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Q6P0Q8

- MAST2_HUMAN

UniProt

Q6P0Q8 - MAST2_HUMAN

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Protein

Microtubule-associated serine/threonine-protein kinase 2

Gene

MAST2

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

Functioni

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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei541 – 5411ATPBy similarityPROSITE-ProRule annotation
Active sitei635 – 6351Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi518 – 5269ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. phosphatase binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein phosphorylation Source: UniProtKB
  2. regulation of interleukin-12 biosynthetic process Source: UniProtKB
  3. spermatid differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ6P0Q8.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated serine/threonine-protein kinase 2 (EC:2.7.11.1)
Gene namesi
Name:MAST2Imported
Synonyms:KIAA0807Imported, MAST205Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:19035. MAST2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. microtubule cytoskeleton Source: Ensembl
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134954073.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17981798Microtubule-associated serine/threonine-protein kinase 2PRO_0000086312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741Phosphoserine4 Publications
Modified residuei148 – 1481Phosphoserine2 Publications
Modified residuei209 – 2091Phosphoserine1 Publication
Modified residuei900 – 9001Phosphoserine1 Publication
Modified residuei1032 – 10321Phosphoserine1 Publication
Modified residuei1337 – 13371PhosphoserineBy similarity
Modified residuei1508 – 15081Phosphothreonine1 Publication

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6P0Q8.
PaxDbiQ6P0Q8.
PRIDEiQ6P0Q8.

PTM databases

PhosphoSiteiQ6P0Q8.

Expressioni

Tissue specificityi

Abundant in the testis.1 Publication

Gene expression databases

BgeeiQ6P0Q8.
CleanExiHS_MAST2.
ExpressionAtlasiQ6P0Q8. baseline and differential.
GenevestigatoriQ6P0Q8.

Organism-specific databases

HPAiHPA039722.
HPA040155.

Interactioni

Subunit structurei

Interacts with CDHR2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDHR2Q9BYE94EBI-493777,EBI-493793
SLC9A3P487642EBI-493777,EBI-7816923
SLC9A3Q283622EBI-493777,EBI-7817027From a different organism.

Protein-protein interaction databases

BioGridi116756. 17 interactions.
IntActiQ6P0Q8. 18 interactions.
MINTiMINT-1892333.
STRINGi9606.ENSP00000354671.

Structurei

Secondary structure

1
1798
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1104 – 11085Combined sources
Beta strandi1116 – 11249Combined sources
Beta strandi1126 – 11294Combined sources
Beta strandi1131 – 114010Combined sources
Beta strandi1142 – 11454Combined sources
Helixi1146 – 11494Combined sources
Beta strandi1156 – 11649Combined sources
Helixi1170 – 118011Combined sources
Beta strandi1182 – 11887Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KQFNMR-A1099-1193[»]
2KYLNMR-A1099-1193[»]
ProteinModelPortaliQ6P0Q8.
SMRiQ6P0Q8. Positions 325-425, 506-849, 1099-1193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini512 – 785274Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini786 – 85469AGC-kinase C-terminalAdd
BLAST
Domaini1104 – 119289PDZPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063286.
HOVERGENiHBG052414.
InParanoidiQ6P0Q8.
KOiK08789.
OMAiDMPRFAI.
OrthoDBiEOG7PK8ZC.
PhylomeDBiQ6P0Q8.
TreeFamiTF313149.

Family and domain databases

Gene3Di1.20.1480.20. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000961. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24356:SF136. PTHR24356:SF136. 1 hit.
PfamiPF08926. DUF1908. 1 hit.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF140482. SSF140482. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q6P0Q8-1) [UniParc]FASTAAdd to Basket

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
MKRSRCRDRP QPPPPDRRED GVQRAAELSQ SLPPRRRAPP GRQRLEERTG
60 70 80 90 100
PAGPEGKEQD VVTGVSPLLF RKLSNPDIFS STGKVKLQRQ LSQDDCKLWR
110 120 130 140 150
GNLASSLSGK QLLPLSSSVH SSVGQVTWQS SGEASNLVRM RNQSLGQSAP
160 170 180 190 200
SLTAGLKELS LPRRGSFCRT SNRKSLIVTS STSPTLPRPH SPLHGHTGNS
210 220 230 240 250
PLDSPRNFSP NAPAHFSFVP ARRTDGRRWS LASLPSSGYG TNTPSSTVSS
260 270 280 290 300
SCSSQEKLHQ LPFQPTADEL HFLTKHFSTE SVPDEEGRQS PAMRPRSRSL
310 320 330 340 350
SPGRSPVSFD SEIIMMNHVY KERFPKATAQ MEERLAEFIS SNTPDSVLPL
360 370 380 390 400
ADGALSFIHH QVIEMARDCL DKSRSGLITS QYFYELQDNL EKLLQDAHER
410 420 430 440 450
SESSEVAFVM QLVKKLMIII ARPARLLECL EFDPEEFYHL LEAAEGHAKE
460 470 480 490 500
GQGIKCDIPR YIVSQLGLTR DPLEEMAQLS SCDSPDTPET DDSIEGHGAS
510 520 530 540 550
LPSKKTPSEE DFETIKLISN GAYGAVFLVR HKSTRQRFAM KKINKQNLIL
560 570 580 590 600
RNQIQQAFVE RDILTFAENP FVVSMFCSFD TKRHLCMVME YVEGGDCATL
610 620 630 640 650
LKNIGALPVD MVRLYFAETV LALEYLHNYG IVHRDLKPDN LLITSMGHIK
660 670 680 690 700
LTDFGLSKIG LMSLTTNLYE GHIEKDAREF LDKQVCGTPE YIAPEVILRQ
710 720 730 740 750
GYGKPVDWWA MGIILYEFLV GCVPFFGDTP EELFGQVISD EIVWPEGDEA
760 770 780 790 800
LPPDAQDLTS KLLHQNPLER LGTGSAYEVK QHPFFTGLDW TGLLRQKAEF
810 820 830 840 850
IPQLESEDDT SYFDTRSERY HHMDSEDEEE VSEDGCLEIR QFSSCSPRFN
860 870 880 890 900
KVYSSMERLS LLEERRTPPP TKRSLSEEKE DHSDGLAGLK GRDRSWVIGS
910 920 930 940 950
PEILRKRLSV SESSHTESDS SPPMTVRRRC SGLLDAPRFP EGPEEASSTL
960 970 980 990 1000
RRQPQEGIWV LTPPSGEGVS GPVTEHSGEQ RPKLDEEAVG RSSGSSPAME
1010 1020 1030 1040 1050
TRGRGTSQLA EGATAKAISD LAVRRARHRL LSGDSTEKRT ARPVNKVIKS
1060 1070 1080 1090 1100
ASATALSLLI PSEHHTCSPL ASPMSPHSQS SNPSSRDSSP SRDFLPALGS
1110 1120 1130 1140 1150
MRPPIIIHRA GKKYGFTLRA IRVYMGDSDV YTVHHMVWHV EDGGPASEAG
1160 1170 1180 1190 1200
LRQGDLITHV NGEPVHGLVH TEVVELILKS GNKVAISTTP LENTSIKVGP
1210 1220 1230 1240 1250
ARKGSYKAKM ARRSKRSRGK DGQESRKRSS LFRKITKQAS LLHTSRSLSS
1260 1270 1280 1290 1300
LNRSLSSGES GPGSPTHSHS LSPRSPTQGY RVTPDAVHSV GGNSSQSSSP
1310 1320 1330 1340 1350
SSSVPSSPAG SGHTRPSSLH GLAPKLQRQY RSPRRKSAGS IPLSPLAHTP
1360 1370 1380 1390 1400
SPPPPTASPQ RSPSPLSGHV AQAFPTKLHL SPPLGRQLSR PKSAEPPRSP
1410 1420 1430 1440 1450
LLKRVQSAEK LAAALAASEK KLATSRKHSL DLPHSELKKE LPPREVSPLE
1460 1470 1480 1490 1500
VVGARSVLSG KGALPGKGVL QPAPSRALGT LRQDRAERRE SLQKQEAIRE
1510 1520 1530 1540 1550
VDSSEDDTEE GPENSQGAQE LSLAPHPEVS QSVAPKGAGE SGEEDPFPSR
1560 1570 1580 1590 1600
DPRSLGPMVP SLLTGITLGP PRMESPSGPH RRLGSPQAIE EAASSSSAGP
1610 1620 1630 1640 1650
NLGQSGATDP IPPEGCWKAQ HLHTQALTAL SPSTSGLTPT SSCSPPSSTS
1660 1670 1680 1690 1700
GKLSMWSWKS LIEGPDRASP SRKATMAGGL ANLQDLENTT PAQPKNLSPR
1710 1720 1730 1740 1750
EQGKTQPPSA PRLAHPSYED PSQGWLWESE CAQAVKEDPA LSITQVPDAS
1760 1770 1780 1790
GDRRQDVPCR GCPLTQKSEP SLRRGQEPGG HQKHRDLALV PDELLKQT
Length:1,798
Mass (Da):196,436
Last modified:March 29, 2005 - v2
Checksum:iDF5C92078A3451AF
GO
Isoform 2Curated (identifier: Q6P0Q8-2) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:1,608
Mass (Da):176,132
Checksum:iE8E7D89D72A99168
GO

Sequence cautioni

The sequence AAH15816.2 differs from that shown. Reason: Frameshift at positions 1114 and 1387. Curated
The sequence AAH15816.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB40778.1 differs from that shown. Reason: Frameshift at position 1688. Curated
The sequence CAH73245.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI16563.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI21706.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1225 – 12251Missing in AAH65499. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691L → F.1 Publication
Corresponds to variant rs55914403 [ dbSNP | Ensembl ].
VAR_040771
Natural varianti275 – 2751K → E in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_040772
Natural varianti388 – 3881D → E.2 Publications
Corresponds to variant rs11211247 [ dbSNP | Ensembl ].
VAR_040773
Natural varianti655 – 6551G → A in a breast mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_040774
Natural varianti659 – 6591I → M.4 Publications
Corresponds to variant rs1707336 [ dbSNP | Ensembl ].
VAR_040775
Natural varianti991 – 9911R → L.1 Publication
Corresponds to variant rs56114653 [ dbSNP | Ensembl ].
VAR_040776
Natural varianti1197 – 11971K → R.1 Publication
Corresponds to variant rs1052607 [ dbSNP | Ensembl ].
VAR_040777
Natural varianti1221 – 12211D → E.1 Publication
Corresponds to variant rs56060730 [ dbSNP | Ensembl ].
VAR_040778
Natural varianti1246 – 12461R → L.1 Publication
Corresponds to variant rs56309943 [ dbSNP | Ensembl ].
VAR_040779
Natural varianti1304 – 13041V → M.1 Publication
Corresponds to variant rs33931638 [ dbSNP | Ensembl ].
VAR_040780
Natural varianti1463 – 14631A → T.1 Publication
Corresponds to variant rs3737738 [ dbSNP | Ensembl ].
VAR_040781
Natural varianti1468 – 14681G → A.1 Publication
Corresponds to variant rs3737737 [ dbSNP | Ensembl ].
VAR_040782
Natural varianti1551 – 15511D → G.3 Publications
Corresponds to variant rs1052610 [ dbSNP | Ensembl ].
VAR_040783
Natural varianti1608 – 16081T → I.
Corresponds to variant rs35474583 [ dbSNP | Ensembl ].
VAR_051645
Natural varianti1673 – 16731K → R.1 Publication
Corresponds to variant rs34070850 [ dbSNP | Ensembl ].
VAR_040784
Natural varianti1703 – 17031G → E.1 Publication
VAR_040785

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei327 – 39670Missing in isoform 2. 1 PublicationVSP_051698Add
BLAST
Alternative sequencei1091 – 111323Missing in isoform 2. 1 PublicationVSP_051699Add
BLAST
Alternative sequencei1290 – 138697Missing in isoform 2. 1 PublicationVSP_051700Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41326.1. [Q6P0Q8-1]
RefSeqiNP_055927.2. NM_015112.2. [Q6P0Q8-1]
XP_005270711.1. XM_005270654.1.
UniGeneiHs.319481.

Genome annotation databases

EnsembliENST00000361297; ENSP00000354671; ENSG00000086015. [Q6P0Q8-1]
GeneIDi23139.
KEGGihsa:23139.
UCSCiuc001cov.3. human. [Q6P0Q8-1]

Polymorphism databases

DMDMi62287152.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS41326.1. [Q6P0Q8-1 ]
RefSeqi NP_055927.2. NM_015112.2. [Q6P0Q8-1 ]
XP_005270711.1. XM_005270654.1.
UniGenei Hs.319481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KQF NMR - A 1099-1193 [» ]
2KYL NMR - A 1099-1193 [» ]
ProteinModelPortali Q6P0Q8.
SMRi Q6P0Q8. Positions 325-425, 506-849, 1099-1193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116756. 17 interactions.
IntActi Q6P0Q8. 18 interactions.
MINTi MINT-1892333.
STRINGi 9606.ENSP00000354671.

Chemistry

ChEMBLi CHEMBL3038500.

PTM databases

PhosphoSitei Q6P0Q8.

Polymorphism databases

DMDMi 62287152.

Proteomic databases

MaxQBi Q6P0Q8.
PaxDbi Q6P0Q8.
PRIDEi Q6P0Q8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361297 ; ENSP00000354671 ; ENSG00000086015 . [Q6P0Q8-1 ]
GeneIDi 23139.
KEGGi hsa:23139.
UCSCi uc001cov.3. human. [Q6P0Q8-1 ]

Organism-specific databases

CTDi 23139.
GeneCardsi GC01P046252.
H-InvDB HIX0000540.
HGNCi HGNC:19035. MAST2.
HPAi HPA039722.
HPA040155.
MIMi 612257. gene.
neXtProti NX_Q6P0Q8.
PharmGKBi PA134954073.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063286.
HOVERGENi HBG052414.
InParanoidi Q6P0Q8.
KOi K08789.
OMAi DMPRFAI.
OrthoDBi EOG7PK8ZC.
PhylomeDBi Q6P0Q8.
TreeFami TF313149.

Enzyme and pathway databases

SignaLinki Q6P0Q8.

Miscellaneous databases

ChiTaRSi MAST2. human.
GeneWikii MAST2.
GenomeRNAii 23139.
NextBioi 44410.
PROi Q6P0Q8.
SOURCEi Search...

Gene expression databases

Bgeei Q6P0Q8.
CleanExi HS_MAST2.
ExpressionAtlasi Q6P0Q8. baseline and differential.
Genevestigatori Q6P0Q8.

Family and domain databases

Gene3Di 1.20.1480.20. 1 hit.
2.30.42.10. 1 hit.
InterProi IPR000961. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24356:SF136. PTHR24356:SF136. 1 hit.
Pfami PF08926. DUF1908. 1 hit.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF140482. SSF140482. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: BrainImported.
  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: LymphImported and PlacentaImported.
  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: BrainImported.
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. 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.
    , 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.

Entry informationi

Entry nameiMAST2_HUMAN
AccessioniPrimary (citable) accession number: Q6P0Q8
Secondary accession number(s): O94899
, Q5VT07, Q5VT08, Q7LGC4, Q8NDG1, Q96B94, Q9BYE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: November 26, 2014
This is version 113 of the entry and version 2 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 1
    Human chromosome 1: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3