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Protein data for HHP2_SCHPO:

Description:
Casein kinase I homolog hhp2 (EC 2.7.1.-).

Molecular weight: 45832

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-FEB-1995, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
07-MAR-2006, entry version 44.

Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.

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 HHP2_SCHPO:

DatabasePointerAdd. info#1Add. info#2
EMBLU10864AAA21545.1-
EMBLX78872CAA55474.1-
EMBLZ99753CAB16883.1-
PIRS46358S46358.
HSSPQ064861CKI
GeneDB_SpombeSPAC23C4.12-.1
BioCycSPOM-XXX-01:SPOM-XXX-01-000881-MONOMER-.1
GOGO:0004674F:protein serine/threonine kinase activityTAS.
GOGO:0006281P:DNA repairIMP.
GOGO:0006468P:protein amino acid phosphorylationTAS.
InterProIPR000719Prot_kinase.
InterProIPR008271Ser_thr_pkin_AS.
InterProIPR002290Ser_thr_pkinase.
InterProIPR001245Tyr_pkinase.
PfamPF00069Pkinase1.
ProDomPD000001Prot_kinase1.
PROSITEPS00107PROTEIN_KINASE_ATP1.
PROSITEPS50011PROTEIN_KINASE_DOM1.
PROSITEPS00108PROTEIN_KINASE_ST1.

General information about the databases mentioned above

Keywords:
ATP-binding; Complete proteome; DNA damage; DNA repair; Kinase; Nuclear protein; Nucleotide-binding; Serine/threonine-protein kinase; Transferase.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP66;
RX MEDLINE=94354807; PubMed=8074660;
RA Kearney P., Ebert M., Kuret J.;
RT "Molecular cloning and sequence analysis of two novel fission yeast
RT casein kinase-1 isoforms.";
RL Biochem. Biophys. Res. Commun. 203:231-236(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=94298768; PubMed=8026462;
RA Dhillon N., Hoekstra M.F.;
RT "Characterization of two protein kinases from Schizosaccharomyces
RT pombe involved in the regulation of DNA repair.";
RL EMBO J. 13:2777-2788(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).

Feature:
CHAIN 1 400 Casein kinase I homolog hhp2.
/FTId=PRO_0000192865.
DOMAIN 12 278 Protein kinase.
NP_BIND 18 26 ATP (By similarity).
COMPBIAS 297 400 Ala/Gln/Pro-rich.
ACT_SITE 131 131 Proton acceptor (By similarity).
BINDING 41 41 ATP (By similarity).
CONFLICT 4 4 Missing (in Ref. 1).

Comments:
-!- FUNCTION: Involved in DNA repair. May regulate the activity of
protein(s) involved in double strand break repair caused by gamma
rays.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBCELLULAR LOCATION: Nucleus (Probable).
-!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. Casein
kinase I subfamily.
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Sequence length: 400

     MTVVDIKIGN KYRIGRKIGS GSFGQIYLGL NTVNGEQVAV KLEPLKARHH QLEYEFRVYN
     ILKGNIGIPT IRWFGVTNSY NAMVMDLLGP SLEDLFCYCG RKFTLKTVLL LADQLISRIE
     YVHSKSFLHR DIKPDNFLMK KHSNVVTMID FGLAKKYRDF KTHVHIPYRD NKNLTGTARY
     ASINTHIGIE QSRRDDLESL GYVLLYFCRG SLPWQGLQAD TKEQKYQRIR DTKIGTPLEV
     LCKGLPEEFI TYMCYTRQLS FTEKPNYAYL RKLFRDLLIR KGYQYDYVFD WMILKYQKRA
     AAAAAASATA PPQVTSPMVS QTQPVNPITP NYSSIPLPAE RNPKTPQSFS TNIVQCASPS
     PLPLSFRSPV PNKDYEYIPS SLQPQYSAQL RRVLDEEPAP

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