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Q96Q15

- SMG1_HUMAN

UniProt

Q96Q15 - SMG1_HUMAN

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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

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 kinase activity Source: UniProtKB
  5. 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 1 Publication. 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.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

BgeeiQ96Q15.
ExpressionAtlasiQ96Q15. baseline and differential.
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. 29 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.
GeneTreeiENSGT00760000119359.
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

        10         20         30         40         50
MSRRAPGSRL SSGGGGGGTK YPRSWNDWQP RTDSASADPD NLKYSSSRDR
60 70 80 90 100
GGSSSYGLQP SNSAVVSRQR HDDTRVHADI QNDEKGGYSV NGGSGENTYG
110 120 130 140 150
RKSLGQELRV NNVTSPEFTS VQHGSRALAT KDMRKSQERS MSYSDESRLS
160 170 180 190 200
NLLRRITRED DRDRRLATVK QLKEFIQQPE NKLVLVKQLD NILAAVHDVL
210 220 230 240 250
NESSKLLQEL RQEGACCLGL LCASLSYEAE KIFKWIFSKF SSSAKDEVKL
260 270 280 290 300
LYLCATYKAL ETVGEKKAFS SVMQLVMTSL QSILENVDTP ELLCKCVKCI
310 320 330 340 350
LLVARCYPHI FSTNFRDTVD ILVGWHIDHT QKPSLTQQVS GWLQSLEPFW
360 370 380 390 400
VADLAFSTTL LGQFLEDMEA YAEDLSHVAS GESVDEDVPP PSVSLPKLAA
410 420 430 440 450
LLRVFSTVVR SIGERFSPIR GPPITEAYVT DVLYRVMRCV TAANQVFFSE
460 470 480 490 500
AVLTAANECV GVLLGSLDPS MTIHCDMVIT YGLDQLENCQ TCGTDYIISV
510 520 530 540 550
LNLLTLIVEQ INTKLPSSFV EKLFIPSSKL LFLRYHKEKE VVAVAHAVYQ
560 570 580 590 600
AVLSLKNIPV LETAYKLILG EMTCALNNLL HSLQLPEACS EIKHEAFKNH
610 620 630 640 650
VFNVDNAKFV VIFDLSALTT IGNAKNSLIG MWALSPTVFA LLSKNLMIVH
660 670 680 690 700
SDLAVHFPAI QYAVLYTLYS HCTRHDHFIS SSLSSSSPSL FDGAVISTVT
710 720 730 740 750
TATKKHFSII LNLLGILLKK DNLNQDTRKL LMTWALEAAV LMKKSETYAP
760 770 780 790 800
LFSLPSFHKF CKGLLANTLV EDVNICLQAC SSLHALSSSL PDDLLQRCVD
810 820 830 840 850
VCRVQLVHSG TRIRQAFGKL LKSIPLDVVL SNNNHTEIQE ISLALRSHMS
860 870 880 890 900
KAPSNTFHPQ DFSDVISFIL YGNSHRTGKD NWLERLFYSC QRLDKRDQST
910 920 930 940 950
IPRNLLKTDA VLWQWAIWEA AQFTVLSKLR TPLGRAQDTF QTIEGIIRSL
960 970 980 990 1000
AAHTLNPDQD VSQWTTADND EGHGNNQLRL VLLLQYLENL EKLMYNAYEG
1010 1020 1030 1040 1050
CANALTSPPK VIRTFFYTNR QTCQDWLTRI RLSIMRVGLL AGQPAVTVRH
1060 1070 1080 1090 1100
GFDLLTEMKT TSLSQGNELE VTIMMVVEAL CELHCPEAIQ GIAVWSSSIV
1110 1120 1130 1140 1150
GKNLLWINSV AQQAEGRFEK ASVEYQEHLC AMTGVDCCIS SFDKSVLTLA
1160 1170 1180 1190 1200
NAGRNSASPK HSLNGESRKT VLSKPTDSSP EVINYLGNKA CECYISIADW
1210 1220 1230 1240 1250
AAVQEWQNAI HDLKKSTSST SLNLKADFNY IKSLSSFESG KFVECTEQLE
1260 1270 1280 1290 1300
LLPGENINLL AGGSKEKIDM KKLLPNMLSP DPRELQKSIE VQLLRSSVCL
1310 1320 1330 1340 1350
ATALNPIEQD QKWQSITENV VKYLKQTSRI AIGPLRLSTL TVSQSLPVLS
1360 1370 1380 1390 1400
TLQLYCSSAL ENTVSNRLST EDCLIPLFSE ALRSCKQHDV RPWMQALRYT
1410 1420 1430 1440 1450
MYQNQLLEKI KEQTVPIRSH LMELGLTAAK FARKRGNVSL ATRLLAQCSE
1460 1470 1480 1490 1500
VQLGKTTTAQ DLVQHFKKLS TQGQVDEKWG PELDIEKTKL LYTAGQSTHA
1510 1520 1530 1540 1550
MEMLSSCAIS FCKSVKAEYA VAKSILTLAK WIQAEWKEIS GQLKQVYRAQ
1560 1570 1580 1590 1600
HQQNFTGLST LSKNILTLIE LPSVNTMEEE YPRIESESTV HIGVGEPDFI
1610 1620 1630 1640 1650
LGQLYHLSSV QAPEVAKSWA ALASWAYRWG RKVVDNASQG EGVRLLPREK
1660 1670 1680 1690 1700
SEVQNLLPDT ITEEEKERIY GILGQAVCRP AGIQDEDITL QITESEDNEE
1710 1720 1730 1740 1750
DDMVDVIWRQ LISSCPWLSE LDESATEGVI KVWRKVVDRI FSLYKLSCSA
1760 1770 1780 1790 1800
YFTFLKLNAG QIPLDEDDPR LHLSHRVEQS TDDMIVMATL RLLRLLVKHA
1810 1820 1830 1840 1850
GELRQYLEHG LETTPTAPWR GIIPQLFSRL NHPEVYVRQS ICNLLCRVAQ
1860 1870 1880 1890 1900
DSPHLILYPA IVGTISLSSE SQASGNKFST AIPTLLGNIQ GEELLVSECE
1910 1920 1930 1940 1950
GGSPPASQDS NKDEPKSGLN EDQAMMQDCY SKIVDKLSSA NPTMVLQVQM
1960 1970 1980 1990 2000
LVAELRRVTV LWDELWLGVL LQQHMYVLRR IQQLEDEVKR VQNNNTLRKE
2010 2020 2030 2040 2050
EKIAIMREKH TALMKPIVFA LEHVRSITAA PAETPHEKWF QDNYGDAIEN
2060 2070 2080 2090 2100
ALEKLKTPLN PAKPGSSWIP FKEIMLSLQQ RAQKRASYIL RLEEISPWLA
2110 2120 2130 2140 2150
AMTNTEIALP GEVSARDTVT IHSVGGTITI LPTKTKPKKL LFLGSDGKSY
2160 2170 2180 2190 2200
PYLFKGLEDL HLDERIMQFL SIVNTMFATI NRQETPRFHA RHYSVTPLGT
2210 2220 2230 2240 2250
RSGLIQWVDG ATPLFGLYKR WQQREAALQA QKAQDSYQTP QNPGIVPRPS
2260 2270 2280 2290 2300
ELYYSKIGPA LKTVGLSLDV SRRDWPLHVM KAVLEELMEA TPPNLLAKEL
2310 2320 2330 2340 2350
WSSCTTPDEW WRVTQSYARS TAVMSMVGYI IGLGDRHLDN VLIDMTTGEV
2360 2370 2380 2390 2400
VHIDYNVCFE KGKSLRVPEK VPFRMTQNIE TALGVTGVEG VFRLSCEQVL
2410 2420 2430 2440 2450
HIMRRGRETL LTLLEAFVYD PLVDWTAGGE AGFAGAVYGG GGQQAESKQS
2460 2470 2480 2490 2500
KREMEREITR SLFSSRVAEI KVNWFKNRDE MLVVLPKLDG SLDEYLSLQE
2510 2520 2530 2540 2550
QLTDVEKLQG KLLEEIEFLE GAEGVDHPSH TLQHRYSEHT QLQTQQRAVQ
2560 2570 2580 2590 2600
EAIQVKLNEF EQWITHYQAA FNNLEATQLA SLLQEISTQM DLGPPSYVPA
2610 2620 2630 2640 2650
TAFLQNAGQA HLISQCEQLE GEVGALLQQR RSVLRGCLEQ LHHYATVALQ
2660 2670 2680 2690 2700
YPKAIFQKHR IEQWKTWMEE LICNTTVERC QELYRKYEMQ YAPQPPPTVC
2710 2720 2730 2740 2750
QFITATEMTL QRYAADINSR LIRQVERLKQ EAVTVPVCED QLKEIERCIK
2760 2770 2780 2790 2800
VFLHENGEEG SLSLASVIIS ALCTLTRRNL MMEGAASSAG EQLVDLTSRD
2810 2820 2830 2840 2850
GAWFLEELCS MSGNVTCLVQ LLKQCHLVPQ DLDIPNPMEA SETVHLANGV
2860 2870 2880 2890 2900
YTSLQELNSN FRQIIFPEAL RCLMKGEYTL ESMLHELDGL IEQTTDGVPL
2910 2920 2930 2940 2950
QTLVESLQAY LRNAAMGLEE ETHAHYIDVA RLLHAQYGEL IQPRNGSVDE
2960 2970 2980 2990 3000
TPKMSAGQML LVAFDGMFAQ VETAFSLLVE KLNKMEIPIA WRKIDIIREA
3010 3020 3030 3040 3050
RSTQVNFFDD DNHRQVLEEI FFLKRLQTIK EFFRLCGTFS KTLSGSSSLE
3060 3070 3080 3090 3100
DQNTVNGPVQ IVNVKTLFRN SCFSEDQMAK PIKAFTADFV RQLLIGLPNQ
3110 3120 3130 3140 3150
ALGLTLCSFI SALGVDIIAQ VEAKDFGAES KVSVDDLCKK AVEHNIQIGK
3160 3170 3180 3190 3200
FSQLVMNRAT VLASSYDTAW KKHDLVRRLE TSISSCKTSL QRVQLHIAMF
3210 3220 3230 3240 3250
QWQHEDLLIN RPQAMSVTPP PRSAILTSMK KKLHTLSQIE TSIATVQEKL
3260 3270 3280 3290 3300
AALESSIEQR LKWAGGANPA LAPVLQDFEA TIAERRNLVL KESQRASQVT
3310 3320 3330 3340 3350
FLCSNIIHFE SLRTRTAEAL NLDAALFELI KRCQQMCSFA SQFNSSVSEL
3360 3370 3380 3390 3400
ELRLLQRVDT GLEHPIGSSE WLLSAHKQLT QDMSTQRAIQ TEKEQQIETV
3410 3420 3430 3440 3450
CETIQNLVDN IKTVLTGHNR QLGDVKHLLK AMAKDEEAAL ADGEDVPYEN
3460 3470 3480 3490 3500
SVRQFLGEYK SWQDNIQTVL FTLVQAMGQV RSQEHVEMLQ EITPTLKELK
3510 3520 3530 3540 3550
TQSQSIYNNL VSFASPLVTD ATNECSSPTS SATYQPSFAA AVRSNTGQKT
3560 3570 3580 3590 3600
QPDVMSQNAR KLIQKNLATS ADTPPSTVPG TGKSVACSPK KAVRDPKTGK
3610 3620 3630 3640 3650
AVQERNSYAV SVWKRVKAKL EGRDVDPNRR MSVAEQVDYV IKEATNLDNL
3660
AQLYEGWTAW V
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. 29 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.
GeneTreei ENSGT00760000119359.
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

Bgeei Q96Q15.
ExpressionAtlasi Q96Q15. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 116 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