Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92540 (SMG7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein SMG7
Alternative name(s):
EST1-like protein C
SMG-7 homolog
Short name=hSMG-7
Gene names
Name:SMG7
Synonyms:C1orf16, EST1C, KIAA0250
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in nonsense-mediated mRNA decay. Recruits UPF1 to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Ref.7 Ref.17

Subunit structure

Part of a complex that contains SMG5, SMG7, PPP2CA, a short isoform ofUPF3A (isoform UPF3AS but not isoform UPF3AL)and phosphorylated UPF1. Ref.1

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic, and nuclear. Shuttles between nucleus and cytoplasm. Ref.1 Ref.7 Ref.17

Sequence similarities

Contains 2 TPR repeats.

Sequence caution

The sequence BAA13381.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92540-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q92540-2)

The sequence of this isoform differs from the canonical sequence as follows:
     569-614: Missing.
Isoform 4 (identifier: Q92540-4)

The sequence of this isoform differs from the canonical sequence as follows:
     569-614: Missing.
     914-914: E → EDPKSSPLLPPDLLKSLAALEEEEELIFSNPPDLYPALLGPLASLPGRSLF
     1101-1137: SIWSSSMMHP...RGQGTMNPPH → KQQHGVQQLG...PFWKRRKKGK
Isoform 5 (identifier: Q92540-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
     914-914: E → EDPKSSPLLPPDLLKSLAALEEEEELIFSNPPDLYPALLGPLASLPGRSLF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 11371136Protein SMG7
PRO_0000076324

Regions

Repeat152 – 18534TPR 1
Repeat187 – 21933TPR 2
Compositional bias648 – 843196Gln/Pro-rich
Compositional bias922 – 101594Ser-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.11 Ref.15 Ref.16
Modified residue5201Phosphoserine Ref.9
Modified residue7811Phosphoserine Ref.8 Ref.9 Ref.12 Ref.14

Natural variations

Alternative sequence1 – 4242Missing in isoform 5.
VSP_047130
Alternative sequence569 – 61446Missing in isoform 2 and isoform 4.
VSP_016574
Alternative sequence9141E → EDPKSSPLLPPDLLKSLAAL EEEEELIFSNPPDLYPALLG PLASLPGRSLF in isoform 4 and isoform 5.
VSP_016575
Alternative sequence1101 – 113737SIWSS…MNPPH → KQQHGVQQLGPKRQSEEEGS SSICVAHRGPRPLPSCSLPA STFRVKFKAARTCAHQAQKK TRRRPFWKRRKKGK in isoform 4.
VSP_016576
Natural variant6271S → F.
Corresponds to variant rs34221194 [ dbSNP | Ensembl ].
VAR_051363
Natural variant9001V → I. Ref.2 Ref.6
Corresponds to variant rs2298083 [ dbSNP | Ensembl ].
VAR_051364

Experimental info

Mutagenesis661K → E: Abolishes interaction with UPF1; when associated with E-163. Ref.17
Mutagenesis1631R → E: Abolishes interaction with UPF1; when associated with E-66. Ref.17
Sequence conflict1871Q → R in BAG61224. Ref.4
Sequence conflict2821R → E in BAC53621. Ref.1
Isoform 4:
Sequence conflict8541V → I in AAH36381. Ref.5
Sequence conflict8981P → T in AAH36381. Ref.5

Secondary structure

................................................................. 1137
Helix Strand Turn

Details...

Sequences

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

Last modified December 20, 2005. Version 2.
Checksum: E152AFAFEF8F3A42

FASTA1,137127,282
        10         20         30         40         50         60 
MSLQSAQYLR QAEVLKADMT DSKLGPAEVW TSRQALQDLY QKMLVTDLEY ALDKKVEQDL 

        70         80         90        100        110        120 
WNHAFKNQIT TLQGQAKNRA NPNRSEVQAN LSLFLEAASG FYTQLLQELC TVFNVDLPCR 

       130        140        150        160        170        180 
VKSSQLGIIS NKQTHTSAIV KPQSSSCSYI CQHCLVHLGD IARYRNQTSQ AESYYRHAAQ 

       190        200        210        220        230        240 
LVPSNGQPYN QLAILASSKG DHLTTIFYYC RSIAVKFPFP AASTNLQKAL SKALESRDEV 

       250        260        270        280        290        300 
KTKWGVSDFI KAFIKFHGHV YLSKSLEKLS PLREKLEEQF KRLLFQKAFN SQQLVHVTVI 

       310        320        330        340        350        360 
NLFQLHHLRD FSNETEQHTY SQDEQLCWTQ LLALFMSFLG ILCKCPLQNE SQEESYNAYP 

       370        380        390        400        410        420 
LPAVKVSMDW LRLRPRVFQE AVVDERQYIW PWLISLLNSF HPHEEDLSSI SATPLPEEFE 

       430        440        450        460        470        480 
LQGFLALRPS FRNLDFSKGH QGITGDKEGQ QRRIRQQRLI SIGKWIADNQ PRLIQCENEV 

       490        500        510        520        530        540 
GKLLFITEIP ELILEDPSEA KENLILQETS VIESLAADGS PGLKSVLSTS RNLSNNCDTG 

       550        560        570        580        590        600 
EKPVVTFKEN IKTREVNRDQ GRSFPPKEVR RDYSKGITVT KNDGKKDNNK RKTETKKCTL 

       610        620        630        640        650        660 
EKLQETGKQN VAVQVKSQTE LRKTPVSEAR KTPVTQTPTQ ASNSQFIPIH HPGAFPPLPS 

       670        680        690        700        710        720 
RPGFPPPTYV IPPPVAFSMG SGYTFPAGVS VPGTFLQPTA HSPAGNQVQA GKQSHIPYSQ 

       730        740        750        760        770        780 
QRPSGPGPMN QGPQQSQPPS QQPLTSLPAQ PTAQSTSQLQ VQALTQQQQS PTKAVPALGK 

       790        800        810        820        830        840 
SPPHHSGFQQ YQQADASKQL WNPPQVQGPL GKIMPVKQPY YLQTQDPIKL FEPSLQPPVM 

       850        860        870        880        890        900 
QQQPLEKKMK PFPMEPYNHN PSEVKVPEFY WDSSYSMADN RSVMAQQANI DRRGKRSPGV 

       910        920        930        940        950        960 
FRPEQDPVPR MPFEKSLLEK PSELMSHSSS FLSLTGFSLN QERYPNNSMF NEVYGKNLTS 

       970        980        990       1000       1010       1020 
SSKAELSPSM APQETSLYSL FEGTPWSPSL PASSDHSTPA SQSPHSSNPS SLPSSPPTHN 

      1030       1040       1050       1060       1070       1080 
HNSVPFSNFG PIGTPDNRDR RTADRWKTDK PAMGGFGIDY LSATSSSESS WHQASTPSGT 

      1090       1100       1110       1120       1130 
WTGHGPSMED SSAVLMESLK SIWSSSMMHP GPSALEQLLM QQKQKQQRGQ GTMNPPH 

« Hide

Isoform 2 [UniParc].

Checksum: 2E6B7AFB0201D533
Show »

FASTA1,091122,020
Isoform 4 [UniParc].

Checksum: 2087382714FE3D57
Show »

FASTA1,178131,650
Isoform 5 [UniParc].

Checksum: 9F9B61B6384AA0FA
Show »

FASTA1,145127,854

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX CONTAINING SMG5; SMG7; UPF1; PPP2CA AND UPF3.
[2]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-900.
Tissue: Bone marrow.
[3]"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.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), VARIANT ILE-900.
Tissue: Testis.
[7]"SMG7 acts as a molecular link between mRNA surveillance and mRNA decay."
Unterholzner L., Izaurralde E.
Mol. Cell 16:587-596(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH CYTOPLASMIC MRNA DECAY BODIES.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway."
Fukuhara N., Ebert J., Unterholzner L., Lindner D., Izaurralde E., Conti E.
Mol. Cell 17:537-547(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-497, FUNCTION, INTERACTION WITH SMG5 AND PHOSPHORYLATED RENT1, SUBCELLULAR LOCATION, TPR REPEAT, MUTAGENESIS OF LYS-66 AND ARG-163.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB085674 mRNA. Translation: BAC53621.1.
D87437 mRNA. Translation: BAA13381.2. Different initiation.
AK299178 mRNA. Translation: BAG61224.1.
AL449223, AL137800 Genomic DNA. Translation: CAI16627.1.
AL137800, AL449223 Genomic DNA. Translation: CAI19486.1.
BC036381 mRNA. Translation: AAH36381.1.
BC052565 mRNA. Translation: AAH52565.1.
RefSeqNP_001167532.1. NM_001174061.1.
NP_775179.1. NM_173156.2.
NP_963862.1. NM_201568.2.
NP_963863.2. NM_201569.2.
UniGeneHs.591463.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YA0X-ray2.55A/B1-497[»]
ProteinModelPortalQ92540.
SMRQ92540. Positions 1-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115218. 7 interactions.
IntActQ92540. 6 interactions.
MINTMINT-1413681.
STRING9606.ENSP00000340766.

PTM databases

PhosphoSiteQ92540.

Polymorphism databases

DMDM84028262.

Proteomic databases

PaxDbQ92540.
PRIDEQ92540.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347615; ENSP00000340766; ENSG00000116698. [Q92540-1]
ENST00000507469; ENSP00000425133; ENSG00000116698. [Q92540-4]
ENST00000508461; ENSP00000426915; ENSG00000116698. [Q92540-5]
ENST00000515829; ENSP00000421358; ENSG00000116698. [Q92540-2]
GeneID9887.
KEGGhsa:9887.
UCSCuc001gqg.3. human. [Q92540-1]
uc001gqh.3. human. [Q92540-2]

Organism-specific databases

CTD9887.
GeneCardsGC01P183441.
H-InvDBHIX0001408.
HGNCHGNC:16792. SMG7.
HPAHPA029350.
MIM610964. gene.
neXtProtNX_Q92540.
PharmGKBPA25605.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302147.
HOGENOMHOG000049052.
HOVERGENHBG056330.
KOK14409.
OMAQETSLYS.
PhylomeDBQ92540.
TreeFamTF327119.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ92540.
BgeeQ92540.
CleanExHS_SMG7.
GenevestigatorQ92540.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR018834. DNA/RNA-bd_Est1-type.
IPR019458. EST1.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF10374. EST1. 1 hit.
PF10373. EST1_DNA_bind. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMG7. human.
EvolutionaryTraceQ92540.
GeneWikiSMG7.
GenomeRNAi9887.
NextBio37276.
PROQ92540.
SOURCESearch...

Entry information

Entry nameSMG7_HUMAN
AccessionPrimary (citable) accession number: Q92540
Secondary accession number(s): B4DRB2 expand/collapse secondary AC list , E9PCI0, E9PEH2, Q5T1Q0, Q6PIE0, Q7Z7H9, Q8IXC1, Q8IXC2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM