Ubiquitin carboxyl-terminal hydrolase 33

Preferred order of sections

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 33
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 33
Ubiquitin thioesterase 33
Ubiquitin-specific-processing protease 33
VHL-interacting deubiquitinating enzyme 1
Short name=hVDU1

Gene names

Name:	USP33
Synonyms:	KIAA1097, VDU1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	942 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Deubiquitinating enzyme involved in various processes such as cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Ref.5 Ref.8 Ref.9
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).
Subunit structure	Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with ARRB1, ARRB2, ADRB2, DIO2 and ROBO1. Interacts with SELENBP1; in a selenium-dependent manner. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm › perinuclear region. Note: According to Ref.5, it localizes in the endoplasmic reticulum; however the relevance of such result is unclear. Ref.7
Tissue specificity	Widely expressed. Ref.1
Domain	The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 86 is replaced by a Glu residue. Ref.10
Post-translational modification	Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. Ref.1
Sequence similarities	Belongs to the peptidase C19 family. USP20/USP33 subfamily. Contains 2 DUSP domains. Contains 1 UBP-type zinc finger.
Sequence caution	The sequence BAA83049.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Endocytosis Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from sequence or structural similarity. Source: UniProtKB cell migration Inferred from sequence or structural similarity. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: UniProtKB-KW protein K48-linked deubiquitination Inferred from direct assay Ref.9. Source: UniProtKB protein K63-linked deubiquitination Inferred from direct assay Ref.9. Source: UniProtKB regulation of G-protein coupled receptor protein signaling pathway Inferred from mutant phenotype Ref.9 Ref.8. Source: UniProtKB ubiquitin-dependent protein catabolic process Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	VCB complex Traceable author statement Ref.1. Source: UniProtKB cell body Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type endopeptidase activity Inferred from mutant phenotype Ref.9 Ref.8. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.9 Ref.8. Source: UniProtKB ubiquitin-specific protease activity Traceable author statement Ref.1. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SELENBP1	Q13228	5	EBI-719307,EBI-711619

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TEY7-1) 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 2 (identifier: Q8TEY7-2) The sequence of this isoform differs from the canonical sequence as follows: 1-31: Missing.

Isoform 3 (identifier: Q8TEY7-3) The sequence of this isoform differs from the canonical sequence as follows: 552-559: Missing. 834-836: LNR → VKK 837-942: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 942

942

Ubiquitin carboxyl-terminal hydrolase 33

PRO_0000080664

Regions

Domain

717 – 810

94

DUSP 1

Domain

818 – 921

104

DUSP 2

Zinc finger

59 – 123

65

UBP-type

Sites

Active site

194

1

Nucleophile

Active site

673

1

Proton acceptor By similarity

Amino acid modifications

Modified residue

439

1

Phosphoserine Ref.6

Natural variations

Alternative sequence

1 – 31

31

Missing in isoform 2.

VSP_008591

Alternative sequence

552 – 559

8

Missing in isoform 3.

VSP_008592

Alternative sequence

834 – 836

3

LNR → VKK in isoform 3.

VSP_008593

Alternative sequence

837 – 942

106

Missing in isoform 3.

VSP_008594

Experimental info

Mutagenesis

194

1

C → S: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with Q-673. Ref.8 Ref.9

Mutagenesis

673

1

H → Q: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with S-194. Ref.8 Ref.9

Sequence conflict

241

1

H → Y in AAL78314. Ref.1

Sequence conflict

241

1

H → Y in AAL78315. Ref.1

Sequence conflict

241

1

H → Y in BAA83049. Ref.2

Sequence conflict

428

1

S → L in BAB14279. Ref.3

Sequence conflict

617

1

K → R in BAB14279. Ref.3

Secondary structure

1

.

942

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 10A3AD632B901A74 Show »	FASTA	942	106,727
10 20 30 40 50 60 MTGSNSHITI LTLKVLPHFE SLGKQEKIPN KMSAFRNHCP HLDSVGEITK EDLIQKSLGT 70 80 90 100 110 120 CQDCKVQGPN LWACLENRCS YVGCGESQVD HSTIHSQETK HYLTVNLTTL RVWCYACSKE 130 140 150 160 170 180 VFLDRKLGTQ PSLPHVRQPH QIQENSVQDF KIPSNTTLKT PLVAVFDDLD IEADEEDELR 190 200 210 220 230 240 ARGLTGLKNI GNTCYMNAAL QALSNCPPLT QFFLDCGGLA RTDKKPAICK SYLKLMTELW 250 260 270 280 290 300 HKSRPGSVVP TTLFQGIKTV NPTFRGYSQQ DAQEFLRCLM DLLHEELKEQ VMEVEEDPQT 310 320 330 340 350 360 ITTEETMEED KSQSDVDFQS CESCSNSDRA ENENGSRCFS EDNNETTMLI QDDENNSEMS 370 380 390 400 410 420 KDWQKEKMCN KINKVNSEGE FDKDRDSISE TVDLNNQETV KVQIHSRASE YITDVHSNDL 430 440 450 460 470 480 STPQILPSNE GVNPRLSASP PKSGNLWPGL APPHKKAQSA SPKRKKQHKK YRSVISDIFD 490 500 510 520 530 540 GTIISSVQCL TCDRVSVTLE TFQDLSLPIP GKEDLAKLHS SSHPTSIVKA GSCGEAYAPQ 550 560 570 580 590 600 GWIAFFMEYV KRFVVSCVPS WFWGPVVTLQ DCLAAFFARD ELKGDNMYSC EKCKKLRNGV 610 620 630 640 650 660 KFCKVQNFPE ILCIHLKRFR HELMFSTKIS THVSFPLEGL DLQPFLAKDS PAQIVTYDLL 670 680 690 700 710 720 SVICHHGTAS SGHYIAYCRN NLNNLWYEFD DQSVTEVSES TVQNAEAYVL FYRKSSEEAQ 730 740 750 760 770 780 KERRRISNLL NIMEPSLLQF YISRQWLNKF KTFAEPGPIS NNDFLCIHGG VPPRKAGYIE 790 800 810 820 830 840 DLVLMLPQNI WDNLYSRYGG GPAVNHLYIC HTCQIEAEKI EKRRKTELEI FIRLNRAFQK 850 860 870 880 890 900 EDSPATFYCI SMQWFREWES FVKGKDGDPP GPIDNTKIAV TKCGNVMLRQ GADSGQISEE 910 920 930 940 TWNFLQSIYG GGPEVILRPP VVHVDPDILQ AEEKIEVETR SL « Hide
Isoform 2 [UniParc]. Checksum: 7F3F40A75F764624 Show »	FASTA	911	103,283
10 20 30 40 50 60 MSAFRNHCPH LDSVGEITKE DLIQKSLGTC QDCKVQGPNL WACLENRCSY VGCGESQVDH 70 80 90 100 110 120 STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTQP SLPHVRQPHQ IQENSVQDFK 130 140 150 160 170 180 IPSNTTLKTP LVAVFDDLDI EADEEDELRA RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ 190 200 210 220 230 240 FFLDCGGLAR TDKKPAICKS YLKLMTELWH KSRPGSVVPT TLFQGIKTVN PTFRGYSQQD 250 260 270 280 290 300 AQEFLRCLMD LLHEELKEQV MEVEEDPQTI TTEETMEEDK SQSDVDFQSC ESCSNSDRAE 310 320 330 340 350 360 NENGSRCFSE DNNETTMLIQ DDENNSEMSK DWQKEKMCNK INKVNSEGEF DKDRDSISET 370 380 390 400 410 420 VDLNNQETVK VQIHSRASEY ITDVHSNDLS TPQILPSNEG VNPRLSASPP KSGNLWPGLA 430 440 450 460 470 480 PPHKKAQSAS PKRKKQHKKY RSVISDIFDG TIISSVQCLT CDRVSVTLET FQDLSLPIPG 490 500 510 520 530 540 KEDLAKLHSS SHPTSIVKAG SCGEAYAPQG WIAFFMEYVK RFVVSCVPSW FWGPVVTLQD 550 560 570 580 590 600 CLAAFFARDE LKGDNMYSCE KCKKLRNGVK FCKVQNFPEI LCIHLKRFRH ELMFSTKIST 610 620 630 640 650 660 HVSFPLEGLD LQPFLAKDSP AQIVTYDLLS VICHHGTASS GHYIAYCRNN LNNLWYEFDD 670 680 690 700 710 720 QSVTEVSEST VQNAEAYVLF YRKSSEEAQK ERRRISNLLN IMEPSLLQFY ISRQWLNKFK 730 740 750 760 770 780 TFAEPGPISN NDFLCIHGGV PPRKAGYIED LVLMLPQNIW DNLYSRYGGG PAVNHLYICH 790 800 810 820 830 840 TCQIEAEKIE KRRKTELEIF IRLNRAFQKE DSPATFYCIS MQWFREWESF VKGKDGDPPG 850 860 870 880 890 900 PIDNTKIAVT KCGNVMLRQG ADSGQISEET WNFLQSIYGG GPEVILRPPV VHVDPDILQA 910 EEKIEVETRS L « Hide
Isoform 3 [UniParc]. Checksum: A6A5D23B288BFC00 Show »	FASTA	828	93,957
10 20 30 40 50 60 MTGSNSHITI LTLKVLPHFE SLGKQEKIPN KMSAFRNHCP HLDSVGEITK EDLIQKSLGT 70 80 90 100 110 120 CQDCKVQGPN LWACLENRCS YVGCGESQVD HSTIHSQETK HYLTVNLTTL RVWCYACSKE 130 140 150 160 170 180 VFLDRKLGTQ PSLPHVRQPH QIQENSVQDF KIPSNTTLKT PLVAVFDDLD IEADEEDELR 190 200 210 220 230 240 ARGLTGLKNI GNTCYMNAAL QALSNCPPLT QFFLDCGGLA RTDKKPAICK SYLKLMTELW 250 260 270 280 290 300 HKSRPGSVVP TTLFQGIKTV NPTFRGYSQQ DAQEFLRCLM DLLHEELKEQ VMEVEEDPQT 310 320 330 340 350 360 ITTEETMEED KSQSDVDFQS CESCSNSDRA ENENGSRCFS EDNNETTMLI QDDENNSEMS 370 380 390 400 410 420 KDWQKEKMCN KINKVNSEGE FDKDRDSISE TVDLNNQETV KVQIHSRASE YITDVHSNDL 430 440 450 460 470 480 STPQILPSNE GVNPRLSASP PKSGNLWPGL APPHKKAQSA SPKRKKQHKK YRSVISDIFD 490 500 510 520 530 540 GTIISSVQCL TCDRVSVTLE TFQDLSLPIP GKEDLAKLHS SSHPTSIVKA GSCGEAYAPQ 550 560 570 580 590 600 GWIAFFMEYV KSWFWGPVVT LQDCLAAFFA RDELKGDNMY SCEKCKKLRN GVKFCKVQNF 610 620 630 640 650 660 PEILCIHLKR FRHELMFSTK ISTHVSFPLE GLDLQPFLAK DSPAQIVTYD LLSVICHHGT 670 680 690 700 710 720 ASSGHYIAYC RNNLNNLWYE FDDQSVTEVS ESTVQNAEAY VLFYRKSSEE AQKERRRISN 730 740 750 760 770 780 LLNIMEPSLL QFYISRQWLN KFKTFAEPGP ISNNDFLCIH GGVPPRKAGY IEDLVLMLPQ 790 800 810 820 NIWDNLYSRY GGGPAVNHLY ICHTCQIEAE KIEKRRKTEL EIFIRVKK « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein." Li Z., Na X., Wang D., Schoen S.R., Messing E.M., Wu G. J. Biol. Chem. 277:4656-4662(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), UBIQUITINATION, INTERACTION WITH VHL, TISSUE SPECIFICITY.
[2]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]	"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] (ISOFORM 3). Tissue: Eye.
[5]	"Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation." Curcio-Morelli C., Zavacki A.M., Christofollete M., Gereben B., de Freitas B.C., Harney J.W., Li Z., Wu G., Bianco A.C. J. Clin. Invest. 112:189-196(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DIO2.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner." Jeong J.Y., Wang Y., Sytkowski A.J. Biochem. Biophys. Res. Commun. 379:583-588(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SELENBP1, SUBCELLULAR LOCATION.
[8]	"The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization." Berthouze M., Venkataramanan V., Li Y., Shenoy S.K. EMBO J. 28:1684-1696(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ADRB2, MUTAGENESIS OF CYS-194 AND HIS-673.
[9]	"Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2." Shenoy S.K., Modi A.S., Shukla A.K., Xiao K., Berthouze M., Ahn S., Wilkinson K.D., Miller W.E., Lefkowitz R.J. Proc. Natl. Acad. Sci. U.S.A. 106:6650-6655(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARRB1 AND ARRB2, MUTAGENESIS OF CYS-194 AND HIS-673.
[10]	"The solution structure of the ZnF UBP domain of USP33/VDU1." Allen M.D., Bycroft M. Protein Sci. 16:2072-2075(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 36-130, ZINC-BINDING, DOMAIN UBP-TYPE ZINC FINGER.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF383172 mRNA. Translation: AAL78314.1.
AF383173 mRNA. Translation: AAL78315.1.
AB029020 mRNA. Translation: BAA83049.1. Different initiation.
AK022864 mRNA. Translation: BAB14279.1.
BC016663 mRNA. Translation: AAH16663.1.

IPI

IPI00236901.
IPI00377264.
IPI00402757.

RefSeq

NP_055832.3. NM_015017.4.
NP_963918.1. NM_201624.2.
NP_963920.1. NM_201626.2.

UniGene

Hs.480597.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2UZG	NMR	-	A	36-130	[»]

ProteinModelPortal

Q8TEY7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48942N.

IntAct

Q8TEY7. 7 interactions.

MINT

MINT-1370210.

STRING

9606.ENSP00000350009.

Protein family/group databases

MEROPS

C19.037.

PTM databases

PhosphoSite

Q8TEY7.

Polymorphism databases

DMDM

116242838.

Proteomic databases

PaxDb

Q8TEY7.

PRIDE

Q8TEY7.

Protocols and materials databases

DNASU

23032.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357428; ENSP00000350009; ENSG00000077254.
ENST00000370792; ENSP00000359828; ENSG00000077254.
ENST00000370793; ENSP00000359829; ENSG00000077254.
ENST00000370794; ENSP00000359830; ENSG00000077254.

GeneID

23032.

KEGG

hsa:23032.

UCSC

uc001dhs.3. human.
uc001dhw.3. human.

Organism-specific databases

CTD

23032.

GeneCards

GC01M078161.

H-InvDB

HIX0159957.

HGNC

HGNC:20059. USP33.

HPA

HPA005719.

neXtProt

NX_Q8TEY7.

PharmGKB

PA134955343.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5560.

HOGENOM

HOG000286031.

HOVERGEN

HBG054196.

InParanoid

Q8TEY7.

KO

K11848.

OMA

TMEEDKS.

PhylomeDB

Q8TEY7.

Gene expression databases

ArrayExpress

Q8TEY7.

Bgee

Q8TEY7.

CleanEx

HS_USP33.

Genevestigator

Q8TEY7.

GermOnline

ENSG00000077254. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]

Pfam

PF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]

SMART

SM00695. DUSP. 2 hits.
[Graphical view]

PROSITE

PS51283. DUSP. 2 hits.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

USP33. human.

EvolutionaryTrace

Q8TEY7.

GenomeRNAi

23032.

NextBio

44018.

Entry information

Entry name

UBP33_HUMAN

Accession

Primary (citable) accession number: Q8TEY7
Secondary accession number(s): Q8TEY6

Q9UPQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents