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Q6P0Q8 (MAST2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated serine/threonine-protein kinase 2

EC=2.7.11.1
Gene names
Name:MAST2
Synonyms:KIAA0807, MAST205
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1798 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation By similarity. UniProtKB Q60592

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q60592

Cofactor

Magnesium By similarity. UniProtKB Q60592

Subunit structure

Interacts with CDHR2. Ref.1

Subcellular location

Cytoplasmcytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Recruited to the sub-membranous area on interaction with CDHR2. Ref.1

Tissue specificity

Abundant in the testis. Ref.7

Post-translational modification

Phosphorylated and ubiquitinated. N-terminal ubiquitination leads to degradation of MAST2 by proteasome-mediated proteolysis. N-terminal phosphorylation appears to be a prerequisite for ubiquitination By similarity. UniProtKB Q60592

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PDZ (DHR) domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAH15816.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAH15816.2 differs from that shown. Reason: Frameshift at positions 1114 and 1387.

The sequence BAB40778.1 differs from that shown. Reason: Frameshift at position 1688.

The sequence CAH73245.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16563.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI21706.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDHR2Q9BYE94EBI-493777,EBI-493793
SLC9A3P487642EBI-493777,EBI-7816923
SLC9A3Q283622EBI-493777,EBI-7817027From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q6P0Q8-1)

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.
Isoform 2 (identifier: Q6P0Q8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     327-396: Missing.
     1091-1113: Missing.
     1290-1386: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17981798Microtubule-associated serine/threonine-protein kinase 2
PRO_0000086312

Regions

Domain512 – 785274Protein kinase
Domain786 – 85469AGC-kinase C-terminal
Domain1104 – 119289PDZ
Nucleotide binding518 – 5269ATP By similarity UniProtKB Q9BXM7

Sites

Active site6351Proton acceptor By similarity UniProtKB Q9BXM7
Binding site5411ATP By similarity UniProtKB Q9BXM7

Amino acid modifications

Modified residue741Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12
Modified residue1481Phosphoserine Ref.11 Ref.13
Modified residue2091Phosphoserine Ref.12
Modified residue9001Phosphoserine Ref.9
Modified residue10321Phosphoserine Ref.13
Modified residue13371Phosphoserine By similarity
Modified residue15081Phosphothreonine Ref.8

Natural variations

Alternative sequence327 – 39670Missing in isoform 2.
VSP_051698
Alternative sequence1091 – 111323Missing in isoform 2.
VSP_051699
Alternative sequence1290 – 138697Missing in isoform 2.
VSP_051700
Natural variant691L → F. Ref.14
Corresponds to variant rs55914403 [ dbSNP | Ensembl ].
VAR_040771
Natural variant2751K → E in an ovarian mucinous carcinoma sample; somatic mutation. Ref.14
VAR_040772
Natural variant3881D → E. Ref.1 Ref.14
Corresponds to variant rs11211247 [ dbSNP | Ensembl ].
VAR_040773
Natural variant6551G → A in a breast mucinous carcinoma sample; somatic mutation. Ref.14
VAR_040774
Natural variant6591I → M. Ref.1 Ref.3 Ref.4 Ref.14
Corresponds to variant rs1707336 [ dbSNP | Ensembl ].
VAR_040775
Natural variant9911R → L. Ref.14
Corresponds to variant rs56114653 [ dbSNP | Ensembl ].
VAR_040776
Natural variant11971K → R. Ref.14
Corresponds to variant rs1052607 [ dbSNP | Ensembl ].
VAR_040777
Natural variant12211D → E. Ref.14
Corresponds to variant rs56060730 [ dbSNP | Ensembl ].
VAR_040778
Natural variant12461R → L. Ref.14
Corresponds to variant rs56309943 [ dbSNP | Ensembl ].
VAR_040779
Natural variant13041V → M. Ref.14
Corresponds to variant rs33931638 [ dbSNP | Ensembl ].
VAR_040780
Natural variant14631A → T. Ref.14
Corresponds to variant rs3737738 [ dbSNP | Ensembl ].
VAR_040781
Natural variant14681G → A. Ref.14
Corresponds to variant rs3737737 [ dbSNP | Ensembl ].
VAR_040782
Natural variant15511D → G. Ref.1 Ref.4 Ref.14
Corresponds to variant rs1052610 [ dbSNP | Ensembl ].
VAR_040783
Natural variant16081T → I.
Corresponds to variant rs35474583 [ dbSNP | Ensembl ].
VAR_051645
Natural variant16731K → R. Ref.14
Corresponds to variant rs34070850 [ dbSNP | Ensembl ].
VAR_040784
Natural variant17031G → E. Ref.14
VAR_040785

Experimental info

Sequence conflict12251Missing in AAH65499. Ref.3

Secondary structure

.................. 1798
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: DF5C92078A3451AF

FASTA1,798196,436
        10         20         30         40         50         60 
MKRSRCRDRP QPPPPDRRED GVQRAAELSQ SLPPRRRAPP GRQRLEERTG PAGPEGKEQD 

        70         80         90        100        110        120 
VVTGVSPLLF RKLSNPDIFS STGKVKLQRQ LSQDDCKLWR GNLASSLSGK QLLPLSSSVH 

       130        140        150        160        170        180 
SSVGQVTWQS SGEASNLVRM RNQSLGQSAP SLTAGLKELS LPRRGSFCRT SNRKSLIVTS 

       190        200        210        220        230        240 
STSPTLPRPH SPLHGHTGNS PLDSPRNFSP NAPAHFSFVP ARRTDGRRWS LASLPSSGYG 

       250        260        270        280        290        300 
TNTPSSTVSS SCSSQEKLHQ LPFQPTADEL HFLTKHFSTE SVPDEEGRQS PAMRPRSRSL 

       310        320        330        340        350        360 
SPGRSPVSFD SEIIMMNHVY KERFPKATAQ MEERLAEFIS SNTPDSVLPL ADGALSFIHH 

       370        380        390        400        410        420 
QVIEMARDCL DKSRSGLITS QYFYELQDNL EKLLQDAHER SESSEVAFVM QLVKKLMIII 

       430        440        450        460        470        480 
ARPARLLECL EFDPEEFYHL LEAAEGHAKE GQGIKCDIPR YIVSQLGLTR DPLEEMAQLS 

       490        500        510        520        530        540 
SCDSPDTPET DDSIEGHGAS LPSKKTPSEE DFETIKLISN GAYGAVFLVR HKSTRQRFAM 

       550        560        570        580        590        600 
KKINKQNLIL RNQIQQAFVE RDILTFAENP FVVSMFCSFD TKRHLCMVME YVEGGDCATL 

       610        620        630        640        650        660 
LKNIGALPVD MVRLYFAETV LALEYLHNYG IVHRDLKPDN LLITSMGHIK LTDFGLSKIG 

       670        680        690        700        710        720 
LMSLTTNLYE GHIEKDAREF LDKQVCGTPE YIAPEVILRQ GYGKPVDWWA MGIILYEFLV 

       730        740        750        760        770        780 
GCVPFFGDTP EELFGQVISD EIVWPEGDEA LPPDAQDLTS KLLHQNPLER LGTGSAYEVK 

       790        800        810        820        830        840 
QHPFFTGLDW TGLLRQKAEF IPQLESEDDT SYFDTRSERY HHMDSEDEEE VSEDGCLEIR 

       850        860        870        880        890        900 
QFSSCSPRFN KVYSSMERLS LLEERRTPPP TKRSLSEEKE DHSDGLAGLK GRDRSWVIGS 

       910        920        930        940        950        960 
PEILRKRLSV SESSHTESDS SPPMTVRRRC SGLLDAPRFP EGPEEASSTL RRQPQEGIWV 

       970        980        990       1000       1010       1020 
LTPPSGEGVS GPVTEHSGEQ RPKLDEEAVG RSSGSSPAME TRGRGTSQLA EGATAKAISD 

      1030       1040       1050       1060       1070       1080 
LAVRRARHRL LSGDSTEKRT ARPVNKVIKS ASATALSLLI PSEHHTCSPL ASPMSPHSQS 

      1090       1100       1110       1120       1130       1140 
SNPSSRDSSP SRDFLPALGS MRPPIIIHRA GKKYGFTLRA IRVYMGDSDV YTVHHMVWHV 

      1150       1160       1170       1180       1190       1200 
EDGGPASEAG LRQGDLITHV NGEPVHGLVH TEVVELILKS GNKVAISTTP LENTSIKVGP 

      1210       1220       1230       1240       1250       1260 
ARKGSYKAKM ARRSKRSRGK DGQESRKRSS LFRKITKQAS LLHTSRSLSS LNRSLSSGES 

      1270       1280       1290       1300       1310       1320 
GPGSPTHSHS LSPRSPTQGY RVTPDAVHSV GGNSSQSSSP SSSVPSSPAG SGHTRPSSLH 

      1330       1340       1350       1360       1370       1380 
GLAPKLQRQY RSPRRKSAGS IPLSPLAHTP SPPPPTASPQ RSPSPLSGHV AQAFPTKLHL 

      1390       1400       1410       1420       1430       1440 
SPPLGRQLSR PKSAEPPRSP LLKRVQSAEK LAAALAASEK KLATSRKHSL DLPHSELKKE 

      1450       1460       1470       1480       1490       1500 
LPPREVSPLE VVGARSVLSG KGALPGKGVL QPAPSRALGT LRQDRAERRE SLQKQEAIRE 

      1510       1520       1530       1540       1550       1560 
VDSSEDDTEE GPENSQGAQE LSLAPHPEVS QSVAPKGAGE SGEEDPFPSR DPRSLGPMVP 

      1570       1580       1590       1600       1610       1620 
SLLTGITLGP PRMESPSGPH RRLGSPQAIE EAASSSSAGP NLGQSGATDP IPPEGCWKAQ 

      1630       1640       1650       1660       1670       1680 
HLHTQALTAL SPSTSGLTPT SSCSPPSSTS GKLSMWSWKS LIEGPDRASP SRKATMAGGL 

      1690       1700       1710       1720       1730       1740 
ANLQDLENTT PAQPKNLSPR EQGKTQPPSA PRLAHPSYED PSQGWLWESE CAQAVKEDPA 

      1750       1760       1770       1780       1790 
LSITQVPDAS GDRRQDVPCR GCPLTQKSEP SLRRGQEPGG HQKHRDLALV PDELLKQT 

« Hide

Isoform 2 [UniParc].

Checksum: E8E7D89D72A99168
Show »

FASTA1,608176,132

References

« Hide 'large scale' references
[1]"Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation."
Okazaki N., Takahashi N., Kojima S., Masuho Y., Koga H.
Carcinogenesis 23:1139-1148(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLU-388; MET-659 AND GLY-1551, SUBCELLULAR LOCATION, INTERACTION WITH CDHR2.
Tissue: Brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-1798 (ISOFORM 2), VARIANT MET-659.
Tissue: Lymph and Placenta.
[4]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 470-1797 (ISOFORM 1), VARIANTS MET-659 AND GLY-1551.
Tissue: Brain.
[5]Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 833-1797 (ISOFORM 1).
Tissue: Testis.
[7]"Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis."
Walden P.D., Millette C.F.
Biol. Reprod. 55:1039-1044(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[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 THR-1508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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 SER-74 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-148 AND SER-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-69; GLU-275; GLU-388; ALA-655; MET-659; LEU-991; ARG-1197; GLU-1221; LEU-1246; MET-1304; THR-1463; ALA-1468; GLY-1551; ARG-1673 AND GLU-1703.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB047005 mRNA. Translation: BAB40778.1. Frameshift.
AL645480 expand/collapse EMBL AC list , AL358075, AL603882, AL603888 Genomic DNA. Translation: CAH73244.1.
AL645480, AL358075, AL603888 Genomic DNA. Translation: CAH73245.1. Sequence problems.
AL603882 expand/collapse EMBL AC list , AL358075, AL603888, AL645480 Genomic DNA. Translation: CAI16217.1.
AL603888 expand/collapse EMBL AC list , AL358075, AL603882, AL645480 Genomic DNA. Translation: CAI16562.1.
AL603888, AL358075, AL645480 Genomic DNA. Translation: CAI16563.1. Sequence problems.
AL358075 expand/collapse EMBL AC list , AL603882, AL603888, AL645480 Genomic DNA. Translation: CAI21705.1.
AL358075, AL603888, AL645480 Genomic DNA. Translation: CAI21706.1. Sequence problems.
BC015816 mRNA. Translation: AAH15816.2. Different initiation.
BC065499 mRNA. Translation: AAH65499.1.
AB018350 mRNA. Translation: BAA34527.2.
AL833919 mRNA. Translation: CAD38775.1.
CCDSCCDS41326.1. [Q6P0Q8-1]
RefSeqNP_055927.2. NM_015112.2. [Q6P0Q8-1]
XP_005270711.1. XM_005270654.1.
UniGeneHs.319481.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KQFNMR-A1099-1193[»]
2KYLNMR-A1099-1193[»]
ProteinModelPortalQ6P0Q8.
SMRQ6P0Q8. Positions 325-849, 1099-1193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116756. 17 interactions.
IntActQ6P0Q8. 18 interactions.
MINTMINT-1892333.
STRING9606.ENSP00000354671.

Chemistry

ChEMBLCHEMBL3038500.

PTM databases

PhosphoSiteQ6P0Q8.

Polymorphism databases

DMDM62287152.

Proteomic databases

MaxQBQ6P0Q8.
PaxDbQ6P0Q8.
PRIDEQ6P0Q8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361297; ENSP00000354671; ENSG00000086015. [Q6P0Q8-1]
GeneID23139.
KEGGhsa:23139.
UCSCuc001cov.3. human. [Q6P0Q8-1]

Organism-specific databases

CTD23139.
GeneCardsGC01P046252.
H-InvDBHIX0000540.
HGNCHGNC:19035. MAST2.
HPAHPA039722.
HPA040155.
MIM612257. gene.
neXtProtNX_Q6P0Q8.
PharmGKBPA134954073.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG052414.
InParanoidQ6P0Q8.
KOK08789.
OMADMPRFAI.
OrthoDBEOG7PK8ZC.
PhylomeDBQ6P0Q8.
TreeFamTF313149.

Enzyme and pathway databases

SignaLinkQ6P0Q8.

Gene expression databases

ArrayExpressQ6P0Q8.
BgeeQ6P0Q8.
CleanExHS_MAST2.
GenevestigatorQ6P0Q8.

Family and domain databases

Gene3D1.20.1480.20. 1 hit.
2.30.42.10. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR015022. MA_Ser/Thr_Kinase_dom.
IPR028779. MAST2.
IPR023142. MAST_pre-PK_dom.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24356:SF136. PTHR24356:SF136. 1 hit.
PfamPF08926. DUF1908. 1 hit.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF140482. SSF140482. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAST2. human.
GeneWikiMAST2.
GenomeRNAi23139.
NextBio44410.
PROQ6P0Q8.
SOURCESearch...

Entry information

Entry nameMAST2_HUMAN
AccessionPrimary (citable) accession number: Q6P0Q8
Secondary accession number(s): O94899 expand/collapse secondary AC list , Q5VT07, Q5VT08, Q7LGC4, Q8NDG1, Q96B94, Q9BYE8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM