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Sequence of UBP4_HUMAN

EC Number:3.4.19.12

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3.4.19.12
ubiquitinyl hydrolase 1
Q13107
Homo sapiens
963
108565
Swiss-Prot
Reaction
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)
Other sequences found for EC No. 3.4.19.12

General information:

Sequence
show sequence in fasta format
  0 MAEGGGCRER PDAETQKSEL GPLMRTTLQR GAQWYLIDSR WFKQWKKYVG FDSWDMYNVG
 60 EHNLFPGPID NSGLFSDPES QTLKEHLIDE LDYVLVPTEA WNKLLNWYGC VEGQQPIVRK
120 VVEHGLFVKH CKVEVYLLEL KLCENSDPTN VLSCHFSKAD TIATIEKEMR KLFNIPAERE
180 TRLWNKYMSN TYEQLSKLDN TVQDAGLYQG QVLVIEPQNE DGTWPRQTLQ SKSSTAPSRN
240 FTTSPKSSAS PYSSVSASLI ANGDSTSTCG MHSSGVSRGG SGFSASYNCQ EPPSSHIQPG
300 LCGLGNLGNT CFMNSALQCL SNTAPLTDYF LKDEYEAEIN RDNPLGMKGE IAEAYAELIK
360 QMWSGRDAHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF LLDGLHEDLN RVKKKPYLEL
420 KDANGRPDAV VAKEAWENHR LRNDSVIVDT FHGLFKSTLV CPECAKVSVT FDPFCYLTLP
480 LPLKKDRVME VFLVPADPHC RPTQYRVTVP LMGAVSDLCE ALSRLSGIAA ENMVVADVYN
540 HRFHKIFQMD EGLNHIMPRD DIFVYEVCST SVDGSECVTL PVYFRERKSR PSSTSSASAL
600 YGQPLLLSVP KHKLTLESLY QAVCDRISRY VKQPLPDEFG SSPLEPGACN GSRNSCEGED
660 EEEMEHQEEG KEQLSETEGS GEDEPGNDPS ETTQKKIKGQ PCPKRLFTFS LVNSYGTADI
720 NSLAADGKLL KLNSRSTLAM DWDSETRRLY YDEQESEAYE KHVSMLQPQK KKKTTVALRD
780 CIELFTTMET LGEHDPWYCP NCKKHQQATK KFDLWSLPKI LVVHLKRFSY NRYWRDKLDT
840 VVEFPIRGLN MSEFVCNLSA RPYVYDLIAV SNHYGAMGVG HYTAYAKNKL NGKWYYFDDS
900 NVSLASEDQI VTKAAYVLFY QRRDDEFYKT PSLSSSGSSD GGTRPSSSQQ GFGDDEACSM
960 DTN
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1011463
Gray D.A.,Inazawa J.,Gupta K.,Wong A.,Ueda R.,Takahashi T.
Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors.
Oncogene
10
2179-2183
1995
7784062
1011465
Frederick A.,Rolfe M.,Chiu M.I.
The human UNP locus at 3p21.31 encodes two tissue-selective, cytoplasmic isoforms with deubiquitinating activity that have reduced expression in small cell lung carcinoma cell lines.
Oncogene
16
153-165
1998
9464533
1011466
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.
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet.
36
40-45
2004
14702039
1011467
Muzny D.M.,Scherer S.E.,Kaul R.,Wang J.,Yu J.,Sudbrak R.,Buhay C.J.,Chen R.,Cree A.,Ding Y.,Dugan-Rocha S.,Gill R.,Gunaratne P.,Harris R.A.,Hawes A.C.,Hernandez J.,Hodgson A.V.,Hume J.,Jackson A.,Khan Z.M.,Kovar-Smith C.,Lewis L.R.,Lozado R.J.,Metzker M.L.,Milosavljevic A.,Miner G.R.,Morgan M.B.,Nazareth L.V.,Scott G.,Sodergren E.,Song X.-Z.,Steffen D.,Wei S.,Wheeler D.A.,Wright M.W.,Worley K.C.,Yuan Y.,Zhang Z.,Adams C.Q.,Ansari-Lari M.A.,Ayele M.,Brown M.J.,Chen G.,Chen Z.,Clendenning J.,Clerc-Blankenburg K.P.,Chen R.,Chen Z.,Davis C.,Delgado O.,Dinh H.H.,Dong W.,Draper H.,Ernst S.,Fu G.,Gonzalez-Garay M.L.,Garcia D.K.,Gillett W.,Gu J.,Hao B.,Haugen E.,Havlak P.,He X.,Hennig S.,Hu S.,Huang W.,Jackson L.R.,Jacob L.S.,Kelly S.H.,Kube M.,Levy R.,Li Z.,Liu B.,Liu J.,Liu W.,Lu J.,Maheshwari M.,Nguyen B.-V.,Okwuonu G.O.,Palmeiri A.,Pasternak S.,Perez L.M.,Phelps K.A.,Plopper F.J.,Qiang B.,Raymond C.,Rodriguez R.,Saenphimmachak C.,Santibanez J.,Shen H.,Shen Y.,Subramanian S.,Tabor P.E.,Verduzco D.,Waldron L.,Wang J.,Wang J.,Wang Q.,Williams G.A.,Wong G.K.-S.,Yao Z.,Zhang J.,Zhang X.,Zhao G.,Zhou J.,Zhou Y.,Nelson D.,Lehrach H.,Reinhardt R.,Naylor S.L.,Yang H.,Olson M.,Weinstock G.,Gibbs R.A.
The DNA sequence, annotation and analysis of human chromosome 3.
Nature
440
1194-1198
2006
16641997
1011468
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
15489334
1011469
DeSalle L.M.,Latres E.,Lin D.,Graner E.,Montagnoli A.,Baker R.T.,Pagano M.,Loda M.
The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.
Oncogene
20
5538-5542
2001
11571652
1011470
Wada K.,Tanji K.,Kamitani T.
Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase activity.
Biochem. Biophys. Res. Commun.
339
731-736
2006
16316627
1011471
Wada K.,Kamitani T.
UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself.
Biochem. Biophys. Res. Commun.
342
253-258
2006
16472766
1011472
Milojevic T.,Reiterer V.,Stefan E.,Korkhov V.M.,Dorostkar M.M.,Ducza E.,Ogris E.,Boehm S.,Freissmuth M.,Nanoff C.
The ubiquitin-specific protease Usp4 regulates the cell surface level of the A2A receptor.
Mol. Pharmacol.
69
1083-1094
2006
16339847
1011473
Song E.J.,Werner S.L.,Neubauer J.,Stegmeier F.,Aspden J.,Rio D.,Harper J.W.,Elledge S.J.,Kirschner M.W.,Rape M.
The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome.
Genes Dev.
24
1434-1447
2010
20595234
1011474
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
21269460
1011475
Luna-Vargas M.P.,Faesen A.C.,van Dijk W.J.,Rape M.,Fish A.,Sixma T.K.
Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain.
EMBO Rep.
12
365-372
2011
21415856
1011476
Luna-Vargas M.P.,Faesen A.C.,van Dijk W.J.,Rape M.,Fish A.,Sixma T.K.
Retraction: 'Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain' by MP Luna-Vargas, AC Faesen, WJ van Dijk, M Rape, A Fish, TK Sixma.
EMBO Rep.
15
121-121
2014
24398133
1011477
Uras I.Z.,List T.,Nijman S.M.
Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1.
PLoS ONE
7
0-0
2012
22347420
1011478
Clerici M.,Luna-Vargas M.P.,Faesen A.C.,Sixma T.K.
The DUSP-Ubl domain of USP4 enhances its catalytic efficiency by promoting ubiquitin exchange.
Nat. Commun.
5
5399-5399
2014
25404403
1011479
Mehic M.,de Sa V.K.,Hebestreit S.,Heldin C.H.,Heldin P.
The deubiquitinating enzymes USP4 and USP17 target hyaluronan synthase 2 and differentially affect its function.
Oncogenesis
6
0-0
2017
28604766