Sequence of DCR1A_HUMAN
EC Number:3.5.2.6
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a beta-lactam + H2O = a substituted beta-amino acid
Other sequences found for EC No. 3.5.2.6
General information:
Sequence
0 MLEDISEEDI WEYKSKRKPK RVDPNNGSKN ILKSVEKATD GKYQSKRSRN RKRAAEAKEV
60 KDHEVPLGNA GCQTSVASSQ NSSCGDGIQQ TQDKETTPGK LCRTQKSQHV SPKIRPVYDG
120 YCPNCQMPFS SLIGQTPRWH VFECLDSPPR SETECPDGLL CTSTIPFHYK RYTHFLLAQS
180 RAGDHPFSSP SPASGGSFSE TKSGVLCSLE ERWSSYQNQT DNSVSNDPLL MTQYFKKSPS
240 LTEASEKIST HIQTSQQALQ FTDFVENDKL VGVALRLANN SEHINLPLPE NDFSDCEISY
300 SPLQSDEDTH DIDEKPDDSQ EQLFFTESSK DGSLEEDDDS CGFFKKRHGP LLKDQDESCP
360 KVNSFLTRDK YDEGLYRFNS LNDLSQPISQ NNESTLPYDL ACTGGDFVLF PPALAGKLAA
420 SVHQATKAKP DEPEFHSAQS NKQKQVIEES SVYNQVSLPL VKSLMLKPFE SQVEGYLSSQ
480 PTQNTIRKLS SENLNAKNNT NSACFCRKAL EGVPVGKATI LNTENLSSTP APKYLKILPS
540 GLKYNARHPS TKVMKQMDIG VYFGLPPKRK EEKLLGESAL EGINLNPVPS PNQKRSSQCK
600 RKAEKSLSDL EFDASTLHES QLSVELSSER SQRQKKRCRK SNSLQEGACQ KRSDHLINTE
660 SEAVNLSKVK VFTKSAHGGL QRGNKKIPES SNVGGSRKKT CPFYKKIPGT GFTVDAFQYG
720 VVEGCTAYFL THFHSDHYAG LSKHFTFPVY CSEITGNLLK NKLHVQEQYI HPLPLDTECI
780 VNGVKVVLLD ANHCPGAVMI LFYLPNGTVI LHTGDFRADP SMERSLLADQ KVHMLYLDTT
840 YCSPEYTFPS QQEVIRFAIN TAFEAVTLNP HALVVCGTYS IGKEKVFLAI ADVLGSKVGM
900 SQEKYKTLQC LNIPEINSLI TTDMCSSLVH LLPMMQINFK GLQSHLKKCG GKYNQILAFR
960 PTGWTHSNKF TRIADVIPQT KGNISIYGIP YSEHSSYLEM KRFVQWLKPQ KIIPTVNVGT
1020 WKSRSTMEKY FREWKLEAGY
Download this sequence
Download all sequences for 3.5.2.6
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1176504
Nagase T.,Miyajima N.,Tanaka A.,Sazuka T.,Seki N.,Sato S.,Tabata S.,Ishikawa K.,Kawarabayasi Y.,Kotani H.,Nomura N.
Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1.
DNA Res.
2
37-43
1995
1176506
Deloukas P.,Earthrowl M.E.,Grafham D.V.,Rubenfield M.,French L.,Steward C.A.,Sims S.K.,Jones M.C.,Searle S.,Scott C.,Howe K.,Hunt S.E.,Andrews T.D.,Gilbert J.G.R.,Swarbreck D.,Ashurst J.L.,Taylor A.,Battles J.,Bird C.P.,Ainscough R.,Almeida J.P.,Ashwell R.I.S.,Ambrose K.D.,Babbage A.K.,Bagguley C.L.,Bailey J.,Banerjee R.,Bates K.,Beasley H.,Bray-Allen S.,Brown A.J.,Brown J.Y.,Burford D.C.,Burrill W.,Burton J.,Cahill P.,Camire D.,Carter N.P.,Chapman J.C.,Clark S.Y.,Clarke G.,Clee C.M.,Clegg S.,Corby N.,Coulson A.,Dhami P.,Dutta I.,Dunn M.,Faulkner L.,Frankish A.,Frankland J.A.,Garner P.,Garnett J.,Gribble S.,Griffiths C.,Grocock R.,Gustafson E.,Hammond S.,Harley J.L.,Hart E.,Heath P.D.,Ho T.P.,Hopkins B.,Horne J.,Howden P.J.,Huckle E.,Hynds C.,Johnson C.,Johnson D.,Kana A.,Kay M.,Kimberley A.M.,Kershaw J.K.,Kokkinaki M.,Laird G.K.,Lawlor S.,Lee H.M.,Leongamornlert D.A.,Laird G.,Lloyd C.,Lloyd D.M.,Loveland J.,Lovell J.,McLaren S.,McLay K.E.,McMurray A.,Mashreghi-Mohammadi M.,Matthews L.,Milne S.,Nickerson T.,Nguyen M.,Overton-Larty E.,Palmer S.A.,Pearce A.V.,Peck A.I.,Pelan S.,Phillimore B.,Porter K.,Rice C.M.,Rogosin A.,Ross M.T.,Sarafidou T.,Sehra H.K.,Shownkeen R.,Skuce C.D.,Smith M.,Standring L.,Sycamore N.,Tester J.,Thorpe A.,Torcasso W.,Tracey A.,Tromans A.,Tsolas J.,Wall M.,Walsh J.,Wang H.,Weinstock K.,West A.P.,Willey D.L.,Whitehead S.L.,Wilming L.,Wray P.W.,Young L.,Chen Y.,Lovering R.C.,Moschonas N.K.,Siebert R.,Fechtel K.,Bentley D.,Durbin R.M.,Hubbard T.,Doucette-Stamm L.,Beck S.,Smith D.R.,Rogers J.
The DNA sequence and comparative analysis of human chromosome 10.
Nature
429
375-381
2004
1176508
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
1176509
Dronkert M.L.G.,de Wit J.,Boeve M.,Vasconcelos M.L.,van Steeg H.,Tan T.L.R.,Hoeijmakers J.H.J.,Kanaar R.
Disruption of mouse SNM1 causes increased sensitivity to the DNA interstrand cross-linking agent mitomycin C.
Mol. Cell. Biol.
20
4553-4561
2000
1176510
Zhang X.,Richie C.,Legerski R.J.
Translation of hSNM1 is mediated by an internal ribosome entry site that upregulates expression during mitosis.
DNA Repair
1
379-390
2002
1176511
Richie C.T.,Peterson C.,Lu T.,Hittelman W.N.,Carpenter P.B.,Legerski R.J.
hSnm1 colocalizes and physically associates with 53BP1 before and after DNA damage.
Mol. Cell. Biol.
22
8635-8647
2002
1176512
Akhter S.,Richie C.T.,Deng J.M.,Brey E.,Zhang X.,Patrick C. Jr.,Behringer R.R.,Legerski R.J.
Deficiency in SNM1 abolishes an early mitotic checkpoint induced by spindle stress.
Mol. Cell. Biol.
24
10448-10455
2004
1176513
Ishiai M.,Kimura M.,Namikoshi K.,Yamazoe M.,Yamamoto K.,Arakawa H.,Agematsu K.,Matsushita N.,Takeda S.,Buerstedde J.-M.,Takata M.
DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation.
Mol. Cell. Biol.
24
10733-10741
2004
1176514
Dephoure N.,Zhou C.,Villen J.,Beausoleil S.A.,Bakalarski C.E.,Elledge S.J.,Gygi S.P.
A quantitative atlas of mitotic phosphorylation.
Proc. Natl. Acad. Sci. U.S.A.
105
10762-10767
2008
1176515
Gauci S.,Helbig A.O.,Slijper M.,Krijgsveld J.,Heck A.J.,Mohammed S.
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem.
81
4493-4501
2009
1176516
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
1176517
Xiao Z.,Chang J.G.,Hendriks I.A.,Sigurdsson J.O.,Olsen J.V.,Vertegaal A.C.
System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
Mol. Cell. Proteomics
14
1419-1434
2015
1176518
Hendriks I.A.,Lyon D.,Young C.,Jensen L.J.,Vertegaal A.C.,Nielsen M.L.
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
Nat. Struct. Mol. Biol.
24
325-336
2017
1176519
Diene S.M.,Pinault L.,Keshri V.,Armstrong N.,Khelaifia S.,Chabriere E.,Caetano-Anolles G.,Colson P.,La Scola B.,Rolain J.M.,Pontarotti P.,Raoult D.
Human metallo-beta-lactamase enzymes degrade penicillin.
Sci. Rep.
9
12173-12173
2019