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Protein

Protein p13 MTCP-1

Gene

MTCP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Enhances the phosphorylation and activation of AKT1 and AKT2.1 Publication

GO - Biological processi

  1. cell proliferation Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein p13 MTCP-1
Short name:
p13MTCP1
Alternative name(s):
Mature T-cell proliferation-1 type B1
Short name:
MTCP-1 type B1
Gene namesi
Name:MTCP1
Synonyms:C6.1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7423. MTCP1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Detected in T-cell leukemia bearing a t(X;14) translocation. Plays a key role in T-cell prolymphocytic leukemia.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA164742098.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Protein p13 MTCP-1PRO_0000184486Add
BLAST

Proteomic databases

MaxQBiP56278.
PRIDEiP56278.

Expressioni

Tissue specificityi

Not found at a significant level in any tissue.

Gene expression databases

BgeeiP56278.
CleanExiHS_MTCP1.
GenevestigatoriP56278.

Interactioni

Subunit structurei

Interacts with AKT1 and AKT2 (via PH domain). Does not interact with AKT3.1 Publication

Protein-protein interaction databases

BioGridi110618. 5 interactions.
MINTiMINT-1484922.
STRINGi9606.ENSP00000329343.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 177Combined sources
Beta strandi20 – 234Combined sources
Beta strandi28 – 358Combined sources
Beta strandi40 – 456Combined sources
Helixi57 – 604Combined sources
Beta strandi67 – 726Combined sources
Turni73 – 753Combined sources
Beta strandi76 – 794Combined sources
Beta strandi84 – 9310Combined sources
Beta strandi96 – 1038Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1XX-ray2.00A2-107[»]
1QTTNMR-A1-107[»]
1QTUNMR-A1-107[»]
ProteinModelPortaliP56278.
SMRiP56278. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56278.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCL1 family.Curated

Phylogenomic databases

eggNOGiNOG76642.
GeneTreeiENSGT00390000006885.
HOGENOMiHOG000037945.
HOVERGENiHBG052523.
InParanoidiP56278.
KOiK16837.
OMAiVHQEGVY.
PhylomeDBiP56278.
TreeFamiTF337903.

Family and domain databases

Gene3Di2.40.15.10. 1 hit.
InterProiIPR004832. TCL1_MTCP1.
[Graphical view]
PfamiPF01840. TCL1_MTCP1. 1 hit.
[Graphical view]
ProDomiPD015575. TCL1_MTCP1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50904. SSF50904. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: P56278-1) [UniParc]FASTAAdd to Basket

Also known as: Long, Type B1, p13 MTCP1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGEDVGAPP DHLWVHQEGI YRDEYQRTWV AVVEEETSFL RARVQQIQVP
60 70 80 90 100
LGDAARPSHL LTSQLPLMWQ LYPEERYMDN NSRLWQIQHH LMVRGVQELL

LKLLPDD

Note: Shares a non-coding 5' exon with isoform 1 which is spliced to a different set of 3' exons encoding an unrelated protein.

Length:107
Mass (Da):12,600
Last modified:July 15, 1998 - v1
Checksum:iC00967E1AECDDDCA
GO
Isoform 1 (identifier: P56277-1) [UniParc]FASTAAdd to Basket

Also known as: Short, Type A, p8 MTCP1

The sequence of this isoform can be found in the external entry P56277.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Shares a non-coding 5' exon with isoform 2 which is spliced to a different set of 3' exons encoding an unrelated protein.

Length:68
Mass (Da):7,747
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z24459 Genomic DNA. Translation: CAA80828.1.
BX470111 Genomic DNA. Translation: CAI41656.1.
CH471172 Genomic DNA. Translation: EAW72642.1.
CCDSiCCDS44027.1. [P56278-1]
PIRiS78532.
RefSeqiNP_001018025.1. NM_001018025.3. [P56278-1]
UniGeneiHs.6917.

Genome annotation databases

EnsembliENST00000362018; ENSP00000355058; ENSG00000214827. [P56278-1]
ENST00000369476; ENSP00000358488; ENSG00000214827. [P56278-1]
GeneIDi4515.
KEGGihsa:4515.
UCSCiuc004fmz.2. human. [P56278-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z24459 Genomic DNA. Translation: CAA80828.1.
BX470111 Genomic DNA. Translation: CAI41656.1.
CH471172 Genomic DNA. Translation: EAW72642.1.
CCDSiCCDS44027.1. [P56278-1]
PIRiS78532.
RefSeqiNP_001018025.1. NM_001018025.3. [P56278-1]
UniGeneiHs.6917.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1XX-ray2.00A2-107[»]
1QTTNMR-A1-107[»]
1QTUNMR-A1-107[»]
ProteinModelPortaliP56278.
SMRiP56278. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110618. 5 interactions.
MINTiMINT-1484922.
STRINGi9606.ENSP00000329343.

Proteomic databases

MaxQBiP56278.
PRIDEiP56278.

Protocols and materials databases

DNASUi4515.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000362018; ENSP00000355058; ENSG00000214827. [P56278-1]
ENST00000369476; ENSP00000358488; ENSG00000214827. [P56278-1]
GeneIDi4515.
KEGGihsa:4515.
UCSCiuc004fmz.2. human. [P56278-1]

Organism-specific databases

CTDi4515.
GeneCardsiGC0XM154290.
HGNCiHGNC:7423. MTCP1.
MIMi300116. gene.
neXtProtiNX_P56278.
PharmGKBiPA164742098.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG76642.
GeneTreeiENSGT00390000006885.
HOGENOMiHOG000037945.
HOVERGENiHBG052523.
InParanoidiP56278.
KOiK16837.
OMAiVHQEGVY.
PhylomeDBiP56278.
TreeFamiTF337903.

Miscellaneous databases

EvolutionaryTraceiP56278.
GeneWikiiMTCP1.
GenomeRNAii4515.
NextBioi17437.
PROiP56278.
SOURCEiSearch...

Gene expression databases

BgeeiP56278.
CleanExiHS_MTCP1.
GenevestigatoriP56278.

Family and domain databases

Gene3Di2.40.15.10. 1 hit.
InterProiIPR004832. TCL1_MTCP1.
[Graphical view]
PfamiPF01840. TCL1_MTCP1. 1 hit.
[Graphical view]
ProDomiPD015575. TCL1_MTCP1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50904. SSF50904. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MTCP-1: a novel gene on the human chromosome Xq28 translocated to the T cell receptor alpha/delta locus in mature T cell proliferations."
    Stern M.-H., Soulier J., Rosenzwajg M., Nakahara K., Canki-Klain N., Aurias A., Sigaux F., Kirsch I.R.
    Oncogene 8:2475-2483(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
    Tissue: T-cell.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The protooncogene TCL1 is an Akt kinase coactivator."
    Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.
    Mol. Cell 6:395-407(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AKT1 AND AKT2.
  5. "Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family."
    Laine J., Kuenstle G., Obata T., Noguchi M.
    J. Biol. Chem. 277:3743-3751(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF INTERACTION WITH AKT3.
  6. "Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies."
    Fu Z.Q., du Bois G.C., Song S.P., Kulikovskaya I., Virgilio L., Rothstein J.L., Croce C.M., Weber I.T., Harrison R.W.
    Proc. Natl. Acad. Sci. U.S.A. 95:3413-3418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  7. "Backbone dynamics and solution structure refinement of the 15N-labeled human oncogenic protein p13MTCP1: comparison with X-ray data."
    Guignard L., Padilla A., Mispelter J., Yang Y.-S., Stern M.-H., Lhoste J.-M., Roumestand C.
    J. Biomol. NMR 17:215-230(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiMTCP1_HUMAN
AccessioniPrimary (citable) accession number: P56278
Secondary accession number(s): Q5HYP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 7, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.