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Q69ZQ2 (ISY1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-mRNA-splicing factor ISY1 homolog
Gene names
Name:Isy1
Synonyms:Kiaa1160
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in pre-mRNA splicing Potential.

Subunit structure

Identified in the spliceosome C complex By similarity.

Subcellular location

Nucleus Potential.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Sequence similarities

Belongs to the ISY1 family.

Sequence caution

The sequence BAD32394.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Pre-mRNA-splicing factor ISY1 homolog
PRO_0000235814

Regions

Compositional bias201 – 21111Poly-Glu

Amino acid modifications

Modified residue1271N6-acetyllysine By similarity
Modified residue2221Phosphoserine By similarity
Modified residue2471Phosphoserine By similarity

Experimental info

Sequence conflict1331R → K in BAB31028. Ref.2

Secondary structure

....... 285
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q69ZQ2 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 4A456045660F29D6

FASTA28532,989
        10         20         30         40         50         60 
MARNAEKAMT ALARFRQAQL EEGKVKERRP FLASECTELP KAEKWRRQII GEISKKVAQI 

        70         80         90        100        110        120 
QNAGLGEFRI RDLNDEINKL LREKGHWEVR IKELGGPDYG KVGPKMLDHE GKEVPGNRGY 

       130        140        150        160        170        180 
KYFGAAKDLP GVRELFEKEP LPPPRKTRAE LMKAIDFEYY GYLDEDDGVI VPLEQEYEKK 

       190        200        210        220        230        240 
LRAELVEKWK AEREARLARG EKEEEEEEEE EINIYAVTEE ESDEEGNQEK AGEDGQQKFI 

       250        260        270        280 
AHVPVPSQQE IEEALVRRKK MELLQKYASE TLQAQSEEAK RLLGY 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary gland.
[4]"Solution structure of ISY1 domain in hypothetical protein."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 24-102.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK173116 mRNA. Translation: BAD32394.1. Different initiation.
AK017996 mRNA. Translation: BAB31028.1.
BC020103 mRNA. Translation: AAH20103.1.
BC037695 mRNA. Translation: AAH37695.1.
IPIIPI00469994.
RefSeqNP_598695.1. NM_133934.4.
UniGeneMm.241546.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4TNMR-A23-102[»]
ProteinModelPortalQ69ZQ2.
SMRQ69ZQ2. Positions 23-102.
ModBaseSearch...

PTM databases

PhosphoSiteQ69ZQ2.

Proteomic databases

PRIDEQ69ZQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089497; ENSMUSP00000086923; ENSMUSG00000030056.
GeneID57905.
KEGGmmu:57905.
UCSCuc009cub.1. mouse.

Organism-specific databases

CTD57461.
MGIMGI:1923310. Isy1.
RougeSearch...

Phylogenomic databases

eggNOGroNOG07206.
HOGENOMHBG628655.
HOVERGENHBG061071.
InParanoidQ69ZQ2.
OMARRYGPKM.
OrthoDBEOG4DJJX6.
PhylomeDBQ69ZQ2.

Gene expression databases

ArrayExpressQ69ZQ2.
BgeeQ69ZQ2.
CleanExMM_ISY1.
GenevestigatorQ69ZQ2.
GermOnlineENSMUSG00000030056. Mus musculus.

Family and domain databases

InterProIPR009360. Isy1.
[Graphical view]
KOK12870.
PANTHERPTHR13021. Isy1. 1 hit.
PfamPF06246. Isy1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio314069.
SOURCESearch...

Entry information

Entry nameISY1_MOUSE
AccessionPrimary (citable) accession number: Q69ZQ2
Secondary accession number(s): Q8VDX4, Q9D3E2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: November 16, 2011
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families