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Protein

Pinin

Gene

Pnn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pinin
Gene namesi
Name:Pnn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1100514. Pnn.

Subcellular locationi

  • Nucleus speckle By similarity
  • Cell junctiondesmosome By similarity

  • Note: Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein (By similarity).By similarity

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: MGI
  • cytoplasm Source: MGI
  • desmosome Source: MGI
  • membrane Source: MGI
  • nuclear speck Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 725724PininPRO_0000190243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei66 – 661PhosphoserineCombined sources
Modified residuei96 – 961PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity
Cross-linki109 – 109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei114 – 1141PhosphoserineBy similarity
Modified residuei115 – 1151PhosphoserineBy similarity
Cross-linki156 – 156Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei237 – 2371N6-acetyllysine; alternateBy similarity
Modified residuei237 – 2371N6-succinyllysine; alternateCombined sources
Cross-linki303 – 303Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei380 – 3801PhosphoserineCombined sources
Modified residuei442 – 4421PhosphoserineCombined sources
Cross-linki536 – 536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki561 – 561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei666 – 6661PhosphoserineBy similarity
Modified residuei700 – 7001PhosphoserineBy similarity
Modified residuei703 – 7031PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO35691.
MaxQBiO35691.
PaxDbiO35691.
PRIDEiO35691.

PTM databases

iPTMnetiO35691.
PhosphoSiteiO35691.

Expressioni

Gene expression databases

CleanExiMM_PNN.

Interactioni

Subunit structurei

Found in a mRNA splicing-dependent exon junction complex (EJC). Found in a complex with SR proteins. Found in a mRNP complex with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18 and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19, PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome C complex (By similarity).By similarity

Protein-protein interaction databases

BioGridi202283. 2 interactions.
IntActiO35691. 1 interaction.
MINTiMINT-1854171.
STRINGi10090.ENSMUSP00000021381.

Structurei

3D structure databases

ProteinModelPortaliO35691.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni220 – 28364Sufficient for PSAP complex assemblyBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 3231Sequence analysisAdd
BLAST
Coiled coili162 – 23372Sequence analysisAdd
BLAST
Coiled coili286 – 37388Sequence analysisAdd
BLAST
Coiled coili444 – 46724Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi171 – 473303Glu-richAdd
BLAST
Compositional biasi468 – 52255Pro-richAdd
BLAST
Compositional biasi471 – 52858Gln-richAdd
BLAST
Compositional biasi579 – 712134Ser-richAdd
BLAST
Compositional biasi640 – 72586Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the pinin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3756. Eukaryota.
ENOG4110W63. LUCA.
HOVERGENiHBG053104.
InParanoidiO35691.
KOiK13114.
PhylomeDBiO35691.

Family and domain databases

InterProiIPR006786. Pinin_SDK_MemA.
IPR006787. Pinin_SDK_N.
[Graphical view]
PfamiPF04696. Pinin_SDK_memA. 1 hit.
PF04697. Pinin_SDK_N. 1 hit.
[Graphical view]
ProDomiPD011048. Pinin_SDK_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35691-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVAVRALQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP
60 70 80 90 100
GGGRGRGSLL LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES
110 120 130 140 150
DPEDDDVKKP ALQSSVVATS KERTRDLIQD QNMDEKGKQR NRRIFGLLMG
160 170 180 190 200
TLQKFKQEST VATERQKRRQ EIEQKLEVQA EEERKQVENE RRELFEERRA
210 220 230 240 250
KQTELRLLEQ KVELAQLQEE WNEHNAKIIK YIRTKTKPHL FYIPGRMCPA
260 270 280 290 300
TQKLIEESQR KMNALFEGRR IEFAEQINKM EARPRRQSMK EKEHQVVRNE
310 320 330 340 350
EQKAEQEEGK VAQREEELEE TGNQHNDVEV EEAGEEEEKE AGIVHSDAEK
360 370 380 390 400
EQEEEEQKQE MEVKTEEEAE VREGEKQQDS QPEEVMDVLE MVESVKHVIA
410 420 430 440 450
EQEVMETNQV ESIEPSENET SKELEPEMEF DVEPDKECKS LSPGKENINS
460 470 480 490 500
QEVEKESEEK EEKEEKEPEP QPEPVAQPQP PPQPLPQSQP HSQPHSQPQP
510 520 530 540 550
VLQSQPLCQP ETLPLAVLQP PPQVIQEQGN LLPERKDFPL ESIKLPEVSV
560 570 580 590 600
EPVLTVHSEN KSKNKTRSRS RGRARNKTSK SRSRSSSSSS SSSSSTSSSS
610 620 630 640 650
GSSSSSGSSS SRSSSSSSSS TSGSSSRDSS SSTSSSSESR SRSRGRGHNR
660 670 680 690 700
DRKHRRSMDR KRRDTSGLER SHKSSKGGSS RDRKGSKDKS SRPDRKRSIS
710 720
ESSRSGKRSS RSERDRKSDR KDKRR
Length:725
Mass (Da):82,436
Last modified:January 23, 2007 - v4
Checksum:iDB99FF2DB17AAF5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311G → A in AAN05017 (Ref. 2) Curated
Sequence conflicti42 – 432AR → GT in CAA69960 (PubMed:9332356).Curated
Sequence conflicti125 – 1251R → RR in BAC27200 (PubMed:16141072).Curated
Sequence conflicti216 – 2172QL → HV in AAN05017 (Ref. 2) Curated
Sequence conflicti287 – 2871Q → P in CAA69960 (PubMed:9332356).Curated
Sequence conflicti327 – 3271D → H in AAN05017 (Ref. 2) Curated
Sequence conflicti365 – 3651T → I in CAA69960 (PubMed:9332356).Curated
Sequence conflicti658 – 6581M → V in BAC27200 (PubMed:16141072).Curated
Sequence conflicti683 – 6831R → T in BAC27200 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08701 mRNA. Translation: CAA69960.1.
AY129403 Genomic DNA. Translation: AAN05017.1.
AK030978 mRNA. Translation: BAC27200.1.
RefSeqiNP_032917.2. NM_008891.2.
UniGeneiMm.22347.

Genome annotation databases

GeneIDi18949.
KEGGimmu:18949.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08701 mRNA. Translation: CAA69960.1.
AY129403 Genomic DNA. Translation: AAN05017.1.
AK030978 mRNA. Translation: BAC27200.1.
RefSeqiNP_032917.2. NM_008891.2.
UniGeneiMm.22347.

3D structure databases

ProteinModelPortaliO35691.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202283. 2 interactions.
IntActiO35691. 1 interaction.
MINTiMINT-1854171.
STRINGi10090.ENSMUSP00000021381.

PTM databases

iPTMnetiO35691.
PhosphoSiteiO35691.

Proteomic databases

EPDiO35691.
MaxQBiO35691.
PaxDbiO35691.
PRIDEiO35691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18949.
KEGGimmu:18949.

Organism-specific databases

CTDi5411.
MGIiMGI:1100514. Pnn.

Phylogenomic databases

eggNOGiKOG3756. Eukaryota.
ENOG4110W63. LUCA.
HOVERGENiHBG053104.
InParanoidiO35691.
KOiK13114.
PhylomeDBiO35691.

Miscellaneous databases

ChiTaRSiPnn. mouse.
PROiO35691.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PNN.

Family and domain databases

InterProiIPR006786. Pinin_SDK_MemA.
IPR006787. Pinin_SDK_N.
[Graphical view]
PfamiPF04696. Pinin_SDK_memA. 1 hit.
PF04697. Pinin_SDK_N. 1 hit.
[Graphical view]
ProDomiPD011048. Pinin_SDK_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and analysis of cDNA encoding murine pinin."
    Ouyang P., Zhen Y.Y., Sugrue S.P.
    Gene 197:115-120(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Mouse pinin gene."
    Leu S., Ouyang P.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. "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.
    Tissue: Thymus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-380 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPININ_MOUSE
AccessioniPrimary (citable) accession number: O35691
Secondary accession number(s): Q8CD89, Q8CGU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 106 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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 one 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.