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Description:
Cyclin-H (MO15-associated protein) (p37) (p34).
Molecular weight: 37643
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-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-MAR-2006, entry version 57.
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 CCNH_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U11791 | AAA21361.1 | - |
| EMBL | U12685 | AAA57006.1 | - |
| EMBL | AF477979 | AAL74271.1 | - |
| EMBL | BC005280 | AAH05280.1 | - |
| EMBL | BC016705 | AAH16705.1 | - |
| EMBL | BC016823 | AAH16823.1 | - |
| EMBL | BC022351 | AAH22351.1 | - |
| PIR | I38731 | I38731. | |
| PDB | 1JKW | X-ray | @=1-323. |
| PDB | 1KXU | X-ray | @=1-323. |
| TRANSFAC | T02184 | -. | |
| Ensembl | ENSG00000134480 | Homo sapiens.1 | |
| H-InvDB | HIX0005017 | -.1 | |
| HGNC | HGNC:1594 | CCNH.1 | |
| MIM | 601953 | gene. | |
| Reactome | P51946 | -.1 | |
| LinkHub | P51946 | -.1 | |
| GO | GO:0005634 | C:nucleus | TAS. |
| InterPro | IPR005258 | Ccl1. | |
| InterPro | IPR006670 | Cyclin. | |
| InterPro | IPR006671 | Cyclin_N. | |
| Pfam | PF00134 | Cyclin_N | 1. |
| SMART | SM00385 | CYCLIN | 1. |
| TIGRFAMs | TIGR00569 | ccl1 | 1. |
| PROSITE | PS00292 | CYCLINS | FALSE_NEG. |
Keywords:
3D-structure; Cell cycle; Cyclin; Direct protein sequencing; Nuclear protein; Phosphorylation; Polymorphism; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 2-20; 106-133 AND
RP 256-279.
RC TISSUE=Liver;
RX MEDLINE=94359612; PubMed=8078587; DOI=10.1038/371254a0;
RA Maekelae T.P., Tassan J.-P., Nigg E.A., Frutiger S., Hughes G.J.,
RA Weinberg R.A.;
RT "A cyclin associated with the CDK-activating kinase MO15.";
RL Nature 371:254-257(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 10-21; 90-102 AND
RP 190-197.
RX MEDLINE=94349374; PubMed=8069918; DOI=10.1016/0092-8674(94)90535-5;
RA Fisher R.P., Morgan D.O.;
RT "A novel cyclin associates with MO15/CDK7 to form the CDK-activating
RT kinase.";
RL Cell 78:713-724(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-28; VAL-54;
RP ARG-138 AND ALA-270.
RA Rieder M.J., Braun A.C., Montoya M.A., Chung M.-W., Nguyen C.P.,
RA Nguyen D.A., Livingston R.J., Poel C.L., Robertson P.D.,
RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-270.
RC TISSUE=Bone marrow, Brain, Embryonic brain, and Urinary bladder;
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.
RX MEDLINE=95191657; PubMed=7533895; DOI=10.1038/374283a0;
RA Shiekhattar R., Mermelstein F., Fisher R.P., Drapkin R., Dynlacht B.,
RA Wessling H.C., Morgan D.O., Reinberg D.;
RT "Cdk-activating kinase complex is a component of human transcription
RT factor TFIIH.";
RL Nature 374:283-287(1995).
RN [6]
RP FUNCTION.
RX MEDLINE=99149021; PubMed=10024882; DOI=10.1016/S1097-2765(00)80177-X;
RA Tirode F., Busso D., Coin F., Egly J.-M.;
RT "Reconstitution of the transcription factor TFIIH: assignment of
RT functions for the three enzymatic subunits, XPB, XPD, and cdk7.";
RL Mol. Cell 3:87-95(1999).
RN [7]
RP PHOSPHORYLATION SITES SER-5 AND SER-304, AND MUTAGENESIS OF SER-5 AND
RP SER-304.
RX MEDLINE=20445178; PubMed=10993082; DOI=10.1038/35024111;
RA Akoulitchev S., Chuikov S., Reinberg D.;
RT "TFIIH is negatively regulated by cdk8-containing mediator
RT complexes.";
RL Nature 407:102-106(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX MEDLINE=96433073; PubMed=8836101;
RA Kim K.K., Chamberlin H.M., Morgan D.O., Kim S.-H.;
RT "Three-dimensional structure of human cyclin H, a positive regulator
RT of the CDK-activating kinase.";
RL Nat. Struct. Biol. 3:849-855(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-287.
RX MEDLINE=97224123; PubMed=9118957; DOI=10.1093/emboj/16.5.958;
RA Andersen G., Busso D., Poterszman A., Hwang J.R., Wurtz J.M., Ripp R.,
RA Thierry J.C., Egly J.-M., Moras D.;
RT "The structure of cyclin H: common mode of kinase activation and
RT specific features.";
RL EMBO J. 16:958-967(1997).
Feature:
CHAIN 1 323 Cyclin-H.
/FTId=PRO_0000080471.
COMPBIAS 310 313 Poly-Glu.
MOD_RES 5 5 Phosphoserine (by CDK8).
MOD_RES 304 304 Phosphoserine (by CDK8).
VARIANT 28 28 R -> L (in dbSNP:2234942).
/FTId=VAR_013067.
VARIANT 54 54 M -> V (in dbSNP:3093785).
/FTId=VAR_013068.
VARIANT 138 138 K -> R (in dbSNP:2266691).
/FTId=VAR_013069.
VARIANT 270 270 V -> A (in dbSNP:2266690).
/FTId=VAR_013070.
MUTAGEN 5 5 S->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex.
MUTAGEN 304 304 S->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex.
STRAND 14 14
HELIX 16 36
TURN 37 37
STRAND 38 40
TURN 42 43
TURN 45 46
STRAND 47 47
HELIX 50 70
TURN 72 74
HELIX 77 93
STRAND 94 94
TURN 96 98
STRAND 99 99
HELIX 101 115
TURN 116 117
HELIX 122 128
STRAND 129 131
HELIX 133 153
TURN 154 156
STRAND 163 163
HELIX 164 177
TURN 179 180
HELIX 184 198
TURN 199 200
STRAND 201 201
TURN 202 202
HELIX 203 206
STRAND 207 207
HELIX 209 224
STRAND 225 225
TURN 229 230
HELIX 231 235
TURN 236 237
STRAND 238 238
STRAND 240 242
TURN 245 245
HELIX 246 260
TURN 261 261
HELIX 267 282
STRAND 283 283
STRAND 285 285
Comments:
-!- FUNCTION: Regulates CDK7, the catalytic subunit of the CDK-
activating kinase (CAK) enzymatic complex. CAK activates the
cyclin-associated kinases CDC2/CDK1, CDK2, CDK4 and CDK6 by
threonine phosphorylation. CAK complexed to the core-TFIIH basal
transcription factor activates RNA polymerase II by serine
phosphorylation of the repetitive C-terminus domain (CTD) of its
large subunit (POLR2A), allowing its escape from the promoter and
elongation of the transcripts. Involved in cell cycle control and
in RNA transcription by RNA polymerase II. Its expression and
activity are constant throughout the cell cycle.
-!- SUBUNIT: Associates primarily with CDK7 and MAT1 to form the CAK
complex. CAK can further associate with the core-TFIIH to form the
TFIIH basal transcription factor.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
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Sequence length: 323
MYHNSSQKRH WTFSSEEQLA RLRADANRKF RCKAVANGKV LPNDPVFLEP HEEMTLCKYY
EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV
SSPQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDLKTRYPI
LENPEILRKT ADDFLNRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE
NRTCLSQLLD IMKSMRNLVK KYEPPRSEEV AVLKQKLERC HSAELALNVI TKKRKGYEDD
DYVSKKSKHE EEEWTDDDLV ESL