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Q8NCE0

- SEN2_HUMAN

UniProt

Q8NCE0 - SEN2_HUMAN

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Protein

tRNA-splicing endonuclease subunit Sen2

Gene

TSEN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. Isoform 1 probably carries the active site for 5'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events. Isoform 2 is responsible for processing a yet unknown RNA substrate. The complex containing isoform 2 is not able to cleave pre-tRNAs properly, although it retains endonucleolytic activity.1 Publication

Catalytic activityi

PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei369 – 3691By similarity
Active sitei377 – 3771By similarity
Active sitei416 – 4161By similarity

GO - Molecular functioni

  1. lyase activity Source: UniProtKB-KW
  2. nucleic acid binding Source: InterPro
  3. tRNA-intron endonuclease activity Source: InterPro

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. tRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

mRNA processing, tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-splicing endonuclease subunit Sen2 (EC:4.6.1.16)
Alternative name(s):
tRNA-intron endonuclease Sen2
Short name:
HsSen2
Gene namesi
Name:TSEN2
Synonyms:SEN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:28422. TSEN2.

Subcellular locationi

Nucleus 1 Publication. Nucleusnucleolus 1 Publication
Note: May be transiently localized in the nucleolus.

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: HPA
  3. nucleus Source: HPA
  4. tRNA-intron endonuclease complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Pontocerebellar hypoplasia 2B (PCH2B) [MIM:612389]: A disorder characterized by an abnormally small cerebellum and brainstem, and progressive microcephaly from birth combined with extrapyramidal dyskinesia. Severe chorea occurs and epilepsy is frequent. There are no signs of spinal cord anterior horn cells degeneration.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti309 – 3091Y → C in PCH2B. 1 Publication
Corresponds to variant rs113994149 [ dbSNP | Ensembl ].
VAR_054810

Keywords - Diseasei

Pontocerebellar hypoplasia

Organism-specific databases

MIMi612389. phenotype.
Orphaneti2524. Pontocerebellar hypoplasia type 2.
PharmGKBiPA142670695.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465tRNA-splicing endonuclease subunit Sen2PRO_0000109452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei408 – 4081PhosphoserineBy similarity
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei415 – 4151PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NCE0.
PaxDbiQ8NCE0.
PRIDEiQ8NCE0.

PTM databases

PhosphoSiteiQ8NCE0.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are widely expressed at very low level.1 Publication

Gene expression databases

BgeeiQ8NCE0.
CleanExiHS_TSEN2.
ExpressionAtlasiQ8NCE0. baseline and differential.
GenevestigatoriQ8NCE0.

Organism-specific databases

HPAiHPA027120.
HPA027125.
HPA027268.

Interactioni

Subunit structurei

tRNA splicing endonuclease is a heterotetramer composed of isoform 1 of SEN2, SEN15, SEN34/LENG5 and SEN54. tRNA splicing endonuclease complex also contains proteins of the pre-mRNA 3'-end processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2. Isoform 2 belongs to a different complex that contains SEN54 but low level of SEN15 and SEN34/LENG5.

Protein-protein interaction databases

BioGridi123288. 19 interactions.
IntActiQ8NCE0. 1 interaction.
STRINGi9606.ENSP00000284995.

Structurei

3D structure databases

ProteinModelPortaliQ8NCE0.
SMRiQ8NCE0. Positions 279-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tRNA-intron endonuclease family.Curated

Phylogenomic databases

eggNOGiCOG1676.
GeneTreeiENSGT00390000013266.
HOGENOMiHOG000154285.
HOVERGENiHBG056610.
InParanoidiQ8NCE0.
KOiK15322.
OMAiTESKEVQ.
PhylomeDBiQ8NCE0.
TreeFamiTF314679.

Family and domain databases

Gene3Di3.40.1350.10. 1 hit.
InterProiIPR011856. tRNA_endonuc-like_dom.
IPR006677. tRNA_intron_Endonuc_cat-like.
IPR006678. tRNA_intron_Endonuc_N.
IPR016589. tRNA_splic_SEN2.
[Graphical view]
PfamiPF01974. tRNA_int_endo. 1 hit.
PF02778. tRNA_int_endo_N. 1 hit.
[Graphical view]
PIRSFiPIRSF011789. tRNA_splic_SEN2. 1 hit.
SUPFAMiSSF53032. SSF53032. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NCE0) [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
MAEAVFHAPK RKRRVYETYE SPLPIPFGQD HGPLKEFKIF RAEMINNNVI
60 70 80 90 100
VRNAEDIEQL YGKGYFGKGI LSRSRPSFTI SDPKLVAKWK DMKTNMPIIT
110 120 130 140 150
SKRYQHSVEW AAELMRRQGQ DESTVRRILK DYTKPLEHPP VKRNEEAQVH
160 170 180 190 200
DKLNSGMVSN MEGTAGGERP SVVNGDSGKS GGVGDPREPL GCLQEGSGCH
210 220 230 240 250
PTTESFEKSV REDASPLPHV CCCKQDALIL QRGLHHEDGS QHIGLLHPGD
260 270 280 290 300
RGPDHEYVLV EEAECAMSER EAAPNEELVQ RNRLICRRNP YRIFEYLQLS
310 320 330 340 350
LEEAFFLVYA LGCLSIYYEK EPLTIVKLWK AFTVVQPTFR TTYMAYHYFR
360 370 380 390 400
SKGWVPKVGL KYGTDLLLYR KGPPFYHASY SVIIELVDDH FEGSLRRPLS
410 420 430 440 450
WKSLAALSRV SVNVSKELML CYLIKPSTMT DKEMESPECM KRIKVQEVIL
460
SRWVSSRERS DQDDL
Length:465
Mass (Da):53,247
Last modified:July 19, 2004 - v2
Checksum:iFF523229B05A1345
GO
Isoform 2 (identifier: Q8NCE0-2) [UniParc]FASTAAdd to Basket

Also known as: SEN2deltaEx8, DeltaEx8

The sequence of this isoform differs from the canonical sequence as follows:
     304-320: Missing.

Show »
Length:448
Mass (Da):51,265
Checksum:iB616BDFCDA590E32
GO
Isoform 3 (identifier: Q8NCE0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-303: Missing.

Note: No experimental confirmation available.

Show »
Length:439
Mass (Da):49,942
Checksum:i97A9E847199BDE08
GO
Isoform 4 (identifier: Q8NCE0-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     173-231: Missing.

Note: No experimental confirmation available.

Show »
Length:406
Mass (Da):47,124
Checksum:i61FD06EBE21EEEFD
GO
Isoform 5 (identifier: Q8NCE0-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     276-301: Missing.
     417-465: ELMLCYLIKPSTMTDKEMESPECMKRIKVQEVILSRWVSSRERSDQDDL → VTQHQLCHWSVT

Note: No experimental confirmation available.

Show »
Length:402
Mass (Da):45,532
Checksum:i8B231F84B72FA227
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381H → Q in BAH13287. (PubMed:14702039)Curated
Sequence conflicti208 – 2081K → E in BAH13287. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411R → H.
Corresponds to variant rs12495784 [ dbSNP | Ensembl ].
VAR_048931
Natural varianti126 – 1261R → H.
Corresponds to variant rs33955793 [ dbSNP | Ensembl ].
VAR_048932
Natural varianti309 – 3091Y → C in PCH2B. 1 Publication
Corresponds to variant rs113994149 [ dbSNP | Ensembl ].
VAR_054810

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei173 – 23159Missing in isoform 4. 1 PublicationVSP_046192Add
BLAST
Alternative sequencei276 – 30126Missing in isoform 5. 1 PublicationVSP_046193Add
BLAST
Alternative sequencei278 – 30326Missing in isoform 3. 1 PublicationVSP_010985Add
BLAST
Alternative sequencei304 – 32017Missing in isoform 2. 1 PublicationVSP_010986Add
BLAST
Alternative sequencei417 – 46549ELMLC…DQDDL → VTQHQLCHWSVT in isoform 5. 1 PublicationVSP_046194Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK074794 mRNA. Translation: BAC11213.1.
AK300449 mRNA. Translation: BAH13287.1.
AK225875 mRNA. No translation available.
AC018500 Genomic DNA. No translation available.
AC090947 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64129.1.
BC004178 mRNA. Translation: AAH04178.1.
BC004211 mRNA. Translation: AAH04211.1.
BC019582 mRNA. Translation: AAH19582.1.
BC021975 mRNA. Translation: AAH21975.2.
CCDSiCCDS2611.1. [Q8NCE0-1]
CCDS46757.1. [Q8NCE0-3]
CCDS46758.1. [Q8NCE0-4]
CCDS46759.1. [Q8NCE0-5]
RefSeqiNP_001138864.1. NM_001145392.1. [Q8NCE0-1]
NP_001138865.1. NM_001145393.1. [Q8NCE0-3]
NP_001138866.1. NM_001145394.1. [Q8NCE0-4]
NP_001138867.1. NM_001145395.1. [Q8NCE0-5]
NP_079541.1. NM_025265.3. [Q8NCE0-1]
XP_005265552.1. XM_005265495.1. [Q8NCE0-1]
XP_005265554.1. XM_005265497.1. [Q8NCE0-3]
UniGeneiHs.335550.

Genome annotation databases

EnsembliENST00000284995; ENSP00000284995; ENSG00000154743. [Q8NCE0-1]
ENST00000402228; ENSP00000385976; ENSG00000154743. [Q8NCE0-1]
ENST00000415684; ENSP00000416510; ENSG00000154743. [Q8NCE0-3]
ENST00000444864; ENSP00000407974; ENSG00000154743. [Q8NCE0-5]
ENST00000454502; ENSP00000392029; ENSG00000154743. [Q8NCE0-4]
GeneIDi80746.
KEGGihsa:80746.
UCSCiuc003bxa.3. human. [Q8NCE0-3]
uc003bxb.3. human. [Q8NCE0-1]
uc011auq.1. human.

Polymorphism databases

DMDMi50428914.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK074794 mRNA. Translation: BAC11213.1 .
AK300449 mRNA. Translation: BAH13287.1 .
AK225875 mRNA. No translation available.
AC018500 Genomic DNA. No translation available.
AC090947 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64129.1 .
BC004178 mRNA. Translation: AAH04178.1 .
BC004211 mRNA. Translation: AAH04211.1 .
BC019582 mRNA. Translation: AAH19582.1 .
BC021975 mRNA. Translation: AAH21975.2 .
CCDSi CCDS2611.1. [Q8NCE0-1 ]
CCDS46757.1. [Q8NCE0-3 ]
CCDS46758.1. [Q8NCE0-4 ]
CCDS46759.1. [Q8NCE0-5 ]
RefSeqi NP_001138864.1. NM_001145392.1. [Q8NCE0-1 ]
NP_001138865.1. NM_001145393.1. [Q8NCE0-3 ]
NP_001138866.1. NM_001145394.1. [Q8NCE0-4 ]
NP_001138867.1. NM_001145395.1. [Q8NCE0-5 ]
NP_079541.1. NM_025265.3. [Q8NCE0-1 ]
XP_005265552.1. XM_005265495.1. [Q8NCE0-1 ]
XP_005265554.1. XM_005265497.1. [Q8NCE0-3 ]
UniGenei Hs.335550.

3D structure databases

ProteinModelPortali Q8NCE0.
SMRi Q8NCE0. Positions 279-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123288. 19 interactions.
IntActi Q8NCE0. 1 interaction.
STRINGi 9606.ENSP00000284995.

PTM databases

PhosphoSitei Q8NCE0.

Polymorphism databases

DMDMi 50428914.

Proteomic databases

MaxQBi Q8NCE0.
PaxDbi Q8NCE0.
PRIDEi Q8NCE0.

Protocols and materials databases

DNASUi 80746.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284995 ; ENSP00000284995 ; ENSG00000154743 . [Q8NCE0-1 ]
ENST00000402228 ; ENSP00000385976 ; ENSG00000154743 . [Q8NCE0-1 ]
ENST00000415684 ; ENSP00000416510 ; ENSG00000154743 . [Q8NCE0-3 ]
ENST00000444864 ; ENSP00000407974 ; ENSG00000154743 . [Q8NCE0-5 ]
ENST00000454502 ; ENSP00000392029 ; ENSG00000154743 . [Q8NCE0-4 ]
GeneIDi 80746.
KEGGi hsa:80746.
UCSCi uc003bxa.3. human. [Q8NCE0-3 ]
uc003bxb.3. human. [Q8NCE0-1 ]
uc011auq.1. human.

Organism-specific databases

CTDi 80746.
GeneCardsi GC03P012525.
HGNCi HGNC:28422. TSEN2.
HPAi HPA027120.
HPA027125.
HPA027268.
MIMi 608753. gene.
612389. phenotype.
neXtProti NX_Q8NCE0.
Orphaneti 2524. Pontocerebellar hypoplasia type 2.
PharmGKBi PA142670695.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1676.
GeneTreei ENSGT00390000013266.
HOGENOMi HOG000154285.
HOVERGENi HBG056610.
InParanoidi Q8NCE0.
KOi K15322.
OMAi TESKEVQ.
PhylomeDBi Q8NCE0.
TreeFami TF314679.

Miscellaneous databases

GeneWikii TSEN2.
GenomeRNAii 80746.
NextBioi 71098.
PROi Q8NCE0.
SOURCEi Search...

Gene expression databases

Bgeei Q8NCE0.
CleanExi HS_TSEN2.
ExpressionAtlasi Q8NCE0. baseline and differential.
Genevestigatori Q8NCE0.

Family and domain databases

Gene3Di 3.40.1350.10. 1 hit.
InterProi IPR011856. tRNA_endonuc-like_dom.
IPR006677. tRNA_intron_Endonuc_cat-like.
IPR006678. tRNA_intron_Endonuc_N.
IPR016589. tRNA_splic_SEN2.
[Graphical view ]
Pfami PF01974. tRNA_int_endo. 1 hit.
PF02778. tRNA_int_endo_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF011789. tRNA_splic_SEN2. 1 hit.
SUPFAMi SSF53032. SSF53032. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3' end formation."
    Paushkin S.V., Patel M., Furia B.S., Peltz S.W., Trotta C.R.
    Cell 117:311-321(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF A COMPLEX WITH SEN15; SEN34; SEN54 AND CLP1, TISSUE SPECIFICITY.
  2. "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.
    , 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] (ISOFORMS 3 AND 5).
    Tissue: Placenta and Teratocarcinoma.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] (ISOFORM 1).
    Tissue: Colon, Eye and Skin.
  7. Cited for: VARIANT PCH2B CYS-309.

Entry informationi

Entry nameiSEN2_HUMAN
AccessioniPrimary (citable) accession number: Q8NCE0
Secondary accession number(s): B7Z6K1
, C9IZI7, G5E9Q3, Q8WTW7, Q9BPU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 103 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3