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   27-MAR-2024, entry version 188.
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="https://atlasgeneticsoncology.org/gene/89/MTCP1";
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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; 9606-ENSP00000358488; -.
DR   PeptideAtlas; P56278; -.
DR   ProteomicsDB; 56909; -. [P56278-1]
DR   Antibodypedia; 31399; 63 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   AGR; HGNC:7423; -.
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; VYCDENQ; -.
DR   OrthoDB; 4369305at2759; -.
DR   PhylomeDB; P56278; -.
DR   TreeFam; TF337903; -.
DR   PathwayCommons; P56278; -.
DR   SignaLink; P56278; -.
DR   SIGNOR; P56278; -.
DR   BioGRID-ORCS; 4515; 10 hits in 753 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 male germ line stem cell (sensu Vertebrata) in testis and 105 other cell types or tissues.
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:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IBA:GO_Central.
DR   Gene3D; 2.40.15.10; TCL1/MTCP1; 1.
DR   InterPro; IPR004832; TCL1_MTCP1.
DR   InterPro; IPR036672; TCL1_MTCP1_sf.
DR   PANTHER; PTHR14060; PROTEIN P13 MTCP-1; 1.
DR   PANTHER; PTHR14060:SF8; PROTEIN P13 MTCP-1; 1.
DR   Pfam; PF01840; TCL1_MTCP1; 1.
DR   SUPFAM; SSF50904; Oncogene products; 1.
DR   Genevisible; P56278; HS.
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
//