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Description:
Ubiquitin carboxyl-terminal hydrolase 1 (EC 3.1.2.15) (Ubiquitinthiolesterase 1) (Ubiquitin-specific processing protease 1)(Deubiquitinating enzyme 1) (hUBP).
Molecular weight: 88207
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
07-FEB-2006, entry version 44.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein UBP1_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AB014458 | BAA34703.1 | - |
| EMBL | AF117386 | AAD11441.1 | - |
| EMBL | AL117575 | CAB55999.1 | - |
| EMBL | AL117503 | CAB55967.1 | - |
| EMBL | BC050525 | AAH50525.1 | - |
| PIR | T17309 | T17309. | |
| MEROPS | C19.019 | -. | |
| OGP | O94782 | -.1 | |
| Ensembl | ENSG00000162607 | Homo sapiens.1 | |
| H-InvDB | HIX0000655 | -.1 | |
| HGNC | HGNC:12607 | USP1.1 | |
| MIM | 603478 | gene. | |
| GO | GO:0004197 | F:cysteine-type endopeptidase activity | TAS. |
| GO | GO:0004843 | F:ubiquitin-specific protease activity | TAS. |
| InterPro | IPR001394 | Peptidase_C19. | |
| Pfam | PF00443 | UCH | 1. |
| PROSITE | PS00972 | UCH_2_1 | 1. |
| PROSITE | PS00973 | UCH_2_2 | 1. |
| PROSITE | PS50235 | UCH_2_3 | 1. |
Keywords:
DNA damage; DNA repair; Hydrolase; Nuclear protein; Protease; Thiol protease; Ubl conjugation; Ubl conjugation pathway.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX MEDLINE=99026138; PubMed=9806842; DOI=10.1006/geno.1998.5554;
RA Fjiwara T., Saito A., Suzuki M., Shinomiya H., Suzuki T.,
RA Takahashi E., Tanigami A., Ichiyama A., Chung C.H., Nakamura Y.,
RA Tanaka K.;
RT "Identification and chromosomal assignment of USP1, a novel gene
RT encoding a human ubiquitin-specific protease.";
RL Genomics 54:155-158(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seibold S., Marx M.;
RT "Molecular cloning of a novel human ubiquitin-specific protease.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.154701;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP FUNCTION, MUTAGENESIS OF CYS-90, SUBCELLULAR LOCATION, INDUCTION,
RP UBIQUITINATION, AND INTERACTION WITH FANCD2.
RX PubMed=15694335; DOI=10.1016/j.molcel.2005.01.008;
RA Nijman S.M.B., Huang T.T., Dirac A.M.G., Brummelkamp T.R.,
RA Kerkhoven R.M., D'Andrea A.D., Bernards R.;
RT "The deubiquitinating enzyme USP1 regulates the Fanconi Anemia
RT pathway.";
RL Mol. Cell 17:331-339(2005).
Feature:
CHAIN 1 785 Ubiquitin carboxyl-terminal hydrolase 1.
/FTId=PRO_0000080615.
ACT_SITE 90 90 By similarity.
ACT_SITE 584 584 By similarity.
ACT_SITE 593 593 By similarity.
MUTAGEN 90 90 C->S: Abolishes catalytic activity.
Promotes the accumulation of
ubiquitinated FANCD2.
CONFLICT 621 621 I -> M (in Ref. 2).
Comments:
-!- FUNCTION: Switches off FANCD2-mediated DNA repair by promoting
FANCD2 deubiquitination.
-!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thiolester + H(2)O =
ubiquitin + a thiol.
-!- SUBUNIT: Interacts with FANCD2.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- INDUCTION: In S-phase.
-!- PTM: Ubiquitinated; leading to its subsequent proteasomal
degradation.
-!- SIMILARITY: Belongs to the peptidase C19 family.
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Sequence length: 785
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKAS EYRASEIDQV
VPAAQSSPIN CEKRENLLPF VGLNNLGNTC YLNSILQVLY FCPGFKSGVK HLFNIISRKK
EALKDEANQK DKGNCKEDSL ASYELICSLQ SLIISVEQLQ ASFLLNPEKY TDELATQPRR
LLNTLRELNP MYEGYLQHDA QEVLQCILGN IQETCQLLKK EEVKNVAELP TKVEEIPHPK
EEMNGINSIE MDSMRHSEDF KEKLPKGNGK RKSDTEFGNM KKKVKLSKEH QSLEENQRQT
RSKRKATSDT LESPPKIIPK YISENESPRP SQKKSRVKIN WLKSATKQPS ILSKFCSLGK
ITTNQGVKGQ SKENECDPEE DLGKCESDNT TNGCGLESPG NTVTPVNVNE VKPINKGEEQ
IGFELVEKLF QGQLVLRTRC LECESLTERR EDFQDISVPV QEDELSKVEE SSEISPEPKT
EMKTLRWAIS QFASVERIVG EDKYFCENCH HYTEAERSLL FDKMPEVITI HLKCFAASGL
EFDCYGGGLS KINTPLLTPL KLSLEEWSTK PTNDSYGLFA VVMHSGITIS SGHYTASVKV
TDLNSLELDK GNFVVDQMCE IGKPEPLNEE EARGVVENYN DEEVSIRVGG NTQPSKVLNK
KNVEAIGLLG GQKSKADYEL YNKASNPDKV ASTAFAENRN SETSDTTGTH ESDRNKESSD
QTGINISGFE NKISYVVQSL KEYEGKWLLF DDSEVKVTEE KDFLNSLSPS TSPTSTPYLL
FYKKL