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Q9D168 (INT12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. 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:
Integrator complex subunit 12

Short name=Int12
Alternative name(s):
PHD finger protein 22
Gene names
Name:Ints12
Synonyms:Phf22
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes By similarity.

Subunit structure

Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, CPSF3L/INTS11 and INTS12 By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 1 PHD-type zinc finger.

Ontologies

Keywords
   Cellular componentNucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsnRNA processing

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentintegrator complex

Inferred from sequence or structural similarity. Source: HGNC

   Molecular_functionzinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Integrator complex subunit 12
PRO_0000059314

Regions

Zinc finger158 – 21457PHD-type
Compositional bias269 – 439171Ser-rich

Amino acid modifications

Modified residue1271Phosphoserine By similarity

Secondary structure

................. 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9D168 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9230385FBD4A9425

FASTA46148,568
        10         20         30         40         50         60 
MAATVNLELD PIFLKALGFL HSKSKDSAEK LKALLDESLA RGIDSSYRPT QKDVEPPKIS 

        70         80         90        100        110        120 
STKSLSIKQE PKTSSSLPSG SSNGKVLTAE KIKKEAEKRP ADKMKDVTEG IDVPKKPRLE 

       130        140        150        160        170        180 
KPETRSSPIT VQTSKDLSMA DLSSFEETSA DDFAMEMGLA CVVCRQMTVA SGNQLVECQE 

       190        200        210        220        230        240 
CHNLYHQDCH KPQVTDKEVN DPRLVWYCAR CTRQMKRMAQ KTQKPPQKPA PTVVSVTPTV 

       250        260        270        280        290        300 
KDPLVKKPET KLKQETTFLA FKRTEVKPST VISGNSSSNN VSSSVTSGLT GWAAFAAKTS 

       310        320        330        340        350        360 
SAGPSTAKLN SAAQNSSGKP AASSSNQKPV GLTGLATSSK GGIGSKIGSG NSTSPSVPLK 

       370        380        390        400        410        420 
PLPPLTLGKT GLSRSVSCDN VSKVGLPSPS SLVPGGSSQL SGNGNSATTG PSGSTTSKAT 

       430        440        450        460 
SETSSSTSAS LKGPTSQESQ LNAMKRLQMV KKKAAQKKLK K 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Embryo.
[2]"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].
Strain: FVB/N.
Tissue: Eye, Mammary gland and Mammary tumor.
[3]"Solution structure of PHD domain in protein NP_082203."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 150-224.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003874 mRNA. Translation: BAB23052.1.
AK155162 mRNA. Translation: BAE33085.1.
BC010657 mRNA. Translation: AAH10657.1.
BC023801 mRNA. Translation: AAH23801.1.
BC046996 mRNA. Translation: AAH46996.1.
RefSeqNP_082203.1. NM_027927.3.
UniGeneMm.246726.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEVNMR-A150-224[»]
ProteinModelPortalQ9D168.
SMRQ9D168. Positions 148-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D168. 1 interaction.
MINTMINT-4126517.

PTM databases

PhosphoSiteQ9D168.

Proteomic databases

PaxDbQ9D168.
PRIDEQ9D168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029650; ENSMUSP00000029650; ENSMUSG00000028016.
GeneID71793.
KEGGmmu:71793.
UCSCuc008rkj.1. mouse.

Organism-specific databases

CTD57117.
MGIMGI:1919043. Ints12.

Phylogenomic databases

eggNOGNOG247951.
GeneTreeENSGT00390000005218.
HOGENOMHOG000059634.
HOVERGENHBG081798.
InParanoidQ9D168.
KOK13149.
OMAKQEPKIS.
OrthoDBEOG7QNVN6.
PhylomeDBQ9D168.
TreeFamTF106418.

Gene expression databases

BgeeQ9D168.
CleanExMM_INTS12.
GenevestigatorQ9D168.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9D168.
NextBio334534.
PROQ9D168.
SOURCESearch...

Entry information

Entry nameINT12_MOUSE
AccessionPrimary (citable) accession number: Q9D168
Secondary accession number(s): Q3U2Q5, Q921U2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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