]
CCDS53848.1. [Q96EP1-2]
CCDS53849.1. [Q96EP1-1]
PIRiT46399.
RefSeqiNP_001154816.1. NM_001161344.1. [Q96EP1-1]
NP_001154817.1. NM_001161345.1. [Q96EP1-4]
NP_001154818.1. NM_001161346.1. [Q96EP1-2]
NP_001154819.1. NM_001161347.1. [Q96EP1-5]
NP_060693.2. NM_018223.2. [Q96EP1-3]
UniGeneiHs.720197.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LGPX-ray2.00A14-128[»]
1LGQX-ray2.10A/B14-124[»]
2XOCX-ray1.89A/B407-664[»]
2XOYX-ray2.60A/B407-664[»]
2XOZX-ray2.37A/B407-664[»]
2XP0X-ray1.98A/B394-664[»]
ProteinModelPortaliQ96EP1.
SMRiQ96EP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120861. 45 interactors.
DIPiDIP-40098N.
IntActiQ96EP1. 19 interactors.
MINTiMINT-1381330.
STRINGi9606.ENSP00000392395.

PTM databases

iPTMnetiQ96EP1.
PhosphoSitePlusiQ96EP1.

Polymorphism and mutation databases

BioMutaiCHFR.
DMDMi41688511.

Proteomic databases

EPDiQ96EP1.
MaxQBiQ96EP1.
PaxDbiQ96EP1.
PeptideAtlasiQ96EP1.
PRIDEiQ96EP1.

Protocols and materials databases

DNASUi55743.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266880; ENSP00000266880; ENSG00000072609. [Q96EP1-3]
ENST00000432561; ENSP00000392395; ENSG00000072609. [Q96EP1-1]
ENST00000443047; ENSP00000416431; ENSG00000072609. [Q96EP1-5]
ENST00000450056; ENSP00000398735; ENSG00000072609. [Q96EP1-2]
GeneIDi55743.
KEGGihsa:55743.
UCSCiuc001uld.3. human. [Q96EP1-1]

Organism-specific databases

CTDi55743.
DisGeNETi55743.
GeneCardsiCHFR.
HGNCiHGNC:20455. CHFR.
MIMi605209. gene.
neXtProtiNX_Q96EP1.
OpenTargetsiENSG00000072609.
PharmGKBiPA134898949.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00400000022306.
HOVERGENiHBG048005.
InParanoidiQ96EP1.
KOiK10644.
OMAiELAYQYR.
OrthoDBiEOG091G03AR.
PhylomeDBiQ96EP1.
TreeFamiTF330957.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiCHFR. human.
EvolutionaryTraceiQ96EP1.
GeneWikiiCHFR.
GenomeRNAii55743.
PROiQ96EP1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000072609.
CleanExiHS_CHFR.
ExpressionAtlasiQ96EP1. baseline and differential.
GenevisibleiQ96EP1. HS.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHFR_HUMAN
AccessioniPrimary (citable) accession number: Q96EP1
Secondary accession number(s): A6NEN5
, B4DZ77, B4E2L6, Q96SL3, Q9NRT4, Q9NT32, Q9NVD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: November 2, 2016
This is version 150 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

Miscellaneous

CHFR is silenced in many primary cancers because of CpG methylation and deacetylated histones on its promoter region. This however raises the question of whether CHFR silencing is a consequence or a cause of primary cancers.

Keywords - Technical termi

3D-structure, Complete proteome, 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.