Q6P0Q8 (MAST2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microtubule-associated serine/threonine-protein kinase 2
EC=2.7.11.1

Gene names

Name:	MAST2
Synonyms:	KIAA0807, MAST205

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1798 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. 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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of interleukin-12 biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB spermatid differentiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA microtubule cytoskeleton Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDHR2	Q9BYE9	4	EBI-493777,EBI-493793

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1798

1798

Microtubule-associated serine/threonine-protein kinase 2

PRO_0000086312

Regions

Domain

512 – 785

274

Protein kinase

Domain

786 – 854

69

AGC-kinase C-terminal

Domain

1104 – 1192

89

PDZ

Nucleotide binding

518 – 526

9

ATP By similarity UniProtKB Q9BXM7

Sites

Active site

635

1

Proton acceptor By similarity UniProtKB Q9BXM7

Binding site

541

1

ATP By similarity UniProtKB Q9BXM7

Amino acid modifications

Modified residue

74

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

148

1

Phosphoserine Ref.11 Ref.13

Modified residue

151

1

Phosphoserine By similarity

Modified residue

209

1

Phosphoserine Ref.12

Modified residue

900

1

Phosphoserine Ref.9

Modified residue

1032

1

Phosphoserine Ref.13

Modified residue

1508

1

Phosphothreonine Ref.8

Natural variations

Alternative sequence

327 – 396

70

Missing in isoform 2.

VSP_051698

Alternative sequence

1091 – 1113

23

Missing in isoform 2.

VSP_051699

Alternative sequence

1290 – 1386

97

Missing in isoform 2.

VSP_051700

Natural variant

69

1

L → F. Ref.14
Corresponds to variant rs55914403 [ dbSNP | Ensembl ].

VAR_040771

Natural variant

275

1

K → E in an ovarian mucinous carcinoma sample; somatic mutation. Ref.14

VAR_040772

Natural variant

388

1

D → E. Ref.1 Ref.14
Corresponds to variant rs11211247 [ dbSNP | Ensembl ].

VAR_040773

Natural variant

655

1

G → A in a breast mucinous carcinoma sample; somatic mutation. Ref.14

VAR_040774

Natural variant

659

1

I → M. Ref.1 Ref.3 Ref.4 Ref.14
Corresponds to variant rs1707336 [ dbSNP | Ensembl ].

VAR_040775

Natural variant

991

1

R → L. Ref.14
Corresponds to variant rs56114653 [ dbSNP | Ensembl ].

VAR_040776

Natural variant

1197

1

K → R. Ref.14
Corresponds to variant rs1052607 [ dbSNP | Ensembl ].

VAR_040777

Natural variant

1221

1

D → E. Ref.14
Corresponds to variant rs56060730 [ dbSNP | Ensembl ].

VAR_040778

Natural variant

1246

1

R → L. Ref.14
Corresponds to variant rs56309943 [ dbSNP | Ensembl ].

VAR_040779

Natural variant

1304

1

V → M. Ref.14
Corresponds to variant rs33931638 [ dbSNP | Ensembl ].

VAR_040780

Natural variant

1463

1

A → T. Ref.14
Corresponds to variant rs3737738 [ dbSNP | Ensembl ].

VAR_040781

Natural variant

1468

1

G → A. Ref.14
Corresponds to variant rs3737737 [ dbSNP | Ensembl ].

VAR_040782

Natural variant

1551

1

D → G. Ref.1 Ref.4 Ref.14
Corresponds to variant rs1052610 [ dbSNP | Ensembl ].

VAR_040783

Natural variant

1608

1

T → I.
Corresponds to variant rs35474583 [ dbSNP | Ensembl ].

VAR_051645

Natural variant

1673

1

K → R. Ref.14
Corresponds to variant rs34070850 [ dbSNP | Ensembl ].

VAR_040784

Natural variant

1703

1

G → E. Ref.14

VAR_040785

Experimental info

Sequence conflict

1225

1

Missing in AAH65499. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1798

Helix Strand Turn

Details...

Beta strand

1104 – 1108

5

Beta strand

1116 – 1124

9

Beta strand

1126 – 1129

4

Beta strand

1131 – 1140

10

Beta strand

1142 – 1145

4

Helix

1146 – 1149

4

Beta strand

1156 – 1164

9

Helix

1170 – 1180

11

Beta strand

1182 – 1188

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: DF5C92078A3451AF	FASTA	1,798	196,436
	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
	Isoform 2 [UniParc]. Checksum: E8E7D89D72A99168	FASTA	1,608	176,132
	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 KERFPKAHER SESSEVAFVM QLVKKLMIII ARPARLLECL 370 380 390 400 410 420 EFDPEEFYHL LEAAEGHAKE GQGIKCDIPR YIVSQLGLTR DPLEEMAQLS SCDSPDTPET 430 440 450 460 470 480 DDSIEGHGAS LPSKKTPSEE DFETIKLISN GAYGAVFLVR HKSTRQRFAM KKINKQNLIL 490 500 510 520 530 540 RNQIQQAFVE RDILTFAENP FVVSMFCSFD TKRHLCMVME YVEGGDCATL LKNIGALPVD 550 560 570 580 590 600 MVRLYFAETV LALEYLHNYG IVHRDLKPDN LLITSMGHIK LTDFGLSKIG LMSLTTNLYE 610 620 630 640 650 660 GHIEKDAREF LDKQVCGTPE YIAPEVILRQ GYGKPVDWWA MGIILYEFLV GCVPFFGDTP 670 680 690 700 710 720 EELFGQVISD EIVWPEGDEA LPPDAQDLTS KLLHQNPLER LGTGSAYEVK QHPFFTGLDW 730 740 750 760 770 780 TGLLRQKAEF IPQLESEDDT SYFDTRSERY HHMDSEDEEE VSEDGCLEIR QFSSCSPRFN 790 800 810 820 830 840 KVYSSMERLS LLEERRTPPP TKRSLSEEKE DHSDGLAGLK GRDRSWVIGS PEILRKRLSV 850 860 870 880 890 900 SESSHTESDS SPPMTVRRRC SGLLDAPRFP EGPEEASSTL RRQPQEGIWV LTPPSGEGVS 910 920 930 940 950 960 GPVTEHSGEQ RPKLDEEAVG RSSGSSPAME TRGRGTSQLA EGATAKAISD LAVRRARHRL 970 980 990 1000 1010 1020 LSGDSTEKRT ARPVNKVIKS ASATALSLLI PSEHHTCSPL ASPMSPHSQS SNPSSRDSSP 1030 1040 1050 1060 1070 1080 YGFTLRAIRV YMGDSDVYTV HHMVWHVEDG GPASEAGLRQ GDLITHVNGE PVHGLVHTEV 1090 1100 1110 1120 1130 1140 VELILKSGNK VAISTTPLEN TSIKVGPARK GSYKAKMARR SKRSRGKDGQ ESRKRSSLFR 1150 1160 1170 1180 1190 1200 KITKQASLLH TSRSLSSLNR SLSSGESGPG SPTHSHSLSP RSPTQGYRVT PDAVHSQLSR 1210 1220 1230 1240 1250 1260 PKSAEPPRSP LLKRVQSAEK LAAALAASEK KLATSRKHSL DLPHSELKKE LPPREVSPLE 1270 1280 1290 1300 1310 1320 VVGARSVLSG KGALPGKGVL QPAPSRALGT LRQDRAERRE SLQKQEAIRE VDSSEDDTEE 1330 1340 1350 1360 1370 1380 GPENSQGAQE LSLAPHPEVS QSVAPKGAGE SGEEDPFPSR DPRSLGPMVP SLLTGITLGP 1390 1400 1410 1420 1430 1440 PRMESPSGPH RRLGSPQAIE EAASSSSAGP NLGQSGATDP IPPEGCWKAQ HLHTQALTAL 1450 1460 1470 1480 1490 1500 SPSTSGLTPT SSCSPPSSTS GKLSMWSWKS LIEGPDRASP SRKATMAGGL ANLQDLENTT 1510 1520 1530 1540 1550 1560 PAQPKNLSPR EQGKTQPPSA PRLAHPSYED PSQGWLWESE CAQAVKEDPA LSITQVPDAS 1570 1580 1590 1600 GDRRQDVPCR GCPLTQKSEP SLRRGQEPGG HQKHRDLALV PDELLKQT

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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 , AL358075, AL603882, AL603888 Genomic DNA. Translation: CAH73244.1.
AL645480, AL358075, AL603888 Genomic DNA. Translation: CAH73245.1. Sequence problems.
AL603882 , AL358075, AL603888, AL645480 Genomic DNA. Translation: CAI16217.1.
AL603888 , AL358075, AL603882, AL645480 Genomic DNA. Translation: CAI16562.1.
AL603888, AL358075, AL645480 Genomic DNA. Translation: CAI16563.1. Sequence problems.
AL358075 , 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.

IPI

IPI00480046.
IPI00514071.

RefSeq

NP_055927.2. NM_015112.2.

UniGene

Hs.319481.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KQF	NMR	-	A	1099-1193	[»]
2KYL	NMR	-	A	1099-1193	[»]

ProteinModelPortal

Q6P0Q8.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q6P0Q8. 12 interactions.

MINT

MINT-1892333.

STRING

9606.ENSP00000354671.

PTM databases

PhosphoSite

Q6P0Q8.

Polymorphism databases

DMDM

62287152.

Proteomic databases

PaxDb

Q6P0Q8.

PRIDE

Q6P0Q8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361297; ENSP00000354671; ENSG00000086015.
ENST00000372008; ENSP00000361078; ENSG00000086015.

GeneID

23139.

KEGG

hsa:23139.

UCSC

uc001cov.3. human.

Organism-specific databases

CTD

23139.

GeneCards

GC01P046252.

H-InvDB

HIX0000540.

HGNC

HGNC:19035. MAST2.

HPA

HPA039722.
HPA040155.

MIM

612257. gene.

neXtProt

NX_Q6P0Q8.

PharmGKB

PA134954073.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG052414.

InParanoid

Q6P0Q8.

KO

K08789.

OMA

LWESECA.

OrthoDB

EOG44F68B.

Gene expression databases

ArrayExpress

Q6P0Q8.

Bgee

Q6P0Q8.

CleanEx

HS_MAST2.

Genevestigator

Q6P0Q8.

GermOnline

ENSG00000086015. Homo sapiens.

Family and domain databases

Gene3D

1.20.1480.20. 1 hit.

InterPro

IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR015022. MA_Ser/Thr_Kinase_dom.
IPR023142. MAST_pre-PK_dom.
IPR001478. PDZ.
IPR000719. Prot_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF08926. DUF1908. 1 hit.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00228. PDZ. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50156. PDZ. 1 hit.
SSF140482. SSF140482. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50106. PDZ. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MAST2. human.

GenomeRNAi

23139.

NextBio

44410.

SOURCE

Search...

Entry information

Entry name

MAST2_HUMAN

Accession

Primary (citable) accession number: Q6P0Q8
Secondary accession number(s): O94899 , Q5VT07, Q5VT08, Q7LGC4, Q8NDG1, Q96B94, Q9BYE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.