MTCP1_HUMAN
ID MTCP1_HUMAN Reviewed; 107 AA.
AC P56278; Q5HYP2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein p13 MTCP-1;
DE Short=p13MTCP1;
DE AltName: Full=Mature T-cell proliferation-1 type B1;
DE Short=MTCP-1 type B1;
GN Name=MTCP1; Synonyms=C6.1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RC TISSUE=T-cell;
RX PubMed=8361760;
RA Stern M.-H., Soulier J., Rosenzwajg M., Nakahara K., Canki-Klain N.,
RA Aurias A., Sigaux F., Kirsch I.R.;
RT "MTCP-1: a novel gene on the human chromosome Xq28 translocated to the T
RT cell receptor alpha/delta locus in mature T cell proliferations.";
RL Oncogene 8:2475-2483(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH AKT1 AND AKT2.
RX PubMed=10983986; DOI=10.1016/s1097-2765(00)00039-3;
RA Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.;
RT "The protooncogene TCL1 is an Akt kinase coactivator.";
RL Mol. Cell 6:395-407(2000).
RN [5]
RP LACK OF INTERACTION WITH AKT3.
RX PubMed=11707444; DOI=10.1074/jbc.m107069200;
RA Laine J., Kuenstle G., Obata T., Noguchi M.;
RT "Differential regulation of Akt kinase isoforms by the members of the TCL1
RT oncogene family.";
RL J. Biol. Chem. 277:3743-3751(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9520380; DOI=10.1073/pnas.95.7.3413;
RA Fu Z.Q., du Bois G.C., Song S.P., Kulikovskaya I., Virgilio L.,
RA Rothstein J.L., Croce C.M., Weber I.T., Harrison R.W.;
RT "Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in
RT T cell malignancies.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3413-3418(1998).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=10959629; DOI=10.1023/a:1008386110930;
RA Guignard L., Padilla A., Mispelter J., Yang Y.-S., Stern M.-H.,
RA Lhoste J.-M., Roumestand C.;
RT "Backbone dynamics and solution structure refinement of the 15N-labeled
RT human oncogenic protein p13MTCP1: comparison with X-ray data.";
RL J. Biomol. NMR 17:215-230(2000).
CC -!- FUNCTION: Enhances the phosphorylation and activation of AKT1 and AKT2.
CC {ECO:0000269|PubMed:10983986}.
CC -!- SUBUNIT: Interacts with AKT1 and AKT2 (via PH domain). Does not
CC interact with AKT3. {ECO:0000269|PubMed:10983986}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Long, Type B1, p13 MTCP1;
CC IsoId=P56278-1; Sequence=Displayed;
CC Name=1; Synonyms=Short, Type A, p8 MTCP1;
CC IsoId=P56277-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Not found at a significant level in any tissue.
CC -!- DISEASE: Note=Detected in T-cell leukemia bearing a t(X;14)
CC translocation. Plays a key role in T-cell prolymphocytic leukemia.
CC -!- MISCELLANEOUS: [Isoform 2]: Shares a non-coding 5' exon with isoform 1
CC which is spliced to a different set of 3' exons encoding an unrelated
CC protein.
CC -!- SIMILARITY: Belongs to the TCL1 family. {ECO:0000305}.
CC -!- CAUTION: MTCP1 and MTCP1NB are transcribed from the same promoter and
CC could be considered the same gene. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MTCP1ID89.html";
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DR EMBL; Z24459; CAA80828.1; -; Genomic_DNA.
DR EMBL; BX470111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72642.1; -; Genomic_DNA.
DR CCDS; CCDS44027.1; -. [P56278-1]
DR PIR; S78532; S78532.
DR RefSeq; NP_001018025.1; NM_001018025.3. [P56278-1]
DR PDB; 1A1X; X-ray; 2.00 A; A=2-107.
DR PDB; 1QTT; NMR; -; A=1-107.
DR PDB; 1QTU; NMR; -; A=1-107.
DR PDBsum; 1A1X; -.
DR PDBsum; 1QTT; -.
DR PDBsum; 1QTU; -.
DR AlphaFoldDB; P56278; -.
DR SMR; P56278; -.
DR BioGRID; 110618; 5.
DR STRING; 9606.ENSP00000358488; -.
DR BioMuta; MTCP1; -.
DR MassIVE; P56278; -.
DR MaxQB; P56278; -.
DR PaxDb; P56278; -.
DR PeptideAtlas; P56278; -.
DR PRIDE; P56278; -.
DR ProteomicsDB; 56909; -. [P56278-1]
DR Antibodypedia; 31399; 62 antibodies from 13 providers.
DR DNASU; 4515; -.
DR Ensembl; ENST00000362018.2; ENSP00000355058.2; ENSG00000214827.11. [P56278-1]
DR Ensembl; ENST00000369476.8; ENSP00000358488.3; ENSG00000214827.11. [P56278-1]
DR GeneID; 4515; -.
DR KEGG; hsa:4515; -.
DR MANE-Select; ENST00000369476.8; ENSP00000358488.3; NM_001018025.4; NP_001018025.1.
DR UCSC; uc004fmz.3; human. [P56278-1]
DR CTD; 4515; -.
DR DisGeNET; 4515; -.
DR GeneCards; MTCP1; -.
DR HGNC; HGNC:7423; MTCP1.
DR HPA; ENSG00000214827; Low tissue specificity.
DR MIM; 300116; gene.
DR neXtProt; NX_P56278; -.
DR OpenTargets; ENSG00000214827; -.
DR PharmGKB; PA164742098; -.
DR VEuPathDB; HostDB:ENSG00000214827; -.
DR eggNOG; ENOG502S5U8; Eukaryota.
DR GeneTree; ENSGT00390000006885; -.
DR HOGENOM; CLU_168379_0_0_1; -.
DR InParanoid; P56278; -.
DR OMA; REGIYRD; -.
DR OrthoDB; 1496659at2759; -.
DR PhylomeDB; P56278; -.
DR TreeFam; TF337903; -.
DR PathwayCommons; P56278; -.
DR SignaLink; P56278; -.
DR SIGNOR; P56278; -.
DR BioGRID-ORCS; 4515; 10 hits in 682 CRISPR screens.
DR ChiTaRS; MTCP1; human.
DR EvolutionaryTrace; P56278; -.
DR GeneWiki; MTCP1; -.
DR GenomeRNAi; 4515; -.
DR Pharos; P56278; Tbio.
DR PRO; PR:P56278; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P56278; protein.
DR Bgee; ENSG00000214827; Expressed in adrenal tissue and 103 other tissues.
DR Genevisible; P56278; HS.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR Gene3D; 2.40.15.10; -; 1.
DR InterPro; IPR004832; TCL1_MTCP1.
DR InterPro; IPR036672; TCL1_MTCP1_sf.
DR PANTHER; PTHR14060; PTHR14060; 1.
DR Pfam; PF01840; TCL1_MTCP1; 1.
DR SUPFAM; SSF50904; SSF50904; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement;
KW Proto-oncogene; Reference proteome.
FT CHAIN 1..107
FT /note="Protein p13 MTCP-1"
FT /id="PRO_0000184486"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:1A1X"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1A1X"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1A1X"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1A1X"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1A1X"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1A1X"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1A1X"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1A1X"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1A1X"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1A1X"
SQ SEQUENCE 107 AA; 12600 MW; C00967E1AECDDDCA CRC64;
MAGEDVGAPP DHLWVHQEGI YRDEYQRTWV AVVEEETSFL RARVQQIQVP LGDAARPSHL
LTSQLPLMWQ LYPEERYMDN NSRLWQIQHH LMVRGVQELL LKLLPDD
