Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell division cycle protein 23 homolog

Gene

CDC23

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

Functioni

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.1 Publication

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.

GO - Molecular functioni

  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ9UJX2.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 23 homolog
Alternative name(s):
Anaphase-promoting complex subunit 8
Short name:
APC8
Cyclosome subunit 8
Gene namesi
Name:CDC23
Synonyms:ANAPC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:1724. CDC23.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • intracellular Source: LIFEdb
  • nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi8697.
OpenTargetsiENSG00000094880.
PharmGKBiPA26258.

Polymorphism and mutation databases

BioMutaiCDC23.
DMDMi254763423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001062702 – 597Cell division cycle protein 23 homologAdd BLAST596

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Cross-linki147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei273Phosphotyrosine1 Publication1
Modified residuei467N6-acetyllysineCombined sources1
Modified residuei562PhosphothreonineCombined sources1 Publication1
Modified residuei565Phosphothreonine1 Publication1
Modified residuei578PhosphoserineCombined sources1
Modified residuei582PhosphothreonineCombined sources1
Modified residuei588PhosphoserineCombined sources1
Modified residuei593PhosphoserineCombined sources1
Modified residuei596PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated. Phosphorylation on Thr-562 occurs specifically during mitosis.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UJX2.
PaxDbiQ9UJX2.
PeptideAtlasiQ9UJX2.
PRIDEiQ9UJX2.

PTM databases

iPTMnetiQ9UJX2.
PhosphoSitePlusiQ9UJX2.

Expressioni

Gene expression databases

BgeeiENSG00000094880.
CleanExiHS_CDC23.
ExpressionAtlasiQ9UJX2. baseline and differential.
GenevisibleiQ9UJX2. HS.

Organism-specific databases

HPAiHPA039593.

Interactioni

Subunit structurei

The mammalian APC/C is composed of 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANAPC13A8K3Z63EBI-396137,EBI-10322710
ANAPC13Q9BS185EBI-396137,EBI-2555953
APOL1O147913EBI-396137,EBI-1221934
ATRIPQ8WXE13EBI-396137,EBI-747353
BCAS3Q9H6U63EBI-396137,EBI-6083685
BYSLQ138955EBI-396137,EBI-358049
CCDC24Q8N4L83EBI-396137,EBI-1104933
CCDC36Q8IYA85EBI-396137,EBI-8638439
CEP44Q9C0F13EBI-396137,EBI-744115
COILP384323EBI-396137,EBI-945751
CRACR2AQ9BSW23EBI-396137,EBI-739773
CYB5R2Q6BCY43EBI-396137,EBI-744761
EIF5A2Q9GZV43EBI-396137,EBI-748028
FAM9BQ8IZU03EBI-396137,EBI-10175124
FLJ34048A4D1I33EBI-396137,EBI-10173415
FSBPO950733EBI-396137,EBI-1059030
GORASP2Q9H8Y85EBI-396137,EBI-739467
HEMK1Q9Y5R43EBI-396137,EBI-10329202
INCA1Q0VD863EBI-396137,EBI-6509505
INPP5JQ157353EBI-396137,EBI-10236940
KCTD6Q8NC695EBI-396137,EBI-2511344
LZTS2Q9BRK43EBI-396137,EBI-741037
OPTNQ96CV94EBI-396137,EBI-748974
PNMA5Q96PV43EBI-396137,EBI-10171633
RAC1P630003EBI-396137,EBI-413628
RBM15BQ8NDT2-23EBI-396137,EBI-10269922
RBPMSQ930624EBI-396137,EBI-740322
RSL24D1Q9UHA33EBI-396137,EBI-749321
SIAH1Q8IUQ43EBI-396137,EBI-747107
SLC52A2Q9HAB33EBI-396137,EBI-10309896
SOX5P357113EBI-396137,EBI-3505701
SPERTQ8NA613EBI-396137,EBI-741724
SSX2IPQ9Y2D83EBI-396137,EBI-2212028
TRIM27P143734EBI-396137,EBI-719493
TSC22D4Q9Y3Q83EBI-396137,EBI-739485

Protein-protein interaction databases

BioGridi114242. 127 interactors.
DIPiDIP-32959N.
IntActiQ9UJX2. 111 interactors.
MINTiMINT-1437590.
STRINGi9606.ENSP00000378350.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60C/P7-597[»]
5A31electron microscopy4.30C/P1-597[»]
5G04electron microscopy4.00C/P1-597[»]
5G05electron microscopy3.40C/P1-597[»]
5KHRelectron microscopy6.10C/P1-597[»]
5L9Uelectron microscopy6.40C/P1-597[»]
5LCWelectron microscopy4.00C/P1-597[»]
ProteinModelPortaliQ9UJX2.
SMRiQ9UJX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati27 – 63TPR 1Add BLAST37
Repeati73 – 112TPR 2Add BLAST40
Repeati114 – 144TPR 3Add BLAST31
Repeati169 – 200TPR 4Add BLAST32
Repeati229 – 259TPR 5Add BLAST31
Repeati263 – 293TPR 6Add BLAST31
Repeati297 – 327TPR 7Add BLAST31
Repeati331 – 361TPR 8Add BLAST31
Repeati366 – 395TPR 9Add BLAST30
Repeati400 – 432TPR 10Add BLAST33
Repeati433 – 466TPR 11Add BLAST34
Repeati468 – 500TPR 12Add BLAST33
Repeati504 – 540TPR 13Add BLAST37

Sequence similaritiesi

Belongs to the APC8/CDC23 family.Curated
Contains 13 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1155. Eukaryota.
ENOG410XPS3. LUCA.
GeneTreeiENSGT00550000074886.
HOVERGENiHBG050858.
InParanoidiQ9UJX2.
KOiK03355.
OMAiEDEMEWE.
OrthoDBiEOG091G0535.
PhylomeDBiQ9UJX2.
TreeFamiTF101055.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR007192. APC8.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04049. ANAPC8. 1 hit.
PF13414. TPR_11. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 7 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 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: Q9UJX2-1) [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
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH
60 70 80 90 100
SSKWSAELAF SLPALPLAEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD
110 120 130 140 150
RAAHFLHGCN SKKAYFLYMY SRYLSGEKKK DDETVDSLGP LEKGQVKNEA
160 170 180 190 200
LRELRVELSK KHQARELDGF GLYLYGVVLR KLDLVKEAID VFVEATHVLP
210 220 230 240 250
LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE LQLIEEALQK
260 270 280 290 300
YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM
310 320 330 340 350
DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA
360 370 380 390 400
ALYFQRALKL NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR
410 420 430 440 450
AWYGLGQTYE ILKMPFYCLY YYRRAHQLRP NDSRMLVALG ECYEKLNQLV
460 470 480 490 500
EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL TESEQAAQCY IKYIQDIYSC
510 520 530 540 550
GEIVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN DTREEGKALL
560 570 580 590
RQILQLRNQG ETPTTEVPAP FFLPASLSAN NTPTRRVSPL NLSSVTP
Length:597
Mass (Da):68,834
Last modified:July 28, 2009 - v3
Checksum:i358F2B8745DB9D32
GO
Isoform 2 (identifier: Q9UJX2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-151: SGEKKKDDETVDSLGPLEKGQVKNEAL → VRAILKCHSAFSETSIFRTNGKVKSFK
     152-597: Missing.

Note: No experimental confirmation available.
Show »
Length:151
Mass (Da):16,821
Checksum:i0FE42406F299DAD4
GO
Isoform 3 (identifier: Q9UJX2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Note: No experimental confirmation available.
Show »
Length:479
Mass (Da):55,882
Checksum:i1E4655ABEAAB2D9A
GO

Sequence cautioni

The sequence AAC70920 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH05258 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH10944 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH17713 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAS99353 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA75628 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAD96970 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAF84299 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti83D → E in BAD96970 (Ref. 4) Curated1
Sequence conflicti105F → S in BAD96970 (Ref. 4) Curated1
Sequence conflicti527D → G in BAG65414 (PubMed:14702039).Curated1
Sequence conflicti588S → F in AAF05755 (PubMed:9469815).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0246759P → L.Corresponds to variant rs2231471dbSNPEnsembl.1
Natural variantiVAR_01923278E → Q.1 PublicationCorresponds to variant rs17228304dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0376781 – 118Missing in isoform 3. 1 PublicationAdd BLAST118
Alternative sequenceiVSP_008429125 – 151SGEKK…KNEAL → VRAILKCHSAFSETSIFRTN GKVKSFK in isoform 2. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_008430152 – 597Missing in isoform 2. 1 PublicationAdd BLAST446

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011472 mRNA. Translation: BAA75628.1. Different initiation.
AK291610 mRNA. Translation: BAF84299.1. Different initiation.
AK304635 mRNA. Translation: BAG65414.1.
AY603103 Genomic DNA. Translation: AAS99353.1. Different initiation.
AK223250 mRNA. Translation: BAD96970.1. Different initiation.
AC106752 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62155.1.
CH471062 Genomic DNA. Translation: EAW62154.1.
CH471062 Genomic DNA. Translation: EAW62156.1.
BC005258 mRNA. Translation: AAH05258.1. Different initiation.
BC010944 mRNA. Translation: AAH10944.1. Different initiation.
BC017713 mRNA. Translation: AAH17713.1. Different initiation.
AF053977 mRNA. Translation: AAC70920.1. Different initiation.
AF191341 mRNA. Translation: AAF05755.1.
BT009810 mRNA. Translation: AAP88812.1.
CCDSiCCDS4200.2. [Q9UJX2-1]
PIRiT51168.
RefSeqiNP_004652.2. NM_004661.3. [Q9UJX2-1]
UniGeneiHs.73625.

Genome annotation databases

EnsembliENST00000394884; ENSP00000378348; ENSG00000094880. [Q9UJX2-2]
ENST00000394886; ENSP00000378350; ENSG00000094880. [Q9UJX2-1]
GeneIDi8697.
KEGGihsa:8697.
UCSCiuc003lcl.3. human. [Q9UJX2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011472 mRNA. Translation: BAA75628.1. Different initiation.
AK291610 mRNA. Translation: BAF84299.1. Different initiation.
AK304635 mRNA. Translation: BAG65414.1.
AY603103 Genomic DNA. Translation: AAS99353.1. Different initiation.
AK223250 mRNA. Translation: BAD96970.1. Different initiation.
AC106752 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62155.1.
CH471062 Genomic DNA. Translation: EAW62154.1.
CH471062 Genomic DNA. Translation: EAW62156.1.
BC005258 mRNA. Translation: AAH05258.1. Different initiation.
BC010944 mRNA. Translation: AAH10944.1. Different initiation.
BC017713 mRNA. Translation: AAH17713.1. Different initiation.
AF053977 mRNA. Translation: AAC70920.1. Different initiation.
AF191341 mRNA. Translation: AAF05755.1.
BT009810 mRNA. Translation: AAP88812.1.
CCDSiCCDS4200.2. [Q9UJX2-1]
PIRiT51168.
RefSeqiNP_004652.2. NM_004661.3. [Q9UJX2-1]
UniGeneiHs.73625.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60C/P7-597[»]
5A31electron microscopy4.30C/P1-597[»]
5G04electron microscopy4.00C/P1-597[»]
5G05electron microscopy3.40C/P1-597[»]
5KHRelectron microscopy6.10C/P1-597[»]
5L9Uelectron microscopy6.40C/P1-597[»]
5LCWelectron microscopy4.00C/P1-597[»]
ProteinModelPortaliQ9UJX2.
SMRiQ9UJX2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114242. 127 interactors.
DIPiDIP-32959N.
IntActiQ9UJX2. 111 interactors.
MINTiMINT-1437590.
STRINGi9606.ENSP00000378350.

PTM databases

iPTMnetiQ9UJX2.
PhosphoSitePlusiQ9UJX2.

Polymorphism and mutation databases

BioMutaiCDC23.
DMDMi254763423.

Proteomic databases

EPDiQ9UJX2.
PaxDbiQ9UJX2.
PeptideAtlasiQ9UJX2.
PRIDEiQ9UJX2.

Protocols and materials databases

DNASUi8697.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394884; ENSP00000378348; ENSG00000094880. [Q9UJX2-2]
ENST00000394886; ENSP00000378350; ENSG00000094880. [Q9UJX2-1]
GeneIDi8697.
KEGGihsa:8697.
UCSCiuc003lcl.3. human. [Q9UJX2-1]

Organism-specific databases

CTDi8697.
DisGeNETi8697.
GeneCardsiCDC23.
H-InvDBHIX0005208.
HGNCiHGNC:1724. CDC23.
HPAiHPA039593.
MIMi603462. gene.
neXtProtiNX_Q9UJX2.
OpenTargetsiENSG00000094880.
PharmGKBiPA26258.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1155. Eukaryota.
ENOG410XPS3. LUCA.
GeneTreeiENSGT00550000074886.
HOVERGENiHBG050858.
InParanoidiQ9UJX2.
KOiK03355.
OMAiEDEMEWE.
OrthoDBiEOG091G0535.
PhylomeDBiQ9UJX2.
TreeFamiTF101055.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ9UJX2.

Miscellaneous databases

ChiTaRSiCDC23. human.
GeneWikiiCDC23.
GenomeRNAii8697.
PROiQ9UJX2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000094880.
CleanExiHS_CDC23.
ExpressionAtlasiQ9UJX2. baseline and differential.
GenevisibleiQ9UJX2. HS.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR007192. APC8.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04049. ANAPC8. 1 hit.
PF13414. TPR_11. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 7 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDC23_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX2
Secondary accession number(s): A8K6E5
, B4E3A2, B7WP05, D3DQB7, O75433, Q53FN2, Q9BS73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: July 28, 2009
Last modified: November 30, 2016
This is version 160 of the entry and version 3 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 5
    Human chromosome 5: 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.