Q86US8 (EST1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Telomerase-binding protein EST1A
EC=3.1.-.-

Alternative name(s):
EST1-like protein A
Ever shorter telomeres 1A
Smg-6 homolog
Telomerase subunit EST1A
hSmg5/7a

Gene names

Name:	SMG6
Synonyms:	C17orf31, EST1A, KIAA0732

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5'-(GTGTGG)4GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER). Ref.1 Ref.5 Ref.9 Ref.10 Ref.14 Plays a role in nonsense-mediated mRNA decay. Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA. Ref.1 Ref.5 Ref.9 Ref.10 Ref.14
Cofactor	Manganese. Ref.14
Subunit structure	Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Interacts with TERT, independently of the telomerase RNA. Interacts with PP2A catalytic subunits, SMG1, UPF1, UPF2 and UPF3B. Ref.1 Ref.5 Ref.7 Ref.10 Ref.12
Subcellular location	Nucleus › nucleolus. Chromosome › telomere Probable. Cytoplasm › cytosol. Note: Particularly enriched in the nucleolus. Ref.1 Ref.10
Tissue specificity	Ubiquitous. Ref.1 Ref.5
Domain	The PINc domain confers endonuclease activity and is expected to bind the catalytic metal ion. Ref.9 Ref.10
Sequence similarities	Contains 1 PINc domain.
Sequence caution	The sequence AAH64916.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA34452.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay
Cellular component	Chromosome Cytoplasm Nucleus Telomere
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	DNA-binding Manganese Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gene expression Traceable author statement. Source: Reactome mRNA export from nucleus Traceable author statement PubMed 16488880. Source: HGNC nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype Ref.9Ref.10. Source: UniProtKB regulation of dephosphorylation Traceable author statement PubMed 15721257. Source: HGNC telomere maintenance Inferred from mutant phenotype Ref.5. Source: HGNC
Cellular_component	chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.10. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA telomerase holoenzyme complex Traceable author statement Ref.5. Source: HGNC
Molecular_function	endoribonuclease activity Inferred from direct assay Ref.10. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW telomeric DNA binding Inferred from direct assay Ref.5. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UPF1	Q92900-2	2	EBI-3232100,EBI-373492

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86US8-1)

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: Q86US8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1089: Missing.
     1090-1119: ILEEDRLLSGFVPLLAAPQDPCYVEKTSDK → MRFRLCHQRGCCPHERENTCTCKMIISSLQ

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1419

1419

Telomerase-binding protein EST1A

PRO_0000087069

Regions

Domain

1246 – 1397

152

PINc

Region

114 – 503

390

Interaction with telomeric DNA

Coiled coil

163 – 193

31

Potential

Coiled coil

567 – 625

59

Potential

Coiled coil

1197 – 1239

43

Potential

Sites

Metal binding

1251

1

Manganese; catalytic Probable

Metal binding

1353

1

Manganese; catalytic Probable

Metal binding

1392

1

Manganese; catalytic Probable

Amino acid modifications

Modified residue

479

1

Phosphothreonine Ref.11

Natural variations

Alternative sequence

1 – 1089

1089

Missing in isoform 2.

VSP_010360

Alternative sequence

1090 – 1119

30

ILEED…KTSDK → MRFRLCHQRGCCPHERENTC TCKMIISSLQ in isoform 2.

VSP_010361

Natural variant

291

1

R → P. Ref.2
Corresponds to variant rs1885986 [ dbSNP | Ensembl ].

VAR_018499

Natural variant

294

1

K → Q.
Corresponds to variant rs216195 [ dbSNP | Ensembl ].

VAR_018500

Natural variant

341

1

N → T. Ref.1 Ref.2
Corresponds to variant rs1885987 [ dbSNP | Ensembl ].

VAR_018501

Natural variant

575

1

N → S.
Corresponds to variant rs34047637 [ dbSNP | Ensembl ].

VAR_050978

Natural variant

972

1

A → T.
Corresponds to variant rs903160 [ dbSNP | Ensembl ].

VAR_018502

Natural variant

984

1

R → C.
Corresponds to variant rs35173108 [ dbSNP | Ensembl ].

VAR_050979

Natural variant

1189

1

E → K.
Corresponds to variant rs58801957 [ dbSNP | Ensembl ].

VAR_061648

Natural variant

1233

1

H → R.
Corresponds to variant rs2273980 [ dbSNP | Ensembl ].

VAR_018503

Experimental info

Mutagenesis

1251

1

D → A: Impaired nonsense-mediated RNA decay. Ref.9 Ref.10

Mutagenesis

1251

1

D → N: Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1392. Ref.9 Ref.10

Mutagenesis

1353

1

D → A: Abolishes RNase activity. Ref.10 Ref.14

Mutagenesis

1392

1

D → A: Impaired nonsense-mediated RNA decay; when associated with A-1251. Ref.9 Ref.10

Mutagenesis

1392

1

D → N: Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1251. Ref.9 Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1419

Helix Strand Turn

Details...

Beta strand

1240 – 1250

11

Helix

1252 – 1268

17

Beta strand

1270 – 1276

7

Helix

1277 – 1287

11

Helix

1298 – 1319

22

Beta strand

1325 – 1328

4

Beta strand

1334 – 1336

3

Helix

1352 – 1361

10

Helix

1368 – 1371

4

Beta strand

1381 – 1389

9

Helix

1393 – 1401

9

Helix

1409 – 1416

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 93FC7DDA68BD218C	FASTA	1,419	160,462
	10 20 30 40 50 60 MAEGLERVRI SASELRGILA TLAPQAGSRE NMKELKEARP RKDNRRPDLE IYKPGLSRLR 70 80 90 100 110 120 NKPKIKEPPG SEEFKDEIVN DRDCSAVENG TQPVKDVCKE LNNQEQNGPI DPENNRGQES 130 140 150 160 170 180 FPRTAGQEDR SLKIIKRTKK PDLQIYQPGR RLQTVSKESA SRVEEEEVLN QVEQLRVEED 190 200 210 220 230 240 ECRGNVAKEE VANKPDRAEI EKSPGGGRVG AAKGEKGKRM GKGEGVRETH DDPARGRPGS 250 260 270 280 290 300 AKRYSRSDKR RNRYRTRSTS SAGSNNSAEG AGLTDNGCRR RRQDRTKERP RLKKQVSVSS 310 320 330 340 350 360 TDSLDEDRID EPDGLGPRRS SERKRHLERN WSGRGEGEQK NSAKEYRGTL RVTFDAEAMN 370 380 390 400 410 420 KESPMVRSAR DDMDRGKPDK GLSSGGKGSE KQESKNPKQE LRGRGRGILI LPAHTTLSVN 430 440 450 460 470 480 SAGSPESAPL GPRLLFGSGS KGSRSWGRGG TTRRLWDPNN PDQKPALKTQ TPQLHFLDTD 490 500 510 520 530 540 DEVSPTSWGD SRQAQASYYK FQNSDNPYYY PRTPGPASQY PYTGYNPLQY PVGPTNGVYP 550 560 570 580 590 600 GPYYPGYPTP SGQYVCSPLP TSTMSPEEVE QHMRNLQQQE LHRLLRVADN QELQLSNLLS 610 620 630 640 650 660 RDRISPEGLE KMAQLRAELL QLYERCILLD IEFSDNQNVD QILWKNAFYQ VIEKFRQLVK 670 680 690 700 710 720 DPNVENPEQI RNRLLELLDE GSDFFDSLLQ KLQVTYKFKL EDYMDGLAIR SKPLRKTVKY 730 740 750 760 770 780 ALISAQRCMI CQGDIARYRE QASDTANYGK ARSWYLKAQH IAPKNGRPYN QLALLAVYTR 790 800 810 820 830 840 RKLDAVYYYM RSLAASNPIL TAKESLMSLF EETKRKAEQM EKKQHEEFDL SPDQWRKGKK 850 860 870 880 890 900 STFRHVGDDT TRLEIWIHPS HPRSSQGTES GKDSEQENGL GSLSPSDLNK RFILSFLHAH 910 920 930 940 950 960 GKLFTRIGME TFPAVAEKVL KEFQVLLQHS PSPIGSTRML QLMTINMFAV HNSQLKDCFS 970 980 990 1000 1010 1020 EECRSVIQEQ AAALGLAMFS LLVRRCTCLL KESAKAQLSS PEDQDDQDDI KVSSFVPDLK 1030 1040 1050 1060 1070 1080 ELLPSVKVWS DWMLGYPDTW NPPPTSLDLP SHVAVDVWST LADFCNILTA VNQSEVPLYK 1090 1100 1110 1120 1130 1140 DPDDDLTLLI LEEDRLLSGF VPLLAAPQDP CYVEKTSDKV IAADCKRVTV LKYFLEALCG 1150 1160 1170 1180 1190 1200 QEEPLLAFKG GKYVSVAPVP DTMGKEMGSQ EGTRLEDEEE DVVIEDFEED SEAEGSGGED 1210 1220 1230 1240 1250 1260 DIRELRAKKL ALARKIAEQQ RRQEKIQAVL EDHSQMRQME LEIRPLFLVP DTNGFIDHLA 1270 1280 1290 1300 1310 1320 SLARLLESRK YILVVPLIVI NELDGLAKGQ ETDHRAGGYA RVVQEKARKS IEFLEQRFES 1330 1340 1350 1360 1370 1380 RDSCLRALTS RGNELESIAF RSEDITGQLG NNDDLILSCC LHYCKDKAKD FMPASKEEPI 1390 1400 1410 RLLREVVLLT DDRNLRVKAL TRNVPVRDIP AFLTWAQVG
	Isoform 2 [UniParc]. Checksum: 11E6E60AC32D4F88	FASTA	330	37,465
	10 20 30 40 50 60 MRFRLCHQRG CCPHERENTC TCKMIISSLQ VIAADCKRVT VLKYFLEALC GQEEPLLAFK 70 80 90 100 110 120 GGKYVSVAPV PDTMGKEMGS QEGTRLEDEE EDVVIEDFEE DSEAEGSGGE DDIRELRAKK 130 140 150 160 170 180 LALARKIAEQ QRRQEKIQAV LEDHSQMRQM ELEIRPLFLV PDTNGFIDHL ASLARLLESR 190 200 210 220 230 240 KYILVVPLIV INELDGLAKG QETDHRAGGY ARVVQEKARK SIEFLEQRFE SRDSCLRALT 250 260 270 280 290 300 SRGNELESIA FRSEDITGQL GNNDDLILSC CLHYCKDKAK DFMPASKEEP IRLLREVVLL 310 320 330 TDDRNLRVKA LTRNVPVRDI PAFLTWAQVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human homolog of yeast est1 associates with telomerase and uncaps chromosome ends when overexpressed." Reichenbach P., Hoess M., Azzalin C.M., Nabholz M., Bucher P., Lingner J. Curr. Biol. 13:568-574(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-341, FUNCTION IN TELOMERE REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TELOMERASE RIBONUCLEOPROTEIN COMPLEX. Tissue: Cervix carcinoma.
[2]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-291 AND THR-341. Tissue: Brain.
[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]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[5]	"Functional conservation of the telomerase protein Est1p in humans." Snow B.E., Erdmann N., Cruickshank J., Goldman H., Gill R.M., Robinson M.O., Harrington L. Curr. Biol. 13:698-704(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-1419 (ISOFORM 1), FUNCTION IN TELOMERE REGULATION, TISSUE SPECIFICITY, SINGLE-STRANDED TELOMERE DNA-BINDING, IDENTIFICATION IN THE TELOMERASE RIBONUCLEOPROTEIN COMPLEX, INTERACTION WITH TERT.
[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] OF 888-1419 (ISOFORM 1). Tissue: Testis.
[7]	"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 PP2A CATALYTIC SUBUNITS; SMG1; UPF1; UPF2 AND UPF3B.
[8]	"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.
[9]	"SMG6 is the catalytic endonuclease that cleaves mRNAs containing nonsense codons in metazoan." Huntzinger E., Kashima I., Fauser M., Sauliere J., Izaurralde E. RNA 14:2609-2617(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, DOMAIN, MUTAGENESIS OF ASP-1251 AND ASP-1392.
[10]	"SMG6 promotes endonucleolytic cleavage of nonsense mRNA in human cells." Eberle A.B., Lykke-Andersen S., Muhlemann O., Jensen T.H. Nat. Struct. Mol. Biol. 16:49-55(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, DOMAIN, SUBCELLULAR LOCATION, INTERACTION WITH UPF1, MUTAGENESIS OF ASP-1251; ASP-1353 AND ASP-1392.
[11]	"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 THR-479, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis." Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E. Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
[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]	"Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex." Glavan F., Behm-Ansmant I., Izaurralde E., Conti E. EMBO J. 25:5117-5125(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1239-1419, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-1353.
[15]	"Crystal structure of the PIN domain of human telomerase-associated protein EST1A." Takeshita D., Zenno S., Lee W.C., Saigo K., Tanokura M. Proteins 68:980-989(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1239-1419.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY145883 mRNA. Translation: AAN46114.1.
AB018275 mRNA. Translation: BAA34452.2. Different initiation.
AL133597 mRNA. Translation: CAB63733.1.
AY168921 mRNA. Translation: AAO17581.1.
BC064916 mRNA. Translation: AAH64916.1. Different initiation.

IPI

IPI00015793.
IPI01012883.

PIR

T43475.

RefSeq

NP_001243756.1. NM_001256827.1.
NP_001243757.1. NM_001256828.1.
NP_060045.4. NM_017575.4.

UniGene

Hs.448342.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DOK	X-ray	1.80	A/B	1239-1419	[»]
2HWW	X-ray	1.80	A/B/C	1239-1419	[»]
2HWX	X-ray	1.90	A	1239-1419	[»]

ProteinModelPortal

Q86US8.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q86US8. 4 interactions.

STRING

9606.ENSP00000263073.

PTM databases

PhosphoSite

Q86US8.

Polymorphism databases

DMDM

91771922.

Proteomic databases

PaxDb

Q86US8.

PRIDE

Q86US8.

Protocols and materials databases

DNASU

23293.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263073; ENSP00000263073; ENSG00000070366.
ENST00000544865; ENSP00000443920; ENSG00000070366.

GeneID

23293.

KEGG

hsa:23293.

UCSC

uc002fub.1. human.

Organism-specific databases

CTD

23293.

GeneCards

GC17M001963.

H-InvDB

HIX0013415.

HGNC

HGNC:17809. SMG6.

HPA

HPA042932.

MIM

610963. gene.

neXtProt

NX_Q86US8.

PharmGKB

PA25584.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG313444.

HOGENOM

HOG000112402.

HOVERGEN

HBG051511.

InParanoid

Q86US8.

KO

K11124.

OMA

MRNMQQQ.

OrthoDB

EOG4KKZ29.

PhylomeDB

Q86US8.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q86US8.

Bgee

Q86US8.

CleanEx

HS_SMG6.

Genevestigator

Q86US8.

GermOnline

ENSG00000070366. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR018834. DNA/RNA-bd_Est1-type.
IPR019458. EST1.
IPR002716. PIN_dom.
IPR006596. PINc_nuc-bd.
IPR011990. TPR-like_helical.
[Graphical view]

Pfam

PF10374. EST1. 1 hit.
PF10373. EST1_DNA_bind. 1 hit.
PF13638. PIN_4. 1 hit.
[Graphical view]

SMART

SM00670. PINc. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SMG6. human.

EvolutionaryTrace

Q86US8.

GenomeRNAi

23293.

NextBio

45116.

SOURCE

Search...

Entry information

Entry name

EST1A_HUMAN

Accession

Primary (citable) accession number: Q86US8
Secondary accession number(s): O94837, Q86VH6, Q9UF60

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.