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Protein

Josephin-2

Gene

JOSD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme.3 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).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei24 – 241NucleophilePROSITE-ProRule annotation
Active sitei125 – 1251Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. omega peptidase activity Source: InterPro
  2. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. protein deubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC86.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Josephin-2 (EC:3.4.19.12)
Alternative name(s):
Josephin domain-containing protein 2
Gene namesi
Name:JOSD2
ORF Names:SBBI54
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:28853. JOSD2.

Subcellular locationi

Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241C → A: Loss of deubiquitination activity, no change in subcellular location. 1 Publication

Organism-specific databases

PharmGKBiPA142671645.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Josephin-2PRO_0000053843Add
BLAST

Proteomic databases

MaxQBiQ8TAC2.
PaxDbiQ8TAC2.
PRIDEiQ8TAC2.

PTM databases

PhosphoSiteiQ8TAC2.

Expressioni

Gene expression databases

BgeeiQ8TAC2.
CleanExiHS_JOSD2.
ExpressionAtlasiQ8TAC2. baseline and differential.
GenevestigatoriQ8TAC2.

Interactioni

Protein-protein interaction databases

BioGridi125956. 12 interactions.
STRINGi9606.ENSP00000293431.

Structurei

3D structure databases

ProteinModelPortaliQ8TAC2.
SMRiQ8TAC2. Positions 14-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 188178JosephinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Josephin domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG321724.
GeneTreeiENSGT00390000009228.
HOVERGENiHBG039523.
InParanoidiQ8TAC2.
KOiK15235.
OMAiVWWDRRR.
OrthoDBiEOG75B871.
PhylomeDBiQ8TAC2.
TreeFamiTF313660.

Family and domain databases

InterProiIPR006155. Josephin.
[Graphical view]
PfamiPF02099. Josephin. 1 hit.
[Graphical view]
PRINTSiPR01233. JOSEPHIN.
PROSITEiPS50957. JOSEPHIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TAC2-1) [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
MSQAPGAQPS PPTVYHERQR LELCAVHALN NVLQQQLFSQ EAADEICKRL
60 70 80 90 100
APDSRLNPHR SLLGTGNYDV NVIMAALQGL GLAAVWWDRR RPLSQLALPQ
110 120 130 140 150
VLGLILNLPS PVSLGLLSLP LRRRHWVALR QVDGVYYNLD SKLRAPEALG
160 170 180
DEDGVRAFLA AALAQGLCEV LLVVTKEVEE KGSWLRTD
Length:188
Mass (Da):20,756
Last modified:May 31, 2002 - v1
Checksum:iA2832B4D9BD675E9
GO
Isoform 2 (identifier: Q8TAC2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-90: Missing.

Note: No experimental confirmation available.

Show »
Length:146
Mass (Da):16,100
Checksum:i86386376B0F16FDB
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 9042Missing in isoform 2. 1 PublicationVSP_047537Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF247787 mRNA. Translation: AAL95692.1.
AK131052 mRNA. No translation available.
AC008743 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW71877.1.
BC062416 mRNA. Translation: AAH62416.1.
CCDSiCCDS12797.1. [Q8TAC2-1]
CCDS59413.1. [Q8TAC2-2]
RefSeqiNP_001257568.1. NM_001270639.1. [Q8TAC2-1]
NP_001257569.1. NM_001270640.1. [Q8TAC2-1]
NP_001257570.1. NM_001270641.1. [Q8TAC2-2]
NP_001257615.1. NM_001270686.1. [Q8TAC2-1]
NP_612207.1. NM_138334.3. [Q8TAC2-1]
UniGeneiHs.467151.
Hs.737597.

Genome annotation databases

EnsembliENST00000595669; ENSP00000468860; ENSG00000161677. [Q8TAC2-2]
ENST00000598418; ENSP00000468956; ENSG00000161677. [Q8TAC2-1]
ENST00000601423; ENSP00000472116; ENSG00000161677. [Q8TAC2-1]
GeneIDi126119.
KEGGihsa:126119.
UCSCiuc002psn.2. human. [Q8TAC2-1]

Polymorphism databases

DMDMi29840785.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF247787 mRNA. Translation: AAL95692.1.
AK131052 mRNA. No translation available.
AC008743 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW71877.1.
BC062416 mRNA. Translation: AAH62416.1.
CCDSiCCDS12797.1. [Q8TAC2-1]
CCDS59413.1. [Q8TAC2-2]
RefSeqiNP_001257568.1. NM_001270639.1. [Q8TAC2-1]
NP_001257569.1. NM_001270640.1. [Q8TAC2-1]
NP_001257570.1. NM_001270641.1. [Q8TAC2-2]
NP_001257615.1. NM_001270686.1. [Q8TAC2-1]
NP_612207.1. NM_138334.3. [Q8TAC2-1]
UniGeneiHs.467151.
Hs.737597.

3D structure databases

ProteinModelPortaliQ8TAC2.
SMRiQ8TAC2. Positions 14-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125956. 12 interactions.
STRINGi9606.ENSP00000293431.

Protein family/group databases

MEROPSiC86.005.

PTM databases

PhosphoSiteiQ8TAC2.

Polymorphism databases

DMDMi29840785.

Proteomic databases

MaxQBiQ8TAC2.
PaxDbiQ8TAC2.
PRIDEiQ8TAC2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000595669; ENSP00000468860; ENSG00000161677. [Q8TAC2-2]
ENST00000598418; ENSP00000468956; ENSG00000161677. [Q8TAC2-1]
ENST00000601423; ENSP00000472116; ENSG00000161677. [Q8TAC2-1]
GeneIDi126119.
KEGGihsa:126119.
UCSCiuc002psn.2. human. [Q8TAC2-1]

Organism-specific databases

CTDi126119.
GeneCardsiGC19M051009.
HGNCiHGNC:28853. JOSD2.
MIMi615324. gene.
neXtProtiNX_Q8TAC2.
PharmGKBiPA142671645.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321724.
GeneTreeiENSGT00390000009228.
HOVERGENiHBG039523.
InParanoidiQ8TAC2.
KOiK15235.
OMAiVWWDRRR.
OrthoDBiEOG75B871.
PhylomeDBiQ8TAC2.
TreeFamiTF313660.

Miscellaneous databases

ChiTaRSiJOSD2. human.
GenomeRNAii126119.
NextBioi81688.
PROiQ8TAC2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TAC2.
CleanExiHS_JOSD2.
ExpressionAtlasiQ8TAC2. baseline and differential.
GenevestigatoriQ8TAC2.

Family and domain databases

InterProiIPR006155. Josephin.
[Graphical view]
PfamiPF02099. Josephin. 1 hit.
[Graphical view]
PRINTSiPR01233. JOSEPHIN.
PROSITEiPS50957. JOSEPHIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Hypothetical transmembrane protein SBBI54."
    Li N., Wan T., Zhang W., Cao X.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Macrophage.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  6. "Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes."
    Tzvetkov N., Breuer P.
    Biol. Chem. 388:973-978(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.
  7. "Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity."
    Weeks S.D., Grasty K.C., Hernandez-Cuebas L., Loll P.J.
    J. Biol. Chem. 286:4555-4565(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.
  8. "JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility, and endocytosis."
    Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.
    J. Biol. Chem. 288:17145-17155(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-24.
  9. "Structural modeling of ataxin-3 reveals distant homology to adaptins."
    Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.
    Proteins 50:355-370(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiJOS2_HUMAN
AccessioniPrimary (citable) accession number: Q8TAC2
Secondary accession number(s): M0QX25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 27, 2003
Last sequence update: May 31, 2002
Last modified: January 6, 2015
This is version 92 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.