Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P45974 (UBP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 5

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 5
Isopeptidase T
Ubiquitin thioesterase 5
Ubiquitin-specific-processing protease 5
Gene names
Name:USP5
Synonyms:ISOT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length858 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. Ref.12

Catalytic activity

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).

Cofactor

Binds 1 zinc ion.

Subunit structure

Interacts with TRIML1 By similarity.

Domain

The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition.

Miscellaneous

The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 2 UBA domains.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAD23BP547272EBI-741277,EBI-954531
TADA3O755282EBI-741277,EBI-473249

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P45974-1)

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.
Isoform Short (identifier: P45974-2)

The sequence of this isoform differs from the canonical sequence as follows:
     629-652: GSLGFYGNEDEDSFCSPHFSSPTS → A

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 858857Ubiquitin carboxyl-terminal hydrolase 5
PRO_0000080623

Regions

Domain326 – 856531USP
Domain654 – 69542UBA 1
Domain722 – 76241UBA 2
Zinc finger197 – 26973UBP-type
Region221 – 2244Substrate binding

Sites

Active site3351Nucleophile
Active site8181Proton acceptor By similarity
Metal binding1991Zinc
Metal binding2021Zinc
Metal binding2191Zinc
Metal binding2321Zinc
Binding site2091Substrate
Binding site2591Substrate
Binding site2611Substrate; via carbonyl oxygen
Binding site2641Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.17 Ref.18
Modified residue6231Phosphothreonine By similarity
Modified residue7831Phosphoserine Ref.13 Ref.14
Disulfide bond195 ↔ 816 Ref.21

Natural variations

Alternative sequence629 – 65224GSLGF…SSPTS → A in isoform Short.
VSP_005259

Experimental info

Mutagenesis1991C → A: Decreased rate of activity and decreased zinc binding. Ref.19
Mutagenesis2021C → A: Decreased rate of activity. Ref.19
Mutagenesis2191C → A: Decreased rate of activity. Ref.19
Mutagenesis221 – 2233RRY → KWF: Loss of polyubiquitin binding and subsequent activation. Ref.9 Ref.16
Mutagenesis2211R → A: Loss of polyubiquitin hydrolysis. Loss of ubiquitin binding; when associated with A-335. Ref.9
Mutagenesis2321H → A: Decreased rate of activity. Ref.19
Mutagenesis2611Y → F: Loss of polyubiquitin binding. Ref.16
Mutagenesis3351C → A: Loss of activity. Loss of ubiquitin binding; when associated with A-221. Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with E-666. Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with E-734. Ref.9
Mutagenesis4351D → A: Loss of polyubiquitin binding and hydrolysis. Ref.9
Mutagenesis6661M → E: Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with A-335. No effect on activity; when associated with E-734. Ref.9
Mutagenesis7341M → E: Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with A-335. No effect on activity; when associated with E-666. Ref.9
Sequence conflict3 – 42EL → DV in CAA62690. Ref.1
Sequence conflict451I → V in CAA62690. Ref.1
Sequence conflict4681K → R in AAA78934. Ref.4
Sequence conflict6811G → D in AAA78934. Ref.4

Secondary structure

.................................................................................................................. 858
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: E99CB7CDFA682C65

FASTA85895,786
        10         20         30         40         50         60 
MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF LGFGKQYVER 

        70         80         90        100        110        120 
HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA IGVEGGFDLS EEKFELDEDV 

       130        140        150        160        170        180 
KIVILPDYLE IARDGLGGLP DIVRDRVTSA VEALLSADSA SRKQEVQAWD GEVRQVSKHA 

       190        200        210        220        230        240 
FSLKQLDNPA RIPPCGWKCS KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET 

       250        260        270        280        290        300 
GYPLAVKLGT ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM 

       310        320        330        340        350        360 
NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF QRKYVDKLEK 

       370        380        390        400        410        420 
IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE RVPEQKEVQD GIAPRMFKAL 

       430        440        450        460        470        480 
IGKGHPEFST NRQQDAQEFF LHLINMVERN CRSSENPNEV FRFLVEEKIK CLATEKVKYT 

       490        500        510        520        530        540 
QRVDYIMQLP VPMDAALNKE ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE 

       550        560        570        580        590        600 
QVDDFWSTAL QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS 

       610        620        630        640        650        660 
QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP TSPMLDESVI 

       670        680        690        700        710        720 
IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD FANPLILPGS SGPGSTSAAA 

       730        740        750        760        770        780 
DPPPEDCVTT IVSMGFSRDQ ALKALRATNN SLERAVDWIF SHIDDLDAEA AMDISEGRSA 

       790        800        810        820        830        840 
ADSISESVPV GPKVRDGPGK YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS 

       850 
EKPPKDLGYI YFYQRVAS 

« Hide

Isoform Short [UniParc].

Checksum: 227CB29B11C7DAEA
Show »

FASTA83593,308

References

« Hide 'large scale' references
[1]"cDNA cloning of a human 100 kDa de-ubiquitinating enzyme: the 100 kDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2)."
Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K., Jaton J.-C.
FEBS Lett. 376:233-237(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13."
Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.
Genome Res. 6:314-326(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Tashayev V.L., O'Connor L.B., Larsen C.N., Kasperek E., Pickart C.M.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Kidney and Lung.
[7]"A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro."
Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K., Jaton J.-C.
FEBS Lett. 359:73-77(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T."
Reyes-Turcu F.E., Shanks J.R., Komander D., Wilkinson K.D.
J. Biol. Chem. 283:19581-19592(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-221; CYS-335; ASP-435; MET-666 AND MET-734, POLYUBIQUITIN BINDING.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53."
Dayal S., Sparks A., Jacob J., Allende-Vega N., Lane D.P., Saville M.K.
J. Biol. Chem. 284:5030-5041(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin."
Zhang Y.H., Zhou C.J., Zhou Z.R., Song A.X., Hu H.Y.
PLoS ONE 6:E29362-E29362(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 221-ARG--TYR-223 AND TYR-261.
[17]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin."
Reyes-Turcu F.E., Horton J.R., Mullally J.E., Heroux A., Cheng X., Wilkinson K.D.
Cell 124:1197-1208(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 163-291 IN COMPLEX WITH UBIQUITIN, ZINC-BINDING, MUTAGENESIS OF CYS-199; CYS-202; CYS-219 AND HIS-232.
[20]"Solution structure of the first and second UBA domains in the human ubiquitin specific protease 5 (isopeptidase 5)."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 655-772.
[21]"Covalent ubiquitin-USP5 complex."
Walker J.R., Avvakumov G.V., Xue S., Butler-Cole C., Weigelt J., Bountra C., Arrowsmith C.H., Edwards A.M., Bochkarev A., Dhe-Paganon S.
Submitted (DEC-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-858 IN COMPLEX WITH UBIQUITIN, DISULFIDE BOND, ZINC-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91349 mRNA. Translation: CAA62690.1.
U47927 mRNA. Translation: AAC50465.1.
U47924 Genomic DNA. Translation: AAB51314.1.
U47924 Genomic DNA. Translation: AAB51315.1.
U35116 mRNA. Translation: AAA78934.1.
CH471116 Genomic DNA. Translation: EAW88724.1.
CH471116 Genomic DNA. Translation: EAW88725.1.
CH471116 Genomic DNA. Translation: EAW88726.1.
CH471116 Genomic DNA. Translation: EAW88727.1.
BC004889 mRNA. Translation: AAH04889.1.
BC005139 mRNA. Translation: AAH05139.1.
PIRS68227.
RefSeqNP_001092006.1. NM_001098536.1.
NP_003472.2. NM_003481.2.
UniGeneHs.631661.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAGNMR-A655-715[»]
2DAKNMR-A723-772[»]
2G43X-ray2.09A/B163-291[»]
2G45X-ray1.99A/D163-291[»]
3IHPX-ray2.80A/B1-858[»]
ProteinModelPortalP45974.
SMRP45974. Positions 1-858.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113751. 60 interactions.
DIPDIP-34459N.
IntActP45974. 7 interactions.
MINTMINT-5001006.
STRING9606.ENSP00000229268.

Chemistry

ChEMBLCHEMBL6158.

Protein family/group databases

MEROPSC19.001.

PTM databases

PhosphoSiteP45974.

Polymorphism databases

DMDM1717869.

2D gel databases

REPRODUCTION-2DPAGEIPI00375145.

Proteomic databases

PaxDbP45974.
PRIDEP45974.

Protocols and materials databases

DNASU8078.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229268; ENSP00000229268; ENSG00000111667. [P45974-1]
ENST00000389231; ENSP00000373883; ENSG00000111667. [P45974-2]
ENST00000595281; ENSP00000472079; ENSG00000268462. [P45974-1]
ENST00000597018; ENSP00000470388; ENSG00000268462. [P45974-2]
GeneID8078.
KEGGhsa:8078.
UCSCuc001qrh.4. human. [P45974-2]
uc001qri.4. human. [P45974-1]

Organism-specific databases

CTD8078.
GeneCardsGC12P007111.
HGNCHGNC:12628. USP5.
HPAHPA006756.
MIM601447. gene.
neXtProtNX_P45974.
PharmGKBPA37253.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5207.
HOGENOMHOG000162311.
HOVERGENHBG002833.
InParanoidP45974.
KOK11836.
OMALRWEFSM.
PhylomeDBP45974.
TreeFamTF300576.

Gene expression databases

ArrayExpressP45974.
BgeeP45974.
CleanExHS_USP5.
GenevestigatorP45974.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFPIRSF016308. UBP. 1 hit.
SMARTSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP5. human.
EvolutionaryTraceP45974.
GeneWikiUSP5.
GenomeRNAi8078.
NextBio30687.
PMAP-CutDBP45974.
PROP45974.
SOURCESearch...

Entry information

Entry nameUBP5_HUMAN
AccessionPrimary (citable) accession number: P45974
Secondary accession number(s): D3DUS7, D3DUS8, Q96J22
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM