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Reviewed, UniProtKB/Swiss-Prot Q96Q15 (SMG1_HUMAN)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase SMG1
      Short name=SMG-1
      Short name=hSMG-1
    EC=2.7.11.1
Alternative name(s):
    Lambda/iota protein kinase C-interacting protein
      Short name=Lambda-interacting protein
    61E3.4
Gene names
Name: SMG1
Synonyms: ATX, KIAA0421, LIP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3657 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Acts as part of the SMG1C complex, a mRNA surveillance complex that recognizes and degrades mRNAs containing premature translation termination codons (PTCs). The complex probably acts by associating with ribosomes during tranlation termination on mRNPs. If an exon junction complex (EJC) is located 50-55 or more nucleotides downstream from the termination codon, it phosphorylates UPF1/RENT1, triggering nonsense-mediated decay (NMD). Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate TP53/p53 and is required for optimal TP53/p53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. Ref.2 Ref.3 Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Manganese. Ref.3

Enzyme regulation

Inhibited by caffeine, LY294002 and wortmannin. Ref.2 Ref.3 Ref.4

Subunit structure

Component of a post-splicing multiprotein NMD complex with UPF1/RENT1, UPF2/RENT2, EST1A (SMG5/7a), EST1B/SMG5 and UPF3 (UPF3A or UPF3B). Component of the SMG1C complex, at least composed of SMG1, SMG8 and SMG9. The SMG1C complex is then recruited on premature translation termination codons (PTCs) to form the ribosome:SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9. Interacts with PRKCI. Ref.2 Ref.7 Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasm. Ref.4

Tissue specificity

Widely expressed, with highest level in heart and skeletal muscle. Expressed in placenta, brain, lung and spleen, but not in liver. Ref.4 Ref.7

Post-translational modification

Autophosphorylated Probable. Phosphorylated upon DNA damage, probably by ATM or ATR.

Miscellaneous

This gene is located in a region of chromosome 16 that contains 2 segmental duplications. Other genes that are highly related to this exist, but they probably represent pseudogenes.

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 1 HEAT repeat.

Contains 1 PI3K/PI4K domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96Q15-1)

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: Q96Q15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.
Isoform 3 (identifier: Q96Q15-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-626: Missing.
Isoform 4 (identifier: Q96Q15-4)

Also known as: BLIP;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1265: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 36573657Serine/threonine-protein kinase SMG1
PRO_0000229791

Regions

Domain1127 – 1862736FAT
Repeat1813 – 184836HEAT
Domain2146 – 2474329PI3K/PI4K
Domain3625 – 365733FATC

Amino acid modifications

Modified residue35461Phosphothreonine Ref.11
Modified residue35521Phosphoserine Ref.11
Modified residue35661Phosphoserine Ref.12
Modified residue35721Phosphoserine Ref.12
Modified residue35731Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 12651265Missing in isoform 4.
VSP_017746
Alternative sequence1 – 626626Missing in isoform 3.
VSP_017747
Alternative sequence1 – 136136Missing in isoform 2.
VSP_017748
Natural variant311A → T Ref.15
VAR_041623
Natural variant1221R → C Ref.15
VAR_041624
Natural variant1401S → C Ref.4 Ref.15
VAR_041625
Natural variant1471N → Y Ref.15
VAR_041626
Natural variant1561D → N Ref.15
VAR_041627
Natural variant1631A → V Ref.15
VAR_041628
Natural variant3161D → G Ref.15
VAR_041629
Natural variant4611G → S Ref.15
VAR_041630
Natural variant5421H → R Ref.15
VAR_041631
Natural variant5841A → S Ref.15
VAR_041632
Natural variant6081K → I Ref.4 Ref.15
VAR_041633
Natural variant7491S → C Ref.15
VAR_041634
Natural variant8051S → C Ref.15
VAR_041635
Natural variant8081R → C Ref.15
VAR_041636
Natural variant8251V → I Ref.15
VAR_041637
Natural variant8281N → D Ref.15
VAR_041638
Natural variant9481A → G Ref.15
VAR_041639
Natural variant9651N → S Ref.15
VAR_041640
Natural variant10121F → L Ref.15
VAR_041641
Natural variant10251R → Q Ref.15
VAR_041642
Natural variant10681T → S Ref.15
VAR_041643
Natural variant10991N → H Ref.15
VAR_041644
Natural variant12711P → R Ref.15
VAR_041645
Natural variant12881Q → P Ref.15
VAR_041646
Natural variant13281I → V Ref.15
VAR_041647
Natural variant13541S → P Ref.15
VAR_041648
Natural variant14141R → T Ref.15
VAR_041649
Natural variant21671S → C in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.15
VAR_041650
Natural variant22541G → S Ref.15
VAR_041651
Natural variant23411M → K Ref.15
VAR_041652
Natural variant27261Q → E Ref.15
VAR_041653
Natural variant28851G → S Ref.15
VAR_041654
Natural variant28951P → A Ref.15
VAR_041655
Natural variant32351I → T in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.15
VAR_041656
Natural variant35791K → Q in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.15
VAR_041657

Experimental info

Mutagenesis23311D → A: Loss of function. Ref.2 Ref.3 Ref.4
Sequence conflict6821A → S Ref.3
Sequence conflict6821A → S Ref.4
Sequence conflict7391R → K Ref.3
Sequence conflict7391R → K Ref.4
Sequence conflict11891F → C Ref.3
Sequence conflict11891F → C Ref.4
Sequence conflict20051K → R in BAB70696. Ref.2
Sequence conflict20731S → N in AAK58892. Ref.1

Sequences

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

Last modified April 4, 2006. Version 2.
Checksum: ADBBEA902F6B7DEA

FASTA3,657410,261
        10         20         30         40         50         60 
MSRRAPGSRL SSGGTNYSRS WNDWQPRTDS ASADPGNLKY SSSRDRGGSS SYGLQPSNSA 

        70         80         90        100        110        120 
VVSRQRHDDT RVHADIQNDE KGGYSVNGGS GENTYGRKSL GQELRVNNVT SPEFTSVQHG 

       130        140        150        160        170        180 
SRALATKDMR KSQERSMSYS DESRLSNLLR RITREDDRDR RLATVKQLKE FIQQPENKLV 

       190        200        210        220        230        240 
LVKQLDNILA AVHDVLNESS KLLQELRQEG ACCLGLLCAS LSYEAEKIFK WIFSKFSSSA 

       250        260        270        280        290        300 
KDEVKLLYLC ATYKALETVG EKKAFSSVMQ LVMTSLQSIL ENVDTPELLC KCVKCILLVA 

       310        320        330        340        350        360 
RCYPHIFSTN FRDTVDILVG WHIDHTQKPS LTQQVSGWLQ SLEPFWVADL AFSTTLLGQF 

       370        380        390        400        410        420 
LEDMEAYAED LSHVASGESV DEDVPPPSVS LPKLAALLRV FSTVVRSIGE RFSPIRGPPI 

       430        440        450        460        470        480 
TEAYVTDVLY RVMRCVTAAN QVFFSEAVLT AANECVGVLL GSLDPSMTIH CDMVITYGLD 

       490        500        510        520        530        540 
QLENCQTCGT DYIISVLNLL TLIVEQINTK LPSSFVEKLF IPSSKLLFLR YHKEKEVVAV 

       550        560        570        580        590        600 
AHAVYQAVLS LKNIPVLETA YKLILGEMTC ALNNLLHSLQ LPEACSEIKH EAFKNHVFNV 

       610        620        630        640        650        660 
DNAKFVVKFD LSALTTIGNA KNSLIGMWAL SPTVFALLSK NLMIVHSDLA VHFPAIQYAV 

       670        680        690        700        710        720 
LYTLYSHCTR HDHFISSSLS SASPSLFDGA VISTVTTATK KHFSIILNLL GILLKKDNLN 

       730        740        750        760        770        780 
QDTRKLLMTW ALEAAVLMRK SETYAPLFSL PSFHKFCKGL LANTLVEDVN ICLQACSSLH 

       790        800        810        820        830        840 
ALSSSLPDDL LQRCVDVCRV QLVHSGTRIR QAFGKLLKSI PLDVVLSNNN HTEIQEISLA 

       850        860        870        880        890        900 
LRSHMSKAPS NTFHPQDFSD VISFILYGNS HRTGKDNWLE RLFYSCQRLD KRDQSTIPRN 

       910        920        930        940        950        960 
LLKTDAVLWQ WAIWEAAQFT VLSKLRTPLG RAQDTFQTIE GIIRSLAAHT LNPDQDVSQW 

       970        980        990       1000       1010       1020 
TTADNDEGHG NNQLRLVLLL QYLENLEKLM YNAYEGCANA LTSPPKVIRT FFYTNRQTCQ 

      1030       1040       1050       1060       1070       1080 
DWLTRIRLSI MRVGLLAGQP AVTVRHGFDL LTEMKTTSLS QGNELEVTIM MVVEALCELH 

      1090       1100       1110       1120       1130       1140 
CPEAIQGIAV WSSSIVGKNL LWINSVAQQA EGRFEKASVE YQEHLCAMTG VDCCISSFDK 

      1150       1160       1170       1180       1190       1200 
SVLTLANAGR NSASPKHSLN GESRKTVLSK PTDSSPEVIN YLGNKACEFY ISIADWAAVQ 

      1210       1220       1230       1240       1250       1260 
EWQNAIHDLK KSTSSTSLNL KADFNYIKSL SSFESGKFVE CTEQLELLPG ENINLLAGGS 

      1270       1280       1290       1300       1310       1320 
KEKIDMKKLL PNMLSPDPRE LQKSIEVQLL RSSVCLATAL NPIEQDQKWQ SITENVVKYL 

      1330       1340       1350       1360       1370       1380 
KQTSRIAIGP LRLSTLTVSQ SLPVLSTLQL YCSSALENTV SNRLSTEDCL IPLFSEALRS 

      1390       1400       1410       1420       1430       1440 
CKQHDVRPWM QALRYTMYQN QLLEKIKEQT VPIRSHLMEL GLTAAKFARK RGNVSLATRL 

      1450       1460       1470       1480       1490       1500 
LAQCSEVQLG KTTTAQDLVQ HFKKLSTQGQ VDEKWGPELD IEKTKLLYTA GQSTHAMEML 

      1510       1520       1530       1540       1550       1560 
SSCAISFCKS VKAEYAVAKS ILTLAKWIQA EWKEISGQLK QVYRAQHQQN FTGLSTLSKN 

      1570       1580       1590       1600       1610       1620 
ILTLIELPSV NTMEEEYPRI ESESTVHIGV GEPDFILGQL YHLSSVQAPE VAKSWAALAS 

      1630       1640       1650       1660       1670       1680 
WAYRWGRKVV DNASQGEGVR LLPREKSEVQ NLLPDTITEE EKERIYGILG QAVCRPAGIQ 

      1690       1700       1710       1720       1730       1740 
DEDITLQITE SEDNEEDDMV DVIWRQLISS CPWLSELDES ATEGVIKVWR KVVDRIFSLY 

      1750       1760       1770       1780       1790       1800 
KLSCSAYFTF LKLNAGQIPL DEDDPRLHLS HRVEQSTDDM IVMATLRLLR LLVKHAGELR 

      1810       1820       1830       1840       1850       1860 
QYLEHGLETT PTAPWRGIIP QLFSRLNHPE VYVRQSICNL LCRVAQDSPH LILYPAIVGT 

      1870       1880       1890       1900       1910       1920 
ISLSSESQAS GNKFSTAIPT LLGNIQGEEL LVSECEGGSP PASQDSNKDE PKSGLNEDQA 

      1930       1940       1950       1960       1970       1980 
MMQDCYSKIV DKLSSANPTM VLQVQMLVAE LRRVTVLWDE LWLGVLLQQH MYVLRRIQQL 

      1990       2000       2010       2020       2030       2040 
EDEVKRVQNN NTLRKEEKIA IMREKHTALM KPIVFALEHV RSITAAPAET PHEKWFQDNY 

      2050       2060       2070       2080       2090       2100 
GDAIENALEK LKTPLNPAKP GSSWIPFKEI MLSLQQRAQK RASYILRLEE ISPWLAAMTN 

      2110       2120       2130       2140       2150       2160 
TEIALPGEVS ARDTVTIHSV GGTITILPTK TKPKKLLFLG SDGKSYPYLF KGLEDLHLDE 

      2170       2180       2190       2200       2210       2220 
RIMQFLSIVN TMFATINRQE TPRFHARHYS VTPLGTRSGL IQWVDGATPL FGLYKRWQQR 

      2230       2240       2250       2260       2270       2280 
EAALQAQKAQ DSYQTPQNPG IVPRPSELYY SKIGPALKTV GLSLDVSRRD WPLHVMKAVL 

      2290       2300       2310       2320       2330       2340 
EELMEATPPN LLAKELWSSC TTPDEWWRVT QSYARSTAVM SMVGYIIGLG DRHLDNVLID 

      2350       2360       2370       2380       2390       2400 
MTTGEVVHID YNVCFEKGKS LRVPEKVPFR MTQNIETALG VTGVEGVFRL SCEQVLHIMR 

      2410       2420       2430       2440       2450       2460 
RGRETLLTLL EAFVYDPLVD WTAGGEAGFA GAVYGGGGQQ AESKQSKREM EREITRSLFS 

      2470       2480       2490       2500       2510       2520 
SRVAEIKVNW FKNRDEMLVV LPKLDGSLDE YLSLQEQLTD VEKLQGKLLE EIEFLEGAEG 

      2530       2540       2550       2560       2570       2580 
VDHPSHTLQH RYSEHTQLQT QQRAVQEAIQ VKLNEFEQWI THYQAAFNNL EATQLASLLQ 

      2590       2600       2610       2620       2630       2640 
EISTQMDLGP PSYVPATAFL QNAGQAHLIS QCEQLEGEVG ALLQQRRSVL RGCLEQLHHY 

      2650       2660       2670       2680       2690       2700 
ATVALQYPKA IFQKHRIEQW KTWMEELICN TTVERCQELY RKYEMQYAPQ PPPTVCQFIT 

      2710       2720       2730       2740       2750       2760 
ATEMTLQRYA ADINSRLIRQ VERLKQEAVT VPVCEDQLKE IERCIKVFLH ENGEEGSLSL 

      2770       2780       2790       2800       2810       2820 
ASVIISALCT LTRRNLMMEG AASSAGEQLV DLTSRDGAWF LEELCSMSGN VTCLVQLLKQ 

      2830       2840       2850       2860       2870       2880 
CHLVPQDLDI PNPMEASETV HLANGVYTSL QELNSNFRQI IFPEALRCLM KGEYTLESML 

      2890       2900       2910       2920       2930       2940 
HELDGLIEQT TDGVPLQTLV ESLQAYLRNA AMGLEEETHA HYIDVARLLH AQYGELIQPR 

      2950       2960       2970       2980       2990       3000 
NGSVDETPKM SAGQMLLVAF DGMFAQVETA FSLLVEKLNK MEIPIAWRKI DIIREARSTQ 

      3010       3020       3030       3040       3050       3060 
VNFFDDDNHR QVLEEIFFLK RLQTIKEFFR LCGTFSKTLS GSSSLEDQNT VNGPVQIVNV 

      3070       3080       3090       3100       3110       3120 
KTLFRNSCFS EDQMAKPIKA FTADFVRQLL IGLPNQALGL TLCSFISALG VDIIAQVEAK 

      3130       3140       3150       3160       3170       3180 
DFGAESKVSV DDLCKKAVEH NIQIGKFSQL VMNRATVLAS SYDTAWKKHD LVRRLETSIS 

      3190       3200       3210       3220       3230       3240 
SCKTSLQRVQ LHIAMFQWQH EDLLINRPQA MSVTPPPRSA ILTSMKKKLH TLSQIETSIA 

      3250       3260       3270       3280       3290       3300 
TVQEKLAALE SSIEQRLKWA GGANPALAPV LQDFEATIAE RRNLVLKESQ RASQVTFLCS 

      3310       3320       3330       3340       3350       3360 
NIIHFESLRT RTAEALNLDA ALFELIKRCQ QMCSFASQFN SSVSELELRL LQRVDTGLEH 

      3370       3380       3390       3400       3410       3420 
PIGSSEWLLS AHKQLTQDMS TQRAIQTEKE QQIETVCETI QNLVDNIKTV LTGHNRQLGD 

      3430       3440       3450       3460       3470       3480 
VKHLLKAMAK DEEAALADGE DVPYENSVRQ FLGEYKSWQD NIQTVLFTLV QAMGQVRSQE 

      3490       3500       3510       3520       3530       3540 
HVEMLQEITP TLKELKTQSQ SIYNNLVSFA SPLVTDATNE CSSPTSSATY QPSFAAAVRS 

      3550       3560       3570       3580       3590       3600 
NTGQKTQPDV MSQNARKLIQ KNLATSADTP PSTVPGTGKS VACSPKKAVR DPKTGKAVQE 

      3610       3620       3630       3640       3650 
RNSYAVSVWK RVKAKLEGRD VDPNRRMSVA EQVDYVIKEA TNLDNLAQLY EGWTAWV 

« Hide

Isoform 2.

Checksum: 1AE916BA42B724F6
Show »

FASTA3,521395,453
Isoform 3.

Checksum: 9ABE0AC258F26DB6
Show »

FASTA3,031340,730
Isoform 4 (BLIP).

Checksum: D63ECA30F812D7A6
Show »

FASTA2,392269,425

References

« Hide 'large scale' references
[1]"Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62."
Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.
Mol. Cell. Biol. 18:3069-3080(1998) [PubMed: 9566925] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[2]"Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay."
Yamashita A., Ohnishi T., Kashima I., Taya Y., Ohno S.
Genes Dev. 15:2215-2228(2001) [PubMed: 11544179] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION OF RENT1, ALTERNATIVE SPLICING, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH RENT1; UPF2 AND UPF3, MUTAGENESIS OF ASP-2331.
[3]"Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein."
Denning G., Jamieson L., Maquat L.E., Thompson E.A., Fields A.P.
J. Biol. Chem. 276:22709-22714(2001) [PubMed: 11331269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, PHOSPHORYLATION OF RENT1, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF ASP-2331.
[4]"The mRNA surveillance protein hSMG-1 functions in genotoxic stress response pathways in mammalian cells."
Brumbaugh K.M., Otterness D.M., Geisen C., Oliveira V., Brognard J., Li X., Lejeune F., Tibbetts R.S., Maquat L.E., Abraham R.T.
Mol. Cell 14:585-598(2004) [PubMed: 15175154] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION OF TP53, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF ASP-2331, VARIANTS CYS-140 AND ILE-608.
[5]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed: 9455477] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1670-3657.
Tissue: Brain.
[6]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract]
Cited for: SEQUENCE REVISION.
[7]"Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo."
Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J.
Mol. Cell. Biol. 16:105-114(1996) [PubMed: 8524286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2874-3657, TISSUE SPECIFICITY, INTERACTION WITH PRKCI.
[8]"Divergent origins and concerted expansion of two segmental duplications on chromosome 16."
Eichler E.E., Johnson M.E., Alkan C., Tuzun E., Sahinalp C., Misceo D., Archidiacono N., Rocchi M.
J. Hered. 92:462-468(2001) [PubMed: 11948212] [Abstract]
Cited for: DUPLICATION.
[9]"Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7."
Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A., Hachiya T., Hentze M.W., Anderson P., Ohno S.
Mol. Cell 12:1187-1200(2003) [PubMed: 14636577] [Abstract]
Cited for: INTERACTION WITH SMG5.
[10]"Characterization of human Smg5/7a: a protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1."
Chiu S.-Y., Serin G., Ohara O., Maquat L.E.
RNA 9:77-87(2003) [PubMed: 12554878] [Abstract]
Cited for: INTERACTION WITH RENT1; UPF2; EST1A AND UPF3B.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3546 AND SER-3552, MASS SPECTROMETRY.
[12]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3566 AND SER-3572, MASS SPECTROMETRY.
[13]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay."
Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.
Genes Dev. 23:1091-1105(2009) [PubMed: 19417104] [Abstract]
Cited for: CATALYTIC ACTIVITY, IDENTIFICATION IN THE SMG1C COMPLEX.
[15]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-31; CYS-122; CYS-140; TYR-147; ASN-156; VAL-163; GLY-316; SER-461; ARG-542; SER-584; ILE-608; CYS-749; CYS-805; CYS-808; ILE-825; ASP-828; GLY-948; SER-965; LEU-1012; GLN-1025; SER-1068; HIS-1099; ARG-1271; PRO-1288; VAL-1328; PRO-1354; THR-1414; CYS-2167; SER-2254; LYS-2341; GLU-2726; SER-2885; ALA-2895; THR-3235 AND GLN-3579.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF186377 mRNA. Translation: AAK58892.1.
AB061371 mRNA. Translation: BAB70696.1.
AY014957 mRNA. Translation: AAK00511.1.
AF395444 mRNA. Translation: AAM73708.1.
AB007881 mRNA. Translation: BAA24851.2.
U32581 mRNA. Translation: AAA86535.2. Different initiation.
IPIIPI00183368.
IPI00556369.
IPI00639874.
IPI00640955.
PIRJC6084.
RefSeqNP_055907.3.
UniGeneHs.460179

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ96Q15. 3 interactions.

PTM databases

PhosphoSiteQ96Q15.

Genome annotation databases

EnsemblENSG00000157106. Homo sapiens. [Contig view]
GeneID23049.
KEGGhsa:23049.

Organism-specific databases

GeneCardsGC16M018726.
H-InvDBHIX0012849.
HIX0012887.
HIX0038531.
HIX0038951.
HIX0059633.
HGNCHGNC:30045. SMG1.
HPAHPA006870.
MIM607032. gene.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ96Q15.
HOVERGENQ96Q15.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.

Gene expression databases

ArrayExpressQ96Q15.
BgeeQ96Q15.
GermOnlineENSG00000157106. Homo sapiens.

Family and domain databases

InterProIPR015519. Ataxia_Telang_Mut.
IPR003152. FATC.
IPR000357. HEAT.
IPR000403. PI3/4_kinase_cat.
IPR018936. PI3/4_kinase_CS.
IPR014009. PIK_FAT.
[Graphical view]
Gene3DG3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
PANTHERPTHR11139:SF3. Ataxia_Telang_Mut. 1 hit.
PfamPF02260. FATC. 1 hit.
PF02985. HEAT. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
PROSITEPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50077. HEAT_REPEAT. False negative.
PS00915. PI3_4_KINASE_1. False negative.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio44092.
SOURCESearch...

Entry information

Entry nameSMG1_HUMAN
AccessionPrimary (citable) accession number: Q96Q15
Secondary accession number(s): O43305 expand/collapse secondary AC list , Q13284, Q8NFX2, Q96QV0, Q96RW3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents