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Protein

MKL/myocardin-like protein 1

Gene

MKL1

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

Functioni

Transcriptional coactivator of serum response factor (SRF) with the potential to modulate SRF target genes. Suppresses TNF-induced cell death by inhibiting activation of caspases; its transcriptional activity is indispensable for the antiapoptotic function. It may up-regulate antiapoptotic molecules, which in turn inhibit caspase activation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei3 – 42Breakpoint for translocation to form RBM15-MKL1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_355252. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
MKL/myocardin-like protein 1
Alternative name(s):
Megakaryoblastic leukemia 1 protein
Megakaryocytic acute leukemia protein
Myocardin-related transcription factor A
Short name:
MRTF-A
Gene namesi
Name:MKL1
Synonyms:KIAA1438, MAL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:14334. MKL1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving MKL1 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with RBM15. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti402023. 'Megakaryoblastic acute myeloid leukemia with t(1;22)(p13;q13)'.
PharmGKBiPA30827.

Polymorphism and mutation databases

BioMutaiMKL1.
DMDMi32363202.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 931931MKL/myocardin-like protein 1PRO_0000126625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine2 Publications
Modified residuei305 – 3051Phosphothreonine1 Publication
Modified residuei385 – 3851Phosphoserine1 Publication
Modified residuei450 – 4501Phosphothreonine3 Publications
Modified residuei454 – 4541Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ969V6.
PaxDbiQ969V6.
PRIDEiQ969V6.

PTM databases

PhosphoSiteiQ969V6.

Expressioni

Tissue specificityi

Ubiquitously expressed, has been detected in lung, placenta, small intestine, liver, kidney, spleen, thymus, colon, muscle, heart and brain.

Gene expression databases

BgeeiQ969V6.
CleanExiHS_MAL.
HS_MKL1.
ExpressionAtlasiQ969V6. baseline and differential.
GenevisibleiQ969V6. HS.

Organism-specific databases

HPAiHPA030782.

Interactioni

Subunit structurei

Forms with SCAI and SRF a nuclear ternary complex which binds the CArG consensus motif (CArG box) on DNA via SRF. Interacts with ACTB; interaction with ACTB prevents interaction with SCAI. Interacts with MKL2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SRFP118312EBI-493122,EBI-493034

Protein-protein interaction databases

BioGridi121642. 14 interactions.
IntActiQ969V6. 4 interactions.
MINTiMINT-4713067.
STRINGi9606.ENSP00000347847.

Structurei

Secondary structure

1
931
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni345 – 3495Combined sources
Helixi352 – 36110Combined sources
Helixi370 – 38213Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi392 – 3943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KVUNMR-A336-396[»]
2KW9NMR-A336-396[»]
ProteinModelPortaliQ969V6.
SMRiQ969V6. Positions 1-91, 333-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ969V6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati24 – 4926RPEL 1Add
BLAST
Repeati68 – 9326RPEL 2Add
BLAST
Domaini347 – 38135SAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 256256Mediates interaction with SCAI and ACTBBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili515 – 56349Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi264 – 28623Gln-richAdd
BLAST
Compositional biasi564 – 811248Pro-richAdd
BLAST

Domaini

The N-terminal region is required for nuclear localization and the C-terminal region mediates transcriptional activity.By similarity
The RPEL repeats mediate binding to globular actin.By similarity

Sequence similaritiesi

Contains 2 RPEL repeats.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG82832.
GeneTreeiENSGT00530000063195.
HOGENOMiHOG000038001.
HOVERGENiHBG036493.
InParanoidiQ969V6.
OrthoDBiEOG7FR7G1.
PhylomeDBiQ969V6.
TreeFamiTF326024.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR029992. MRTF-A.
IPR004018. RPEL_repeat.
IPR003034. SAP_dom.
[Graphical view]
PANTHERiPTHR22793:SF6. PTHR22793:SF6. 1 hit.
PfamiPF02755. RPEL. 2 hits.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00707. RPEL. 2 hits.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51073. RPEL. 2 hits.
PS50800. SAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q969V6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPLKSPAAF HEQRRSLERA RTEDYLKRKI RSRPERSELV RMHILEETSA
60 70 80 90 100
EPSLQAKQLK LKRARLADDL NEKIAQRPGP MELVEKNILP VESSLKEAII
110 120 130 140 150
VGQVNYPKVA DSSSFDEDSS DALSPEQPAS HESQGSVPSP LEARVSEPLL
160 170 180 190 200
SATSASPTQV VSQLPMGRDS REMLFLAEQP PLPPPPLLPP SLTNGTTIPT
210 220 230 240 250
AKSTPTLIKQ SQPKSASEKS QRSKKAKELK PKVKKLKYHQ YIPPDQKQDR
260 270 280 290 300
GAPPMDSSYA KILQQQQLFL QLQILNQQQQ QHHNYQAILP APPKSAGEAL
310 320 330 340 350
GSSGTPPVRS LSTTNSSSSS GAPGPCGLAR QNSTSLTGKP GALPANLDDM
360 370 380 390 400
KVAELKQELK LRSLPVSGTK TELIERLRAY QDQISPVPGA PKAPAATSIL
410 420 430 440 450
HKAGEVVVAF PAARLSTGPA LVAAGLAPAE VVVATVASSG VVKFGSTGST
460 470 480 490 500
PPVSPTPSER SLLSTGDENS TPGDTFGEMV TSPLTQLTLQ ASPLQILVKE
510 520 530 540 550
EGPRAGSCCL SPGGRAELEG RDKDQMLQEK DKQIEALTRM LRQKQQLVER
560 570 580 590 600
LKLQLEQEKR AQQPAPAPAP LGTPVKQENS FSSCQLSQQP LGPAHPFNPS
610 620 630 640 650
LAAPATNHID PCAVAPGPPS VVVKQEALQP EPEPVPAPQL LLGPQGPSLI
660 670 680 690 700
KGVAPPTLIT DSTGTHLVLT VTNKNADSPG LSSGSPQQPS SQPGSPAPAP
710 720 730 740 750
SAQMDLEHPL QPLFGTPTSL LKKEPPGYEE AMSQQPKQQE NGSSSQQMDD
760 770 780 790 800
LFDILIQSGE ISADFKEPPS LPGKEKPSPK TVCGSPLAAQ PSPSAELPQA
810 820 830 840 850
APPPPGSPSL PGRLEDFLES STGLPLLTSG HDGPEPLSLI DDLHSQMLSS
860 870 880 890 900
TAILDHPPSP MDTSELHFVP EPSSTMGLDL ADGHLDSMDW LELSSGGPVL
910 920 930
SLAPLSTTAP SLFSTDFLDG HDLQLHWDSC L
Length:931
Mass (Da):98,919
Last modified:December 1, 2001 - v1
Checksum:i6EDE5E2C56D89609
GO

Sequence cautioni

The sequence AAK56920.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA92676.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC38828.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC38829.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti648 – 6481S → G.2 Publications
Corresponds to variant rs878756 [ dbSNP | Ensembl ].
VAR_021409

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297257 mRNA. Translation: CAC38826.1.
AF364035 mRNA. Translation: AAK56920.1. Different initiation.
CR456522 mRNA. Translation: CAG30408.1.
AJ297258 mRNA. Translation: CAC38827.1.
AF368061 mRNA. Translation: AAK54721.1.
AJ303089 mRNA. Translation: CAC38828.1. Different initiation.
AJ303090 mRNA. Translation: CAC38829.1. Different initiation.
AB037859 mRNA. Translation: BAA92676.2. Different initiation.
AL022238 Genomic DNA. Translation: CAI18985.1.
AL713710 mRNA. Translation: CAD28507.2.
CCDSiCCDS14003.1.
RefSeqiNP_001269589.1. NM_001282660.1.
NP_001269590.1. NM_001282661.1.
NP_065882.1. NM_020831.4.
XP_005261751.1. XM_005261694.1.
UniGeneiHs.654688.

Genome annotation databases

EnsembliENST00000355630; ENSP00000347847; ENSG00000196588.
ENST00000407029; ENSP00000385835; ENSG00000196588.
GeneIDi57591.
KEGGihsa:57591.
UCSCiuc003ayv.1. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297257 mRNA. Translation: CAC38826.1.
AF364035 mRNA. Translation: AAK56920.1. Different initiation.
CR456522 mRNA. Translation: CAG30408.1.
AJ297258 mRNA. Translation: CAC38827.1.
AF368061 mRNA. Translation: AAK54721.1.
AJ303089 mRNA. Translation: CAC38828.1. Different initiation.
AJ303090 mRNA. Translation: CAC38829.1. Different initiation.
AB037859 mRNA. Translation: BAA92676.2. Different initiation.
AL022238 Genomic DNA. Translation: CAI18985.1.
AL713710 mRNA. Translation: CAD28507.2.
CCDSiCCDS14003.1.
RefSeqiNP_001269589.1. NM_001282660.1.
NP_001269590.1. NM_001282661.1.
NP_065882.1. NM_020831.4.
XP_005261751.1. XM_005261694.1.
UniGeneiHs.654688.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KVUNMR-A336-396[»]
2KW9NMR-A336-396[»]
ProteinModelPortaliQ969V6.
SMRiQ969V6. Positions 1-91, 333-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121642. 14 interactions.
IntActiQ969V6. 4 interactions.
MINTiMINT-4713067.
STRINGi9606.ENSP00000347847.

PTM databases

PhosphoSiteiQ969V6.

Polymorphism and mutation databases

BioMutaiMKL1.
DMDMi32363202.

Proteomic databases

MaxQBiQ969V6.
PaxDbiQ969V6.
PRIDEiQ969V6.

Protocols and materials databases

DNASUi57591.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355630; ENSP00000347847; ENSG00000196588.
ENST00000407029; ENSP00000385835; ENSG00000196588.
GeneIDi57591.
KEGGihsa:57591.
UCSCiuc003ayv.1. human.

Organism-specific databases

CTDi57591.
GeneCardsiGC22M040908.
HGNCiHGNC:14334. MKL1.
HPAiHPA030782.
MIMi606078. gene.
neXtProtiNX_Q969V6.
Orphaneti402023. 'Megakaryoblastic acute myeloid leukemia with t(1;22)(p13;q13)'.
PharmGKBiPA30827.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG82832.
GeneTreeiENSGT00530000063195.
HOGENOMiHOG000038001.
HOVERGENiHBG036493.
InParanoidiQ969V6.
OrthoDBiEOG7FR7G1.
PhylomeDBiQ969V6.
TreeFamiTF326024.

Enzyme and pathway databases

ReactomeiREACT_355252. RHO GTPases Activate Formins.

Miscellaneous databases

ChiTaRSiMKL1. human.
EvolutionaryTraceiQ969V6.
GeneWikiiMKL1.
GenomeRNAii57591.
NextBioi64178.
PROiQ969V6.
SOURCEiSearch...

Gene expression databases

BgeeiQ969V6.
CleanExiHS_MAL.
HS_MKL1.
ExpressionAtlasiQ969V6. baseline and differential.
GenevisibleiQ969V6. HS.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR029992. MRTF-A.
IPR004018. RPEL_repeat.
IPR003034. SAP_dom.
[Graphical view]
PANTHERiPTHR22793:SF6. PTHR22793:SF6. 1 hit.
PfamiPF02755. RPEL. 2 hits.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00707. RPEL. 2 hits.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51073. RPEL. 2 hits.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fusion of two novel genes, RBM15 and MKL1, in the t(1;22)(p13;q13) of acute megakaryoblastic leukemia."
    Ma Z., Morris S.W., Valentine V., Li M., Herbrick J.-A., Cui X., Bouman D., Li Y., Mehta P.K., Nizetic D., Kaneko Y., Chan G.C.F., Chan L.C., Squire J., Scherer S.W., Hitzler J.K.
    Nat. Genet. 28:220-221(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH RBM15.
  2. "Involvement of a human gene related to the Drosophila spen gene in the recurrent t(1;22) translocation of acute megakaryocytic leukemia."
    Mercher T., Coniat M.B.-L., Monni R., Mauchauffe M., Khac F.N., Gressin L., Mugneret F., Leblanc T., Dastugue N., Berger R., Bernard O.A.
    Proc. Natl. Acad. Sci. U.S.A. 98:5776-5779(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH RBM15.
    Tissue: Blood.
  3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-648.
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-931, VARIANT GLY-648.
    Tissue: Testis.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305 AND THR-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin."
    Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P., Grosse R.
    Nat. Cell Biol. 11:557-568(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAI AND SRF, SUBCELLULAR LOCATION.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450 AND SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-450 AND SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Redox modification of nuclear actin by MICAL-2 regulates SRF signaling."
    Lundquist M.R., Storaska A.J., Liu T.C., Larsen S.D., Evans T., Neubig R.R., Jaffrey S.R.
    Cell 156:563-576(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Northeast structural genomics consortium target HR4547E."
    Northeast structural genomics consortium (NESG)
    Submitted (JUN-2010) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 336-396.

Entry informationi

Entry nameiMKL1_HUMAN
AccessioniPrimary (citable) accession number: Q969V6
Secondary accession number(s): Q8TCL1
, Q96SC5, Q96SC6, Q9P2B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 138 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 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.