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Q96Q15

- SMG1_HUMAN

UniProt

Q96Q15 - SMG1_HUMAN

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Protein

Serine/threonine-protein kinase SMG1

Gene
SMG1, ATX, KIAA0421, LIP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

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 Inferred.3 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1131 – 1866736FATAdd
BLAST
Repeati1817 – 185236HEATAdd
BLAST
Domaini2150 – 2478329PI3K/PI4KAdd
BLAST
Domaini3629 – 366133FATCAdd
BLAST

Region

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

Sequence similaritiesi

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

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.

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. VSP_017746Add
BLAST
Alternative sequencei1 – 630630Missing in isoform 3. VSP_017747Add
BLAST
Alternative sequencei1 – 140140Missing in isoform 2. VSP_017748Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141G → GGGGG in BAB70696. 1 Publication
Sequence conflicti20 – 201K → N in BAB70696. 1 Publication
Sequence conflicti22 – 221P → S in BAB70696. 1 Publication
Sequence conflicti40 – 401D → G in BAB70696. 1 Publication
Sequence conflicti686 – 6861S → A in BAB70696. 1 Publication
Sequence conflicti743 – 7431K → R in BAB70696. 1 Publication
Sequence conflicti1193 – 11931C → F in BAB70696. 1 Publication
Sequence conflicti2009 – 20091K → R in BAB70696. 1 Publication
Sequence conflicti2077 – 20771S → N in AAK58892. 1 Publication

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.
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Publicationsi

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  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: September 3, 2014
This is version 114 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

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