O60307 (MAST3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microtubule-associated serine/threonine-protein kinase 3
EC=2.7.11.1

Gene names

Name:	MAST3
Synonyms:	KIAA0561

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	1309 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Subunit structure	Interacts with PTEN. Ref.3
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.
Caution	It is uncertain whether Met-1, Met-171 or Met-172 is the initiator.
Sequence caution	The sequence AAC62830.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTEN	P60484	3	EBI-311420,EBI-696162

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1309

1309

Microtubule-associated serine/threonine-protein kinase 3

PRO_0000086314

Regions

Domain

367 – 640

274

Protein kinase

Domain

641 – 712

72

AGC-kinase C-terminal

Domain

950 – 1038

89

PDZ

Nucleotide binding

373 – 381

9

ATP By similarity

Compositional bias

104 – 109

6

Poly-Ser

Compositional bias

764 – 767

4

Poly-Ser

Compositional bias

877 – 941

65

Ser-rich

Compositional bias

1080 – 1149

70

Ser-rich

Sites

Active site

490

1

Proton acceptor By similarity

Binding site

396

1

ATP By similarity

Amino acid modifications

Modified residue

146

1

Phosphoserine Ref.5

Modified residue

680

1

Phosphoserine Ref.5

Modified residue

774

1

Phosphoserine Ref.6

Modified residue

782

1

Phosphoserine Ref.6

Modified residue

792

1

Phosphoserine Ref.6

Modified residue

793

1

Phosphoserine Ref.6

Modified residue

1223

1

Phosphoserine Ref.4 Ref.5

Modified residue

1273

1

Phosphoserine By similarity

Natural variations

Natural variant

203

1

R → Q.
Corresponds to variant rs35945810 [ dbSNP | Ensembl ].

VAR_051646

Natural variant

861

1

G → S.
Corresponds to variant rs8108738 [ dbSNP | Ensembl ].

VAR_051647

Natural variant

883

1

G → S. Ref.8

VAR_040786

Secondary structure

1

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.

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.

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.

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.

.

.

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.

.

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1309

Helix Strand Turn

Details...

Helix

185 – 197

13

Turn

201 – 203

3

Helix

209 – 230

22

Helix

236 – 255

20

Helix

259 – 276

18

Beta strand

951 – 954

4

Beta strand

962 – 975

14

Beta strand

977 – 986

10

Helix

991 – 995

5

Beta strand

1002 – 1006

5

Helix

1016 – 1025

10

Beta strand

1028 – 1035

8

Sequences

	Sequence		Length	Mass (Da)
	O60307 [UniParc]. Last modified November 22, 2005. Version 2. Checksum: 87E82F2D032ED122	FASTA	1,309	143,137
	10 20 30 40 50 60 MDESSLLRRR GLQKELSLPR RGRGCRSGNR KSLVVGTPSP TLSRPLSPLS VPTAGSSPLD 70 80 90 100 110 120 SPRNFSAASA LNFPFARRAD GRRWSLASLP SSGYGTNTPS STLSSSSSSR ERLHQLPFQP 130 140 150 160 170 180 TPDELHFLSK HFRSSENVLD EEGGRSPRLR PRSRSLSPGR ATGTFDNEIV MMNHVYRERF 190 200 210 220 230 240 PKATAQMEGR LQEFLTAYAP GARLALADGV LGFIHHQIVE LARDCLAKSG ENLVTSRYFL 250 260 270 280 290 300 EMQEKLERLL QDAHERSDSE EVSFIVQLVR KLLIIISRPA RLLECLEFDP EEFYHLLEAA 310 320 330 340 350 360 EGHAREGQGI KTDLPQYIIG QLGLAKDPLE EMVPLSHLEE EQPPAPESPE SRALVGQSRR 370 380 390 400 410 420 KPCESDFETI KLISNGAYGA VYLVRHRDTR QRFAIKKINK QNLILRNQIQ QVFVERDILT 430 440 450 460 470 480 FAENPFVVSM FCSFETRRHL CMVMEYVEGG DCATLLKNMG PLPVDMARLY FAETVLALEY 490 500 510 520 530 540 LHNYGIVHRD LKPDNLLITS LGHIKLTDFG LSKIGLMSMA TNLYEGHIEK DAREFIDKQV 550 560 570 580 590 600 CGTPEYIAPE VIFRQGYGKP VDWWAMGVVL YEFLVGCVPF FGDTPEELFG QVVSDEIMWP 610 620 630 640 650 660 EGDEALPADA QDLITRLLRQ SPLDRLGTGG THEVKQHPFF LALDWAGLLR HKAEFVPQLE 670 680 690 700 710 720 AEDDTSYFDT RSERYRHLGS EDDETNDEES STEIPQFSSC SHRFSKVYSS SEFLAVQPTP 730 740 750 760 770 780 TFAERSFSED REEGWERSEV DYGRRLSADI RLRSWTSSGS SCQSSSSQPE RGPSPSLLNT 790 800 810 820 830 840 ISLDTMPKFA FSSEDEGVGP GPAGPKRPVF ILGEPDPPPA ATPVMPKPSS LSADTAALSH 850 860 870 880 890 900 ARLRSNSIGA RHSTPRPLDA GRGRRLGGPR DPAPEKSRAS SSGGSGGGSG GRVPKSASVS 910 920 930 940 950 960 ALSLIITADD GSGGPLMSPL SPRSLSSNPS SRDSSPSRDP SPVCGSLRPP IVIHSSGKKY 970 980 990 1000 1010 1020 GFSLRAIRVY MGDSDVYTVH HVVWSVEDGS PAQEAGLRAG DLITHINGES VLGLVHMDVV 1030 1040 1050 1060 1070 1080 ELLLKSGNKI SLRTTALENT SIKVGPARKN VAKGRMARRS KRSRRRETQD RRKSLFKKIS 1090 1100 1110 1120 1130 1140 KQTSVLHTSR SFSSGLHHSL SSSESLPGSP THSLSPSPTT PCRSPAPDVP ADTTASPPSA 1150 1160 1170 1180 1190 1200 SPSSSSPASP AAAGHTRPSS LHGLAAKLGP PRPKTGRRKS TSSIPPSPLA CPPISAPPPR 1210 1220 1230 1240 1250 1260 SPSPLPGHPP APARSPRLRR GQSADKLGTG ERLDGEAGRR TRGPEAELVV MRRLHLSERR 1270 1280 1290 1300 DSFKKQEAVQ EVSFDEPQEE ATGLPTSVPQ IAVEGEEAVP VALGPTGRD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1309. Tissue: Brain.
[3]	"Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases." Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C., Antonarakis S.E., Pulido R. J. Biol. Chem. 280:28936-28943(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTEN.
[4]	"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-1223, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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-146; SER-680 AND SER-1223, MASS SPECTROMETRY.
[6]	"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-774; SER-782; SER-792 AND SER-793, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Solution structure of putative domain of human KIAA0561 protein." RIKEN structural genomics initiative (RSGI) Submitted (MAR-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 181-281.
[8]	"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: VARIANT [LARGE SCALE ANALYSIS] SER-883.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AC005793 Genomic DNA. Translation: AAC62830.1. Different initiation.
AC007192 Genomic DNA. Translation: AAD22670.1.
AC093054 Genomic DNA. No translation available.
AB011133 mRNA. Translation: BAA25487.1.

IPI

IPI00028932.

RefSeq

NP_055831.1. NM_015016.1.

UniGene

Hs.466184.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V9V	NMR	-	A	181-280	[»]
3KHF	X-ray	1.20	A/B	948-1040	[»]

ProteinModelPortal

O60307.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60307. 5 interactions.

STRING

9606.ENSP00000262811.

PTM databases

PhosphoSite

O60307.

Proteomic databases

PaxDb

O60307.

PRIDE

O60307.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262811; ENSP00000262811; ENSG00000099308.

GeneID

23031.

KEGG

hsa:23031.

UCSC

uc002nhz.4. human.

Organism-specific databases

CTD

23031.

GeneCards

GC19P018208.

H-InvDB

HIX0014904.

HGNC

HGNC:19036. MAST3.

HPA

HPA035061.
HPA035062.

MIM

612258. gene.

neXtProt

NX_O60307.

PharmGKB

PA134877725.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000046662.

HOVERGEN

HBG052414.

InParanoid

O60307.

KO

K08789.

OMA

SVHSGAI.

OrthoDB

EOG4SF957.

Enzyme and pathway databases

SignaLink

O60307.

Gene expression databases

Bgee

O60307.

CleanEx

HS_MAST3.

Genevestigator

O60307.

GermOnline

ENSG00000099308. 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

MAST3. human.

EvolutionaryTrace

O60307.

GenomeRNAi

23031.

NextBio

44010.

SOURCE

Search...

Entry information

Entry name

MAST3_HUMAN

Accession

Primary (citable) accession number: O60307
Secondary accession number(s): Q7LDZ8, Q9UPI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	November 22, 2005
Last modified:	May 29, 2013
This is version 113 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.