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Protein

Integrator complex subunit 12

Gene

Ints12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 21457PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. snRNA processing Source: HGNC
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Integrator complex subunit 12
Short name:
Int12
Alternative name(s):
PHD finger protein 22
Gene namesi
Name:Ints12
Synonyms:Phf22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1919043. Ints12.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. integrator complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Integrator complex subunit 12PRO_0000059314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9D168.
PaxDbiQ9D168.
PRIDEiQ9D168.

PTM databases

PhosphoSiteiQ9D168.

Expressioni

Gene expression databases

BgeeiQ9D168.
CleanExiMM_INTS12.
GenevestigatoriQ9D168.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9D168. 1 interaction.
MINTiMINT-4126517.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi154 – 1574Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi184 – 1863Combined sources
Turni187 – 1893Combined sources
Beta strandi190 – 1923Combined sources
Helixi196 – 2005Combined sources
Helixi209 – 2157Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEVNMR-A150-224[»]
ProteinModelPortaliQ9D168.
SMRiQ9D168. Positions 148-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D168.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi269 – 439171Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 21457PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG247951.
GeneTreeiENSGT00390000005218.
HOGENOMiHOG000059634.
HOVERGENiHBG081798.
InParanoidiQ9D168.
KOiK13149.
OMAiKQEPKIS.
OrthoDBiEOG7QNVN6.
PhylomeDBiQ9D168.
TreeFamiTF106418.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATVNLELD PIFLKALGFL HSKSKDSAEK LKALLDESLA RGIDSSYRPT
60 70 80 90 100
QKDVEPPKIS STKSLSIKQE PKTSSSLPSG SSNGKVLTAE KIKKEAEKRP
110 120 130 140 150
ADKMKDVTEG IDVPKKPRLE KPETRSSPIT VQTSKDLSMA DLSSFEETSA
160 170 180 190 200
DDFAMEMGLA CVVCRQMTVA SGNQLVECQE CHNLYHQDCH KPQVTDKEVN
210 220 230 240 250
DPRLVWYCAR CTRQMKRMAQ KTQKPPQKPA PTVVSVTPTV KDPLVKKPET
260 270 280 290 300
KLKQETTFLA FKRTEVKPST VISGNSSSNN VSSSVTSGLT GWAAFAAKTS
310 320 330 340 350
SAGPSTAKLN SAAQNSSGKP AASSSNQKPV GLTGLATSSK GGIGSKIGSG
360 370 380 390 400
NSTSPSVPLK PLPPLTLGKT GLSRSVSCDN VSKVGLPSPS SLVPGGSSQL
410 420 430 440 450
SGNGNSATTG PSGSTTSKAT SETSSSTSAS LKGPTSQESQ LNAMKRLQMV
460
KKKAAQKKLK K
Length:461
Mass (Da):48,568
Last modified:June 1, 2001 - v1
Checksum:i9230385FBD4A9425
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17848.1.
RefSeqiNP_082203.1. NM_027927.3.
UniGeneiMm.246726.

Genome annotation databases

EnsembliENSMUST00000029650; ENSMUSP00000029650; ENSMUSG00000028016.
GeneIDi71793.
KEGGimmu:71793.
UCSCiuc008rkj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17848.1.
RefSeqiNP_082203.1. NM_027927.3.
UniGeneiMm.246726.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEVNMR-A150-224[»]
ProteinModelPortaliQ9D168.
SMRiQ9D168. Positions 148-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D168. 1 interaction.
MINTiMINT-4126517.

PTM databases

PhosphoSiteiQ9D168.

Proteomic databases

MaxQBiQ9D168.
PaxDbiQ9D168.
PRIDEiQ9D168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029650; ENSMUSP00000029650; ENSMUSG00000028016.
GeneIDi71793.
KEGGimmu:71793.
UCSCiuc008rkj.1. mouse.

Organism-specific databases

CTDi57117.
MGIiMGI:1919043. Ints12.

Phylogenomic databases

eggNOGiNOG247951.
GeneTreeiENSGT00390000005218.
HOGENOMiHOG000059634.
HOVERGENiHBG081798.
InParanoidiQ9D168.
KOiK13149.
OMAiKQEPKIS.
OrthoDBiEOG7QNVN6.
PhylomeDBiQ9D168.
TreeFamiTF106418.

Miscellaneous databases

EvolutionaryTraceiQ9D168.
NextBioi334534.
PROiQ9D168.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D168.
CleanExiMM_INTS12.
GenevestigatoriQ9D168.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiINT12_MOUSE
AccessioniPrimary (citable) accession number: Q9D168
Secondary accession number(s): Q3U2Q5, Q921U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.