Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine-protein kinase ATM

Gene

ATM

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by wortmannin.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine-protein kinase ATM (EC:2.7.11.1)
Alternative name(s):
Ataxia telangiectasia mutated homolog
Short name:
A-T mutated homolog
Gene namesi
Name:ATM
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmic vesicle By similarity

  • Note: Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 30573056Serine-protein kinase ATMPRO_0000088842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei367 – 3671PhosphoserineBy similarity
Modified residuei1894 – 18941PhosphoserineBy similarity
Modified residuei1982 – 19821Phosphoserine; by autocatalysisBy similarity
Modified residuei1984 – 19841PhosphoserineBy similarity
Modified residuei2997 – 29971PhosphoserineBy similarity
Modified residuei3017 – 30171N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated by NUAK1/ARK5. Autophosphorylated on Ser-1982 upon DNA damage (By similarity).By similarity
Acetylated by KAT5 upon DNA damage; which is required for autophosphorylation and subsequent activation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ6PQD5.
PRIDEiQ6PQD5.

Interactioni

Subunit structurei

Dimers or tetramers in inactive state. On DNA damage, autophosphorylation dissociates ATM into monomers rendering them catalytically active. Binds DNA ends, p53/TP53, ABL1, BRCA1, NBN/nibrin and TERF1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. DNA damage promotes association with RAD17. Interacts with EEF1E1; the interaction, induced on DNA damage, up-regulates TP53. Interacts with DCLRE1C, MYST1, KAT5, NABP2, ATMIN and CEP164 (By similarity). Interacts with AP2B1 AND AP3B2; the interaction occurs in cytoplasmic vesicles (By similarity). Interacts with DDX1. Interacts with TELO2 AND TTI1. Interacts with BRAT1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019250.

Structurei

3D structure databases

ProteinModelPortaliQ6PQD5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1961 – 2567607FATPROSITE-ProRule annotationAdd
BLAST
Domaini2713 – 3057345PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini3025 – 305733FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1374 – 138310Interaction with ABL1By similarity

Domaini

The FATC domain is required for interaction with KAT5.By similarity

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family. ATM subfamily.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0892. Eukaryota.
ENOG410XNPY. LUCA.
HOGENOMiHOG000204213.
HOVERGENiHBG004304.
InParanoidiQ6PQD5.
KOiK04728.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR015519. ATM/Tel1.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR018278. Ribosomal_S21_CS.
IPR021668. TAN.
[Graphical view]
PANTHERiPTHR11139:SF72. PTHR11139:SF72. 6 hits.
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM01342. TAN. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS01181. RIBOSOMAL_S21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6PQD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLALNDLLI CCRQLEHDRA TERRKAVENF RHLIQDPETV QHLDQHSDSK
60 70 80 90 100
QGKYLNWDAA FRFLQKYIQK ETECLRTAKQ NVSASTQATR QKKMQEISSL
110 120 130 140 150
VKYFIKCANK RAPRLKCQEL LNYIMDTVRD SSNNPIYGAD YSNILLKDIL
160 170 180 190 200
SVRKYWCEIS QQQWRELFLI YFTLYLKPSQ DINRLLVARI IQAVTKGCCS
210 220 230 240 250
QTDGLNSEFL DFFTKAIQNA RQEKSSPGLN HILAAYVIFL KTLAANFRIR
260 270 280 290 300
VCELGDKILP TLLYIWTQHR LNDSLKEVIV ELFQLQVYMH HPKGAKTQEK
310 320 330 340 350
GAYESAKWKS ILYNLYDLLV NEISRIGSRG KYSSGSRNIA VKENLIELMA
360 370 380 390 400
DICHQVFNED TRSLEISQSY TTTQREFSDY NAPCKKRKIE LGWGVIKDHL
410 420 430 440 450
QKSQNDFDVV PWLQIATQLI SKYPASLPNC ELSPLLMILY QLLPQQRRGE
460 470 480 490 500
RTPYVLRCLM EVALCQGKKP NLESSHKSDL LKIWIKIWSI TFRGISSEQI
510 520 530 540 550
QAENFGLLGA IIQGSLVEVD REFWKLFTGS ACKPSCPTVC CLTLALKTCV
560 570 580 590 600
VPETVETGME NICDGNRKFS LKESIMKWLL FCQLEDDFED RIELPPILHS
610 620 630 640 650
NFPHLALEKI LVSLIMKNCK AAMNFFQSVP ECEQHQKDTE EPSLLEVEEL
660 670 680 690 700
FLQTTFDKMD FLTVVQECTI EKHQSSVGFS FHQNLKESLD RYLLGLSEQL
710 720 730 740 750
LNNYLPETSD SETLVRCSSL LVGVLGCYCY VGVIAEEEAY TSELFQKAKS
760 770 780 790 800
LMQCAGESIT LFKSKTNEES RIISLRNMMH LCTNCLYKCA KRSPNKIASG
810 820 830 840 850
FFLRLLTSKL MHDIADVCRS LAFIIKKPFD CREVESMEDD TDKNLMEMND
860 870 880 890 900
QSSMSLFNDN PASSVIDANE SGESQITMGA MNPLAEEHLS KQDLLVLDML
910 920 930 940 950
RFLCMCITIA QSNTMSFRAA DIRRKLLMLI DSDRLDPTKS LHLHMYLVLL
960 970 980 990 1000
KELPGEEYPL PMEDVVELLK PLSSVCSLYR RDQDVCKTIL NHVLHIVPNL
1010 1020 1030 1040 1050
CRENVDAEST RDAQGQFLTV IGAFWHLTKE GKCTFSVRLA LVKCLKTLLE
1060 1070 1080 1090 1100
ADPYSRWAIL NVMEKDFPVN EVFPQFLADN HHQVCMLAAG LINRLFQHMK
1110 1120 1130 1140 1150
QGDSSTIMRA LPLKLQQTAF ENAYLKAQER IRQVKSQGGE NRELLDEICN
1160 1170 1180 1190 1200
RKAVLLTMIA VVLCCSPVCE KQALFALCKS VKENGLEPHL IKKVLEKVSE
1210 1220 1230 1240 1250
TFGYRHLEDF MASHLDYLVL EWLHLQDAEY SLSSFPFILL NYTNIEDFYR
1260 1270 1280 1290 1300
SCYKVLIPHL VMRCHFDEVK SIANQIQGDW KSLLTDCFPK ILVNILPYFA
1310 1320 1330 1340 1350
YEDTGDRGMA QQRETASKVY DMLKDENLLG KQIDQLFINN LPEIVVELLM
1360 1370 1380 1390 1400
TLHEPATSDA SQSTDPCDFS GDLDPRPNPP HFPSHVIKAT FAYISNCHKT
1410 1420 1430 1440 1450
KLKSILEVLS KSPDSYQKIL LAICEQAAET NNVYKKHRIL KIYHLFVSLL
1460 1470 1480 1490 1500
LKDMKSGLGG AWAFVLRDVI YTLIHYINKR PSRFMDVSLR SFSLCCDLLS
1510 1520 1530 1540 1550
RVCHTAVTYS KDALESHLHV IVGTLIPLVD GQMEVQKQVL DLLKYLVIDN
1560 1570 1580 1590 1600
KDNENLYVMI KLLDPFPDNA VFKDLRITQQ EIKYSKGPFS LLEEINHFLS
1610 1620 1630 1640 1650
VSVYDALPLT RLEGLKDLRR QLAQHKDQMM DLMRASQDNP QDGIVVKLVV
1660 1670 1680 1690 1700
SLLQLSKMAV NHTGEREVLE AVGRCLGEVG PIDFSTIAIQ HSKDMPYTKA
1710 1720 1730 1740 1750
LELFEDKEHH WTLMMLTYLN STLVEDCVKV RSAAVTCLKS ILATKTGHGF
1760 1770 1780 1790 1800
WEIFKTTADP MLTYLLPFRT SRKKFLEVPR LNKESPLEGL DDISLWIPQS
1810 1820 1830 1840 1850
ENHDIWIKTL TCALLDSGGI NSEVLQLLKP MCEVKTDFCQ TVLPYLIHDI
1860 1870 1880 1890 1900
LLQDTNESWR SLLSTHIQGF FTNCFRHSSQ TSRSTTPANM DSESEHVFRC
1910 1920 1930 1940 1950
HLDKKSQRTM LAVVDYMRRQ KRSSSGTVFD DAFWLELNYL EVAKVAQSCA
1960 1970 1980 1990 2000
AHFTALLYAE IYADKKNMDD QEKRSPTFEE GSQSTTISSL SEKSKEETGI
2010 2020 2030 2040 2050
SLQDLLLEIY RSIGEPDSLY GCGGGKMLQP LTRLRTYEHE AMWGKALVTY
2060 2070 2080 2090 2100
DLETAISSST RQAGIIQALQ NLGLCHILSV YLKGLDHENK EQCAELQELH
2110 2120 2130 2140 2150
YQVAWRNMQW DSCVSVNKGM EGTSYHESLY NALQSLRDRE FSTFYESLKY
2160 2170 2180 2190 2200
ARVKEVEELC KGSLESVYSL YPTLSRLQAI GELENIGELF SRSVTDRQPS
2210 2220 2230 2240 2250
EVYNKWWKHS QLLKDSDFSF QEPIMALRTV ILEILMEKEM ENSQRECLKD
2260 2270 2280 2290 2300
ILTKHLVELS LLARTFQNTQ LPERAIFQIK QYNSANCGVS EWQLEEAQVF
2310 2320 2330 2340 2350
WAKKEQSLAL SILKQMIKKL DASCTENDPR LKLIHIECLR VCGTWLAETC
2360 2370 2380 2390 2400
LENPAVIMQT YLEKAVELAG NYDGESNDEL RNGKMKAFLS LARFSDTQYQ
2410 2420 2430 2440 2450
RIENYMKSSE FENKQALLKR AKEEVGLLRE HKIQTNRYTI KVQRELELDE
2460 2470 2480 2490 2500
GALRALKKDR KRFLCKAVEN YINCLLSGEG HDMWIFRLCS LWLENSGVSE
2510 2520 2530 2540 2550
VNGMMKRDGM KIPSYKFLPL MYQLAARMGT KMMGGLGFHD VLNSLISRIS
2560 2570 2580 2590 2600
VDHPHHTLFI ILALANANKD EFLTKPEAAR SSRITKNTPK ESSQLDEDRT
2610 2620 2630 2640 2650
EAANKVICTL RNRRRQMVRS VEALCDAYII LANLDATQWR TQRKGIRIPA
2660 2670 2680 2690 2700
DQPITKLKNL EDVVVPTMEI KVDPTGEYGN MVTIQSFKPE FRLAGGLNLP
2710 2720 2730 2740 2750
KIIDCVGSDG KERRQLVKGR DDLRQDAVMQ QVFQMCNTLL QRNTETRKRK
2760 2770 2780 2790 2800
LTICTYKVVP LSQRSGVLEW CTGTVPIGEY LVNNDTGAHK RYRPKDFSPV
2810 2820 2830 2840 2850
QCQKKMMEAQ NKSFEEKYEI FMNICQNFQP VFRYFCMEKF LDPAVWFERR
2860 2870 2880 2890 2900
LAYTQSVATS SIVGYILGLG DRHVQNILIN EQSAELVHID LGVAFEQGKI
2910 2920 2930 2940 2950
LPTPETVPFR LTRDIVDGMG ITGVEGVFRR CCEKTMEVMR NSQETLLTIV
2960 2970 2980 2990 3000
EVLLYDPLFD WTMNPLKALY LQQRPEDESE LHSTPRADDQ ECKRNLSDTD
3010 3020 3030 3040 3050
QSFNKVAERV LMRLQEKLKG VEEGTVLSVG GQVNFLIQQA MDPKNLSKLF

SGWKAWV
Length:3,057
Mass (Da):350,564
Last modified:July 10, 2007 - v2
Checksum:iBE5546AA0BF9E32C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY587061 Genomic DNA. Translation: AAT01608.2.
RefSeqiNP_001116552.1. NM_001123080.1.
UniGeneiSsc.101725.
Ssc.21876.

Genome annotation databases

GeneIDi100101922.
KEGGissc:100101922.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY587061 Genomic DNA. Translation: AAT01608.2.
RefSeqiNP_001116552.1. NM_001123080.1.
UniGeneiSsc.101725.
Ssc.21876.

3D structure databases

ProteinModelPortaliQ6PQD5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019250.

Proteomic databases

PaxDbiQ6PQD5.
PRIDEiQ6PQD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100101922.
KEGGissc:100101922.

Organism-specific databases

CTDi472.

Phylogenomic databases

eggNOGiKOG0892. Eukaryota.
ENOG410XNPY. LUCA.
HOGENOMiHOG000204213.
HOVERGENiHBG004304.
InParanoidiQ6PQD5.
KOiK04728.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR015519. ATM/Tel1.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR018278. Ribosomal_S21_CS.
IPR021668. TAN.
[Graphical view]
PANTHERiPTHR11139:SF72. PTHR11139:SF72. 6 hits.
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM01342. TAN. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS01181. RIBOSOMAL_S21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genomic organization and comparative analysis of the porcine ataxia-telangiectasia mutated (ATM) gene."
    Fritz K.L., Rogatcheva M.B., Counter C.M., Schook L.B., Beever J.E.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiATM_PIG
AccessioniPrimary (citable) accession number: Q6PQD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 10, 2007
Last modified: May 11, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.