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Q96Q15

- SMG1_HUMAN

UniProt

Q96Q15 - SMG1_HUMAN

Protein

Serine/threonine-protein kinase SMG1

Gene

SMG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (08 Feb 2011)
      Previous versions | rss
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    Functioni

    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. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 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.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Manganese.1 Publication

    Enzyme regulationi

    Inhibited by caffeine, LY294002 and wortmannin.3 Publications

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: UniProtKB
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. gene expression Source: Reactome
    3. mRNA export from nucleus Source: UniProtKB
    4. mRNA metabolic process Source: Reactome
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    6. peptidyl-serine phosphorylation Source: UniProtKB
    7. phosphatidylinositol phosphorylation Source: UniProtKB
    8. protein autophosphorylation Source: UniProtKB
    9. response to stress Source: UniProtKB
    10. RNA metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, Nonsense-mediated mRNA decay

    Keywords - Ligandi

    ATP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase SMG1 (EC:2.7.11.1)
    Short name:
    SMG-1
    Short name:
    hSMG-1
    Alternative name(s):
    61E3.4
    Lambda/iota protein kinase C-interacting protein
    Short name:
    Lambda-interacting protein
    Gene namesi
    Name:SMG1
    Synonyms:ATX, KIAA0421, LIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:30045. SMG1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2335 – 23351D → A: Loss of function. 3 Publications

    Organism-specific databases

    PharmGKBiPA164725852.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 36613661Serine/threonine-protein kinase SMG1PRO_0000229791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei173 – 1731N6-acetyllysine1 Publication
    Modified residuei3550 – 35501Phosphothreonine1 Publication
    Modified residuei3556 – 35561Phosphoserine1 Publication
    Modified residuei3570 – 35701Phosphoserine1 Publication
    Modified residuei3573 – 35731Phosphothreonine1 Publication

    Post-translational modificationi

    Autophosphorylated.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96Q15.
    PaxDbiQ96Q15.
    PRIDEiQ96Q15.

    PTM databases

    PhosphoSiteiQ96Q15.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest level in heart and skeletal muscle. Expressed in placenta, brain, lung and spleen, but not in liver.2 Publications

    Gene expression databases

    ArrayExpressiQ96Q15.
    BgeeiQ96Q15.
    GenevestigatoriQ96Q15.

    Organism-specific databases

    HPAiHPA006870.

    Interactioni

    Subunit structurei

    Component of the SMG1C complex composed of SMG1, SMG8 and SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large conformational change in the SMG1 C-terminal head domain containing the catalytic domain. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with PRKCI. Interacts with TELO2 and TTI1. Interacts with RUVBL1 and RUVBL2. Interacts with UPF2.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PABPC1P119402EBI-1049832,EBI-81531
    UPF2Q9HAU57EBI-1049832,EBI-372073

    Protein-protein interaction databases

    BioGridi116687. 28 interactions.
    IntActiQ96Q15. 30 interactions.
    MINTiMINT-1513197.
    STRINGi9606.ENSP00000402515.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96Q15.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1131 – 1866736FATPROSITE-ProRule annotationAdd
    BLAST
    Repeati1817 – 185236HEATAdd
    BLAST
    Domaini2150 – 2478329PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST
    Domaini3629 – 366133FATCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 19771977Interaction with SMG8 and SMG9Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5032.
    HOGENOMiHOG000168703.
    HOVERGENiHBG093965.
    InParanoidiQ96Q15.
    KOiK08873.
    OrthoDBiEOG7RV9F7.
    PhylomeDBiQ96Q15.
    TreeFamiTF352560.

    Family and domain databases

    Gene3Di1.10.1070.11. 2 hits.
    InterProiIPR016024. ARM-type_fold.
    IPR003152. FATC.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR014009. PIK_FAT.
    [Graphical view]
    PfamiPF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    [Graphical view]
    SMARTiSM00146. PI3Kc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 5 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEiPS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96Q15-1) [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

    MSRRAPGSRL SSGGGGGGTK YPRSWNDWQP RTDSASADPD NLKYSSSRDR     50
    GGSSSYGLQP SNSAVVSRQR HDDTRVHADI QNDEKGGYSV NGGSGENTYG 100
    RKSLGQELRV NNVTSPEFTS VQHGSRALAT KDMRKSQERS MSYSDESRLS 150
    NLLRRITRED DRDRRLATVK QLKEFIQQPE NKLVLVKQLD NILAAVHDVL 200
    NESSKLLQEL RQEGACCLGL LCASLSYEAE KIFKWIFSKF SSSAKDEVKL 250
    LYLCATYKAL ETVGEKKAFS SVMQLVMTSL QSILENVDTP ELLCKCVKCI 300
    LLVARCYPHI FSTNFRDTVD ILVGWHIDHT QKPSLTQQVS GWLQSLEPFW 350
    VADLAFSTTL LGQFLEDMEA YAEDLSHVAS GESVDEDVPP PSVSLPKLAA 400
    LLRVFSTVVR SIGERFSPIR GPPITEAYVT DVLYRVMRCV TAANQVFFSE 450
    AVLTAANECV GVLLGSLDPS MTIHCDMVIT YGLDQLENCQ TCGTDYIISV 500
    LNLLTLIVEQ INTKLPSSFV EKLFIPSSKL LFLRYHKEKE VVAVAHAVYQ 550
    AVLSLKNIPV LETAYKLILG EMTCALNNLL HSLQLPEACS EIKHEAFKNH 600
    VFNVDNAKFV VIFDLSALTT IGNAKNSLIG MWALSPTVFA LLSKNLMIVH 650
    SDLAVHFPAI QYAVLYTLYS HCTRHDHFIS SSLSSSSPSL FDGAVISTVT 700
    TATKKHFSII LNLLGILLKK DNLNQDTRKL LMTWALEAAV LMKKSETYAP 750
    LFSLPSFHKF CKGLLANTLV EDVNICLQAC SSLHALSSSL PDDLLQRCVD 800
    VCRVQLVHSG TRIRQAFGKL LKSIPLDVVL SNNNHTEIQE ISLALRSHMS 850
    KAPSNTFHPQ DFSDVISFIL YGNSHRTGKD NWLERLFYSC QRLDKRDQST 900
    IPRNLLKTDA VLWQWAIWEA AQFTVLSKLR TPLGRAQDTF QTIEGIIRSL 950
    AAHTLNPDQD VSQWTTADND EGHGNNQLRL VLLLQYLENL EKLMYNAYEG 1000
    CANALTSPPK VIRTFFYTNR QTCQDWLTRI RLSIMRVGLL AGQPAVTVRH 1050
    GFDLLTEMKT TSLSQGNELE VTIMMVVEAL CELHCPEAIQ GIAVWSSSIV 1100
    GKNLLWINSV AQQAEGRFEK ASVEYQEHLC AMTGVDCCIS SFDKSVLTLA 1150
    NAGRNSASPK HSLNGESRKT VLSKPTDSSP EVINYLGNKA CECYISIADW 1200
    AAVQEWQNAI HDLKKSTSST SLNLKADFNY IKSLSSFESG KFVECTEQLE 1250
    LLPGENINLL AGGSKEKIDM KKLLPNMLSP DPRELQKSIE VQLLRSSVCL 1300
    ATALNPIEQD QKWQSITENV VKYLKQTSRI AIGPLRLSTL TVSQSLPVLS 1350
    TLQLYCSSAL ENTVSNRLST EDCLIPLFSE ALRSCKQHDV RPWMQALRYT 1400
    MYQNQLLEKI KEQTVPIRSH LMELGLTAAK FARKRGNVSL ATRLLAQCSE 1450
    VQLGKTTTAQ DLVQHFKKLS TQGQVDEKWG PELDIEKTKL LYTAGQSTHA 1500
    MEMLSSCAIS FCKSVKAEYA VAKSILTLAK WIQAEWKEIS GQLKQVYRAQ 1550
    HQQNFTGLST LSKNILTLIE LPSVNTMEEE YPRIESESTV HIGVGEPDFI 1600
    LGQLYHLSSV QAPEVAKSWA ALASWAYRWG RKVVDNASQG EGVRLLPREK 1650
    SEVQNLLPDT ITEEEKERIY GILGQAVCRP AGIQDEDITL QITESEDNEE 1700
    DDMVDVIWRQ LISSCPWLSE LDESATEGVI KVWRKVVDRI FSLYKLSCSA 1750
    YFTFLKLNAG QIPLDEDDPR LHLSHRVEQS TDDMIVMATL RLLRLLVKHA 1800
    GELRQYLEHG LETTPTAPWR GIIPQLFSRL NHPEVYVRQS ICNLLCRVAQ 1850
    DSPHLILYPA IVGTISLSSE SQASGNKFST AIPTLLGNIQ GEELLVSECE 1900
    GGSPPASQDS NKDEPKSGLN EDQAMMQDCY SKIVDKLSSA NPTMVLQVQM 1950
    LVAELRRVTV LWDELWLGVL LQQHMYVLRR IQQLEDEVKR VQNNNTLRKE 2000
    EKIAIMREKH TALMKPIVFA LEHVRSITAA PAETPHEKWF QDNYGDAIEN 2050
    ALEKLKTPLN PAKPGSSWIP FKEIMLSLQQ RAQKRASYIL RLEEISPWLA 2100
    AMTNTEIALP GEVSARDTVT IHSVGGTITI LPTKTKPKKL LFLGSDGKSY 2150
    PYLFKGLEDL HLDERIMQFL SIVNTMFATI NRQETPRFHA RHYSVTPLGT 2200
    RSGLIQWVDG ATPLFGLYKR WQQREAALQA QKAQDSYQTP QNPGIVPRPS 2250
    ELYYSKIGPA LKTVGLSLDV SRRDWPLHVM KAVLEELMEA TPPNLLAKEL 2300
    WSSCTTPDEW WRVTQSYARS TAVMSMVGYI IGLGDRHLDN VLIDMTTGEV 2350
    VHIDYNVCFE KGKSLRVPEK VPFRMTQNIE TALGVTGVEG VFRLSCEQVL 2400
    HIMRRGRETL LTLLEAFVYD PLVDWTAGGE AGFAGAVYGG GGQQAESKQS 2450
    KREMEREITR SLFSSRVAEI KVNWFKNRDE MLVVLPKLDG SLDEYLSLQE 2500
    QLTDVEKLQG KLLEEIEFLE GAEGVDHPSH TLQHRYSEHT QLQTQQRAVQ 2550
    EAIQVKLNEF EQWITHYQAA FNNLEATQLA SLLQEISTQM DLGPPSYVPA 2600
    TAFLQNAGQA HLISQCEQLE GEVGALLQQR RSVLRGCLEQ LHHYATVALQ 2650
    YPKAIFQKHR IEQWKTWMEE LICNTTVERC QELYRKYEMQ YAPQPPPTVC 2700
    QFITATEMTL QRYAADINSR LIRQVERLKQ EAVTVPVCED QLKEIERCIK 2750
    VFLHENGEEG SLSLASVIIS ALCTLTRRNL MMEGAASSAG EQLVDLTSRD 2800
    GAWFLEELCS MSGNVTCLVQ LLKQCHLVPQ DLDIPNPMEA SETVHLANGV 2850
    YTSLQELNSN FRQIIFPEAL RCLMKGEYTL ESMLHELDGL IEQTTDGVPL 2900
    QTLVESLQAY LRNAAMGLEE ETHAHYIDVA RLLHAQYGEL IQPRNGSVDE 2950
    TPKMSAGQML LVAFDGMFAQ VETAFSLLVE KLNKMEIPIA WRKIDIIREA 3000
    RSTQVNFFDD DNHRQVLEEI FFLKRLQTIK EFFRLCGTFS KTLSGSSSLE 3050
    DQNTVNGPVQ IVNVKTLFRN SCFSEDQMAK PIKAFTADFV RQLLIGLPNQ 3100
    ALGLTLCSFI SALGVDIIAQ VEAKDFGAES KVSVDDLCKK AVEHNIQIGK 3150
    FSQLVMNRAT VLASSYDTAW KKHDLVRRLE TSISSCKTSL QRVQLHIAMF 3200
    QWQHEDLLIN RPQAMSVTPP PRSAILTSMK KKLHTLSQIE TSIATVQEKL 3250
    AALESSIEQR LKWAGGANPA LAPVLQDFEA TIAERRNLVL KESQRASQVT 3300
    FLCSNIIHFE SLRTRTAEAL NLDAALFELI KRCQQMCSFA SQFNSSVSEL 3350
    ELRLLQRVDT GLEHPIGSSE WLLSAHKQLT QDMSTQRAIQ TEKEQQIETV 3400
    CETIQNLVDN IKTVLTGHNR QLGDVKHLLK AMAKDEEAAL ADGEDVPYEN 3450
    SVRQFLGEYK SWQDNIQTVL FTLVQAMGQV RSQEHVEMLQ EITPTLKELK 3500
    TQSQSIYNNL VSFASPLVTD ATNECSSPTS SATYQPSFAA AVRSNTGQKT 3550
    QPDVMSQNAR KLIQKNLATS ADTPPSTVPG TGKSVACSPK KAVRDPKTGK 3600
    AVQERNSYAV SVWKRVKAKL EGRDVDPNRR MSVAEQVDYV IKEATNLDNL 3650
    AQLYEGWTAW V 3661
    Length:3,661
    Mass (Da):410,501
    Last modified:February 8, 2011 - v3
    Checksum:i216A55F3121F5829
    GO
    Isoform 2 (identifier: Q96Q15-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-140: Missing.

    Show »
    Length:3,521
    Mass (Da):395,382
    Checksum:iC2DDDEEA77C6D976
    GO
    Isoform 3 (identifier: Q96Q15-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-630: Missing.

    Show »
    Length:3,031
    Mass (Da):340,674
    Checksum:i1932F4BF6722348C
    GO
    Isoform 4 (identifier: Q96Q15-4) [UniParc]FASTAAdd to Basket

    Also known as: BLIP

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1269: Missing.

    Show »
    Length:2,392
    Mass (Da):269,425
    Checksum:iD63ECA30F812D7A6
    GO

    Sequence cautioni

    The sequence AAA86535.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141G → GGGGG in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti20 – 201K → N in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti22 – 221P → S in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti40 – 401D → G in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti686 – 6861S → A in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti743 – 7431K → R in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti1193 – 11931C → F in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti2009 – 20091K → R in BAB70696. (PubMed:11544179)Curated
    Sequence conflicti2077 – 20771S → N in AAK58892. (PubMed:9566925)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351A → T.1 Publication
    Corresponds to variant rs12051350 [ dbSNP | Ensembl ].
    VAR_041623
    Natural varianti126 – 1261R → C.1 Publication
    VAR_041624
    Natural varianti144 – 1441S → C.2 Publications
    VAR_041625
    Natural varianti151 – 1511N → Y.1 Publication
    VAR_041626
    Natural varianti160 – 1601D → N.1 Publication
    VAR_041627
    Natural varianti167 – 1671A → V.1 Publication
    VAR_041628
    Natural varianti320 – 3201D → G.1 Publication
    VAR_041629
    Natural varianti465 – 4651G → S.1 Publication
    VAR_041630
    Natural varianti546 – 5461H → R.1 Publication
    VAR_041631
    Natural varianti588 – 5881A → S.1 Publication
    VAR_041632
    Natural varianti612 – 6121I → K.2 Publications
    VAR_041633
    Natural varianti753 – 7531S → C.1 Publication
    VAR_041634
    Natural varianti809 – 8091S → C.1 Publication
    VAR_041635
    Natural varianti812 – 8121R → C.1 Publication
    VAR_041636
    Natural varianti829 – 8291V → I.1 Publication
    VAR_041637
    Natural varianti832 – 8321N → D.1 Publication
    Corresponds to variant rs192246457 [ dbSNP | Ensembl ].
    VAR_041638
    Natural varianti952 – 9521A → G.1 Publication
    VAR_041639
    Natural varianti969 – 9691N → S.1 Publication
    VAR_041640
    Natural varianti1016 – 10161F → L.1 Publication
    VAR_041641
    Natural varianti1029 – 10291R → Q.1 Publication
    VAR_041642
    Natural varianti1072 – 10721T → S.1 Publication
    VAR_041643
    Natural varianti1103 – 11031N → H.1 Publication
    VAR_041644
    Natural varianti1275 – 12751P → R.1 Publication
    VAR_041645
    Natural varianti1292 – 12921Q → P.1 Publication
    VAR_041646
    Natural varianti1332 – 13321I → V.1 Publication
    VAR_041647
    Natural varianti1358 – 13581S → P.1 Publication
    VAR_041648
    Natural varianti1418 – 14181R → T.1 Publication
    Corresponds to variant rs17731779 [ dbSNP | Ensembl ].
    VAR_041649
    Natural varianti2171 – 21711S → C in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
    VAR_041650
    Natural varianti2258 – 22581G → S.1 Publication
    VAR_041651
    Natural varianti2345 – 23451M → K.1 Publication
    VAR_041652
    Natural varianti2730 – 27301Q → E.1 Publication
    VAR_041653
    Natural varianti2889 – 28891G → S.1 Publication
    Corresponds to variant rs35952340 [ dbSNP | Ensembl ].
    VAR_041654
    Natural varianti2899 – 28991P → A.1 Publication
    VAR_041655
    Natural varianti3239 – 32391I → T in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_041656
    Natural varianti3583 – 35831K → Q in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_041657

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 12691269Missing in isoform 4. 1 PublicationVSP_017746Add
    BLAST
    Alternative sequencei1 – 630630Missing in isoform 3. 1 PublicationVSP_017747Add
    BLAST
    Alternative sequencei1 – 140140Missing in isoform 2. 1 PublicationVSP_017748Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF186377 mRNA. Translation: AAK58892.1.
    AB061371 mRNA. Translation: BAB70696.1.
    AY014957 mRNA. Translation: AAK00511.1.
    AF395444 mRNA. Translation: AAM73708.1.
    AC092287 Genomic DNA. No translation available.
    AB007881 mRNA. Translation: BAA24851.2.
    U32581 mRNA. Translation: AAA86535.2. Different initiation.
    CCDSiCCDS45430.1. [Q96Q15-1]
    PIRiJC6084.
    RefSeqiNP_055907.3. NM_015092.4. [Q96Q15-1]
    UniGeneiHs.460179.

    Genome annotation databases

    EnsembliENST00000446231; ENSP00000402515; ENSG00000157106. [Q96Q15-1]
    GeneIDi23049.
    KEGGihsa:23049.
    UCSCiuc002dfm.3. human. [Q96Q15-1]

    Polymorphism databases

    DMDMi322510104.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF186377 mRNA. Translation: AAK58892.1 .
    AB061371 mRNA. Translation: BAB70696.1 .
    AY014957 mRNA. Translation: AAK00511.1 .
    AF395444 mRNA. Translation: AAM73708.1 .
    AC092287 Genomic DNA. No translation available.
    AB007881 mRNA. Translation: BAA24851.2 .
    U32581 mRNA. Translation: AAA86535.2 . Different initiation.
    CCDSi CCDS45430.1. [Q96Q15-1 ]
    PIRi JC6084.
    RefSeqi NP_055907.3. NM_015092.4. [Q96Q15-1 ]
    UniGenei Hs.460179.

    3D structure databases

    ProteinModelPortali Q96Q15.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116687. 28 interactions.
    IntActi Q96Q15. 30 interactions.
    MINTi MINT-1513197.
    STRINGi 9606.ENSP00000402515.

    Chemistry

    ChEMBLi CHEMBL1795195.

    PTM databases

    PhosphoSitei Q96Q15.

    Polymorphism databases

    DMDMi 322510104.

    Proteomic databases

    MaxQBi Q96Q15.
    PaxDbi Q96Q15.
    PRIDEi Q96Q15.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000446231 ; ENSP00000402515 ; ENSG00000157106 . [Q96Q15-1 ]
    GeneIDi 23049.
    KEGGi hsa:23049.
    UCSCi uc002dfm.3. human. [Q96Q15-1 ]

    Organism-specific databases

    CTDi 23049.
    GeneCardsi GC16M018816.
    H-InvDB HIX0012849.
    HIX0038625.
    HIX0202313.
    HGNCi HGNC:30045. SMG1.
    HPAi HPA006870.
    MIMi 607032. gene.
    neXtProti NX_Q96Q15.
    PharmGKBi PA164725852.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5032.
    HOGENOMi HOG000168703.
    HOVERGENi HBG093965.
    InParanoidi Q96Q15.
    KOi K08873.
    OrthoDBi EOG7RV9F7.
    PhylomeDBi Q96Q15.
    TreeFami TF352560.

    Enzyme and pathway databases

    Reactomei REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    ChiTaRSi SMG1. human.
    GeneWikii SMG1_(gene).
    GenomeRNAii 23049.
    NextBioi 44092.
    PROi Q96Q15.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96Q15.
    Bgeei Q96Q15.
    Genevestigatori Q96Q15.

    Family and domain databases

    Gene3Di 1.10.1070.11. 2 hits.
    InterProi IPR016024. ARM-type_fold.
    IPR003152. FATC.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR014009. PIK_FAT.
    [Graphical view ]
    Pfami PF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    [Graphical view ]
    SMARTi SM00146. PI3Kc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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-2335.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, PHOSPHORYLATION OF RENT1, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF ASP-2335.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION OF TP53, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF ASP-2335, VARIANTS CYS-144 AND LYS-612.
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1674-3661.
      Tissue: Brain.
    7. "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] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    8. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2878-3661, TISSUE SPECIFICITY, INTERACTION WITH PRKCI.
    9. "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] [Europe PMC] [Abstract]
      Cited for: DUPLICATION.
    10. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMG5.
    11. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RENT1; UPF2; EST1A AND UPF3B.
    12. "Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay."
      Kashima I., Yamashita A., Izumi N., Kataoka N., Morishita R., Hoshino S., Ohno M., Dreyfuss G., Ohno S.
      Genes Dev. 20:355-367(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UPF2, IDENTIFICATION IN THE SURF COMPLEX.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550 AND SER-3556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, IDENTIFICATION IN THE SMG1C COMPLEX.
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly."
      Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N.
      J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TELO2 AND TTI1.
    21. "A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability."
      Hurov K.E., Cotta-Ramusino C., Elledge S.J.
      Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTI1.
    22. "AAA+ proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in nonsense-mediated mRNA decay."
      Izumi N., Yamashita A., Iwamatsu A., Kurata R., Nakamura H., Saari B., Hirano H., Anderson P., Ohno S.
      Sci. Signal. 3:RA27-RA27(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RUVBL1 AND RUVBL2.
    23. "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 THR-3573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The nonsense-mediated mRNA decay SMG-1 kinase is regulated by large-scale conformational changes controlled by SMG-8."
      Arias-Palomo E., Yamashita A., Fernandez I.S., Nunez-Ramirez R., Bamba Y., Izumi N., Ohno S., Llorca O.
      Genes Dev. 25:153-164(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMG8 AND SMG9, ELECTRON MICROSCOPY OF THE SMG1C COMPLEX.
    26. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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] THR-35; CYS-126; CYS-144; TYR-151; ASN-160; VAL-167; GLY-320; SER-465; ARG-546; SER-588; LYS-612; CYS-753; CYS-809; CYS-812; ILE-829; ASP-832; GLY-952; SER-969; LEU-1016; GLN-1029; SER-1072; HIS-1103; ARG-1275; PRO-1292; VAL-1332; PRO-1358; THR-1418; CYS-2171; SER-2258; LYS-2345; GLU-2730; SER-2889; ALA-2899; THR-3239 AND GLN-3583.

    Entry informationi

    Entry nameiSMG1_HUMAN
    AccessioniPrimary (citable) accession number: Q96Q15
    Secondary accession number(s): O43305
    , Q13284, Q8NFX2, Q96QV0, Q96RW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 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

    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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3