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Protein

Ubiquitin carboxyl-terminal hydrolase 2

Gene

USP2

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

Functioni

Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1 (By similarity).By similarity3 Publications

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Cofactori

Zn2+Note: Binds 1 zinc ion.1 Publication

Enzyme regulationi

Cleavage is inhibited by ubiquitin in a dosage-dependent manner. Cleavage is blocked by ubiquitin aldehyde.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei276NucleophilePROSITE-ProRule annotation1
Metal bindingi425Zinc1 Publication1
Metal bindingi428Zinc1 Publication1
Metal bindingi476Zinc1 Publication1
Metal bindingi479Zinc1 Publication1
Active sitei557Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • cyclin binding Source: UniProtKB
  • cysteine-type endopeptidase activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • thiol-dependent ubiquitin-specific protease activity Source: FlyBase
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Biological rhythms, Cell cycle, Myogenesis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS00519-MONOMER.
ReactomeiR-HSA-5357786. TNFR1-induced proapoptotic signaling.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-6804757. Regulation of TP53 Degradation.

Protein family/group databases

MEROPSiC19.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 2 (EC:3.4.19.12)
Alternative name(s):
41 kDa ubiquitin-specific protease
Deubiquitinating enzyme 2
Ubiquitin thioesterase 2
Ubiquitin-specific-processing protease 2
Gene namesi
Name:USP2
Synonyms:UBP41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:12618. USP2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmperinuclear region By similarity

  • Note: Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane.By similarity
Isoform 4 :
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi276C → A: Loss of enzymatic activity. Increases the steady-state level of CCND1. 1 Publication1
Mutagenesisi549H → A: Loss of enzymatic activity. Increases the steady-state level of MDM2 and MDM4 that leads to attenuation of MDM2-mediated degradation of p53/TP53 and MDM4. Increases the level of p53/TP53 and MDM4 ubiquitin conjugates. 2 Publications1

Organism-specific databases

DisGeNETi9099.
OpenTargetsiENSG00000036672.
PharmGKBiPA37244.

Chemistry databases

ChEMBLiCHEMBL1293227.

Polymorphism and mutation databases

BioMutaiUSP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000806161 – 605Ubiquitin carboxyl-terminal hydrolase 2Add BLAST605

Proteomic databases

MaxQBiO75604.
PaxDbiO75604.
PeptideAtlasiO75604.
PRIDEiO75604.

PTM databases

iPTMnetiO75604.
PhosphoSitePlusiO75604.

Expressioni

Tissue specificityi

Expressed in mesangial cells of the kidney and in different types of glomerulonephritides (at protein level).1 Publication

Inductioni

Down-regulated by cisplatin (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000036672.
CleanExiHS_USP2.
ExpressionAtlasiO75604. baseline and differential.
GenevisibleiO75604. HS.

Organism-specific databases

HPAiHPA006777.
HPA007222.

Interactioni

Subunit structurei

Homooligomer (By similarity). Found in trimeric complex with MDM2 and MDM4 and USP2. Interacts with CCND1; the interaction is direct and promotes its stabilization by antagonizing ubiquitin-dependent degradation. Interacts (via N-terminus and C-terminus) with MDM2. Interacts with MDM4. Interacts with PER1 (By similarity). Interacts with KCNQ1; counteracts the NEDD4L-specific down-regulation of I(Ks) and restore plasma membrane localization of KCNQ1 (PubMed:22024150).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC136Q96JN2-23EBI-743272,EBI-10171416
CCDC36Q8IYA83EBI-743272,EBI-8638439
CCDC57Q2TAC23EBI-743272,EBI-2808286
GOLGA2Q083793EBI-743272,EBI-618309
HOMER3B2RA103EBI-743272,EBI-10175777
HOOK1Q9UJC33EBI-743272,EBI-746704
KIFC3Q9BVG83EBI-743272,EBI-2125614
KRT15P190125EBI-743272,EBI-739566
KRT40Q6A1623EBI-743272,EBI-10171697
LHX4Q969G23EBI-743272,EBI-2865388
LZTS2Q9BRK45EBI-743272,EBI-741037
MDM2Q009874EBI-743272,EBI-389668
MTUS2Q5JR593EBI-743272,EBI-742948
NDEL1Q9GZM85EBI-743272,EBI-928842
NEFLI6L9F63EBI-743272,EBI-10178578
PNMA1Q8ND903EBI-743272,EBI-302345
TRAF2Q129336EBI-743272,EBI-355744
TRAF6Q9Y4K33EBI-743272,EBI-359276
TRIM27P143735EBI-743272,EBI-719493
VPS52Q8N1B45EBI-743272,EBI-2799833

GO - Molecular functioni

  • cyclin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114553. 101 interactors.
DIPiDIP-29134N.
IntActiO75604. 82 interactors.
MINTiMINT-4304073.
STRINGi9606.ENSP00000260187.

Chemistry databases

BindingDBiO75604.

Structurei

Secondary structure

1605
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi272 – 274Combined sources3
Helixi276 – 286Combined sources11
Helixi289 – 296Combined sources8
Helixi299 – 302Combined sources4
Helixi312 – 325Combined sources14
Helixi337 – 346Combined sources10
Helixi348 – 350Combined sources3
Beta strandi351 – 353Combined sources3
Helixi358 – 373Combined sources16
Helixi392 – 404Combined sources13
Helixi410 – 415Combined sources6
Beta strandi417 – 425Combined sources9
Turni426 – 428Combined sources3
Beta strandi431 – 443Combined sources13
Helixi455 – 463Combined sources9
Beta strandi466 – 468Combined sources3
Helixi470 – 472Combined sources3
Turni477 – 480Combined sources4
Beta strandi485 – 493Combined sources9
Beta strandi496 – 502Combined sources7
Helixi529 – 531Combined sources3
Beta strandi532 – 536Combined sources5
Beta strandi540 – 551Combined sources12
Beta strandi553 – 555Combined sources3
Beta strandi556 – 563Combined sources8
Turni565 – 567Combined sources3
Beta strandi570 – 574Combined sources5
Beta strandi577 – 581Combined sources5
Helixi583 – 585Combined sources3
Beta strandi591 – 598Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HD5X-ray1.85A258-605[»]
2IBIX-ray2.20A251-605[»]
3NHEX-ray1.26A258-605[»]
3V6CX-ray1.70A258-605[»]
3V6EX-ray2.10A258-605[»]
ProteinModelPortaliO75604.
SMRiO75604.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75604.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini267 – 599USPAdd BLAST333

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 200Necessary for interaction with MDM41 PublicationAdd BLAST200
Regioni403 – 503Necessary for interaction with MDM41 PublicationAdd BLAST101

Domaini

The different N-terminus extensions of isoform 1 and isoform 4 determine their respective subcellular localization and differentiel effect on myoblast fusion and accumulation of muscle-specific proteins. The different N-terminus extensions of isoform 1 and isoform 4 are not essential for their catalytic activity.By similarity

Sequence similaritiesi

Belongs to the peptidase C19 family. USP2 subfamily.Curated
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiKOG1868. Eukaryota.
ENOG410XP8T. LUCA.
GeneTreeiENSGT00860000133682.
HOGENOMiHOG000231498.
HOVERGENiHBG011164.
InParanoidiO75604.
KOiK11833.
OMAiMRTSYTV.
OrthoDBiEOG091G0120.
PhylomeDBiO75604.
TreeFamiTF106277.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75604-1) [UniParc]FASTAAdd to basket
Also known as: USP2a, USP2-69

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
MSQLSSTLKR YTESARYTDA HYAKSGYGAY TPSSYGANLA ASLLEKEKLG
60 70 80 90 100
FKPVPTSSFL TRPRTYGPSS LLDYDRGRPL LRPDITGGGK RAESQTRGTE
110 120 130 140 150
RPLGSGLSGG SGFPYGVTNN CLSYLPINAY DQGVTLTQKL DSQSDLARDF
160 170 180 190 200
SSLRTSDSYR IDPRNLGRSP MLARTRKELC TLQGLYQTAS CPEYLVDYLE
210 220 230 240 250
NYGRKGSASQ VPSQAPPSRV PEIISPTYRP IGRYTLWETG KGQAPGPSRS
260 270 280 290 300
SSPGRDGMNS KSAQGLAGLR NLGNTCFMNS ILQCLSNTRE LRDYCLQRLY
310 320 330 340 350
MRDLHHGSNA HTALVEEFAK LIQTIWTSSP NDVVSPSEFK TQIQRYAPRF
360 370 380 390 400
VGYNQQDAQE FLRFLLDGLH NEVNRVTLRP KSNPENLDHL PDDEKGRQMW
410 420 430 440 450
RKYLEREDSR IGDLFVGQLK SSLTCTDCGY CSTVFDPFWD LSLPIAKRGY
460 470 480 490 500
PEVTLMDCMR LFTKEDVLDG DEKPTCCRCR GRKRCIKKFS IQRFPKILVL
510 520 530 540 550
HLKRFSESRI RTSKLTTFVN FPLRDLDLRE FASENTNHAV YNLYAVSNHS
560 570 580 590 600
GTTMGGHYTA YCRSPGTGEW HTFNDSSVTP MSSSQVRTSD AYLLFYELAS

PPSRM
Length:605
Mass (Da):68,072
Last modified:March 27, 2002 - v2
Checksum:iAFF4DA9344D21812
GO
Isoform 2 (identifier: O75604-2) [UniParc]FASTAAdd to basket
Also known as: USP2b

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.
     253-258: PGRDGM → MLNKAK

Note: No experimental confirmation available.
Show »
Length:353
Mass (Da):40,638
Checksum:i7CDF2F9A300B864F
GO
Isoform 3 (identifier: O75604-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-258: MSQLSSTLKR...RSSSPGRDGM → MLVPGSTRPYSKKRQ

Show »
Length:362
Mass (Da):41,682
Checksum:i5C93CA5F03D43293
GO
Isoform 4 (identifier: O75604-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-258: MSQLSSTLKR...RSSSPGRDGM → MRTSYTVTLP...FVGLLLNKAK

Show »
Length:396
Mass (Da):45,241
Checksum:i2A5B0403419F0655
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti421S → G in BAB71388 (PubMed:14702039).Curated1
Sequence conflicti501H → R in BAB71388 (PubMed:14702039).Curated1
Sequence conflicti594L → H in AAC28392 (Ref. 1) Curated1
Sequence conflicti602 – 605PSRM → TSPI in AAC28392 (Ref. 1) Curated4
Isoform 3 (identifier: O75604-3)
Sequence conflicti10Y → S in AAH41366 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051519174R → Q.Corresponds to variant rs33929148dbSNPEnsembl.1
Natural variantiVAR_051520383N → S.Corresponds to variant rs45533837dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0395591 – 258MSQLS…GRDGM → MLVPGSTRPYSKKRQ in isoform 3. 1 PublicationAdd BLAST258
Alternative sequenceiVSP_0395601 – 258MSQLS…GRDGM → MRTSYTVTLPEDPPAAPFPA LAKELRPRSPLSPSLLLSTF VGLLLNKAK in isoform 4. 2 PublicationsAdd BLAST258
Alternative sequenceiVSP_0052561 – 252Missing in isoform 2. 1 PublicationAdd BLAST252
Alternative sequenceiVSP_005257253 – 258PGRDGM → MLNKAK in isoform 2. 1 Publication6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079564 mRNA. Translation: AAC28392.1.
AF440755 mRNA. Translation: AAN65363.1.
AK057225 mRNA. Translation: BAB71388.1.
AK292255 mRNA. Translation: BAF84944.1.
EF445044 Genomic DNA. Translation: ACA06096.1.
EF445044 Genomic DNA. Translation: ACA06097.1.
AP003396 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67484.1.
CH471065 Genomic DNA. Translation: EAW67485.1.
CH471065 Genomic DNA. Translation: EAW67486.1.
BC002854 mRNA. Translation: AAH02854.1.
BC002955 mRNA. Translation: AAH02955.1.
BC041366 mRNA. Translation: AAH41366.1.
CCDSiCCDS58189.1. [O75604-3]
CCDS8422.1. [O75604-1]
CCDS8423.1. [O75604-4]
RefSeqiNP_001230688.1. NM_001243759.1. [O75604-3]
NP_004196.4. NM_004205.4. [O75604-1]
NP_741994.1. NM_171997.2. [O75604-4]
XP_005271778.1. XM_005271721.4. [O75604-1]
XP_005271779.1. XM_005271722.2. [O75604-1]
UniGeneiHs.524085.

Genome annotation databases

EnsembliENST00000260187; ENSP00000260187; ENSG00000036672. [O75604-1]
ENST00000455332; ENSP00000407842; ENSG00000036672. [O75604-3]
ENST00000525735; ENSP00000436952; ENSG00000036672. [O75604-4]
GeneIDi9099.
KEGGihsa:9099.
UCSCiuc001pwl.5. human. [O75604-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079564 mRNA. Translation: AAC28392.1.
AF440755 mRNA. Translation: AAN65363.1.
AK057225 mRNA. Translation: BAB71388.1.
AK292255 mRNA. Translation: BAF84944.1.
EF445044 Genomic DNA. Translation: ACA06096.1.
EF445044 Genomic DNA. Translation: ACA06097.1.
AP003396 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67484.1.
CH471065 Genomic DNA. Translation: EAW67485.1.
CH471065 Genomic DNA. Translation: EAW67486.1.
BC002854 mRNA. Translation: AAH02854.1.
BC002955 mRNA. Translation: AAH02955.1.
BC041366 mRNA. Translation: AAH41366.1.
CCDSiCCDS58189.1. [O75604-3]
CCDS8422.1. [O75604-1]
CCDS8423.1. [O75604-4]
RefSeqiNP_001230688.1. NM_001243759.1. [O75604-3]
NP_004196.4. NM_004205.4. [O75604-1]
NP_741994.1. NM_171997.2. [O75604-4]
XP_005271778.1. XM_005271721.4. [O75604-1]
XP_005271779.1. XM_005271722.2. [O75604-1]
UniGeneiHs.524085.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HD5X-ray1.85A258-605[»]
2IBIX-ray2.20A251-605[»]
3NHEX-ray1.26A258-605[»]
3V6CX-ray1.70A258-605[»]
3V6EX-ray2.10A258-605[»]
ProteinModelPortaliO75604.
SMRiO75604.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114553. 101 interactors.
DIPiDIP-29134N.
IntActiO75604. 82 interactors.
MINTiMINT-4304073.
STRINGi9606.ENSP00000260187.

Chemistry databases

BindingDBiO75604.
ChEMBLiCHEMBL1293227.

Protein family/group databases

MEROPSiC19.013.

PTM databases

iPTMnetiO75604.
PhosphoSitePlusiO75604.

Polymorphism and mutation databases

BioMutaiUSP2.

Proteomic databases

MaxQBiO75604.
PaxDbiO75604.
PeptideAtlasiO75604.
PRIDEiO75604.

Protocols and materials databases

DNASUi9099.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260187; ENSP00000260187; ENSG00000036672. [O75604-1]
ENST00000455332; ENSP00000407842; ENSG00000036672. [O75604-3]
ENST00000525735; ENSP00000436952; ENSG00000036672. [O75604-4]
GeneIDi9099.
KEGGihsa:9099.
UCSCiuc001pwl.5. human. [O75604-1]

Organism-specific databases

CTDi9099.
DisGeNETi9099.
GeneCardsiUSP2.
HGNCiHGNC:12618. USP2.
HPAiHPA006777.
HPA007222.
MIMi604725. gene.
neXtProtiNX_O75604.
OpenTargetsiENSG00000036672.
PharmGKBiPA37244.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1868. Eukaryota.
ENOG410XP8T. LUCA.
GeneTreeiENSGT00860000133682.
HOGENOMiHOG000231498.
HOVERGENiHBG011164.
InParanoidiO75604.
KOiK11833.
OMAiMRTSYTV.
OrthoDBiEOG091G0120.
PhylomeDBiO75604.
TreeFamiTF106277.

Enzyme and pathway databases

BioCyciZFISH:HS00519-MONOMER.
ReactomeiR-HSA-5357786. TNFR1-induced proapoptotic signaling.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-6804757. Regulation of TP53 Degradation.

Miscellaneous databases

ChiTaRSiUSP2. human.
EvolutionaryTraceiO75604.
GeneWikiiUSP2.
GenomeRNAii9099.
PROiO75604.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000036672.
CleanExiHS_USP2.
ExpressionAtlasiO75604. baseline and differential.
GenevisibleiO75604. HS.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBP2_HUMAN
AccessioniPrimary (citable) accession number: O75604
Secondary accession number(s): B0YJB8
, E9PPM2, Q8IUM2, Q8IW04, Q96MB9, Q9BQ21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 27, 2002
Last modified: November 30, 2016
This is version 157 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 11
    Human chromosome 11: 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. Peptidase families
    Classification of peptidase families and list of 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.