Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

PC4 and SFRS1-interacting protein

Gene

Psip1

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

Functioni

Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • mRNA 5'-splice site recognition Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to heat Source: UniProtKB
  • response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
PC4 and SFRS1-interacting protein
Alternative name(s):
Lens epithelium-derived growth factor
Short name:
mLEDGF
Gene namesi
Name:Psip1
Synonyms:Ledgf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2142116. Psip1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528PC4 and SFRS1-interacting proteinPRO_0000191709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei106 – 1061PhosphoserineCombined sources
Modified residuei115 – 1151PhosphothreonineCombined sources
Modified residuei122 – 1221PhosphothreonineCombined sources
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei141 – 1411PhosphothreonineCombined sources
Modified residuei176 – 1761PhosphoserineCombined sources
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei270 – 2701PhosphoserineCombined sources
Modified residuei271 – 2711PhosphothreonineCombined sources
Modified residuei272 – 2721PhosphoserineCombined sources
Modified residuei274 – 2741PhosphoserineCombined sources
Modified residuei432 – 4321PhosphoserineBy similarity
Modified residuei435 – 4351PhosphothreonineBy similarity
Modified residuei441 – 4411PhosphoserineBy similarity
Modified residuei515 – 5151Citrulline1 Publication
Modified residuei520 – 5201PhosphoserineCombined sources
Modified residuei525 – 5251PhosphothreonineBy similarity

Post-translational modificationi

Citrullinated by PADI4.1 Publication

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

EPDiQ99JF8.
MaxQBiQ99JF8.
PaxDbiQ99JF8.
PRIDEiQ99JF8.

PTM databases

iPTMnetiQ99JF8.
PhosphoSiteiQ99JF8.

Expressioni

Gene expression databases

BgeeiQ99JF8.
CleanExiMM_PSIP1.
ExpressionAtlasiQ99JF8. baseline and differential.
GenevisibleiQ99JF8. MM.

Interactioni

Subunit structurei

Interacts with IFRD1/PC4. Interacts POGZ and CDCA7L (By similarity). Murine leukemia virus (MLV) integrase does not interact with PSIP1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221716. 3 interactions.
IntActiQ99JF8. 2 interactions.
MINTiMINT-4123368.
STRINGi10090.ENSMUSP00000030207.

Structurei

3D structure databases

ProteinModelPortaliQ99JF8.
SMRiQ99JF8. Positions 1-93, 346-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 6458PWWPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili306 – 33227Sequence analysisAdd
BLAST
Coiled coili369 – 39325Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi146 – 15611Nuclear localization signalBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the HDGF family.Curated
Contains 1 PWWP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1904. Eukaryota.
ENOG410Y5WD. LUCA.
GeneTreeiENSGT00530000063013.
HOVERGENiHBG108300.
InParanoidiQ99JF8.
OMAiESKDSHE.
OrthoDBiEOG7NKKMQ.
PhylomeDBiQ99JF8.
TreeFamiTF105385.

Family and domain databases

InterProiIPR021567. LEDGF.
IPR000313. PWWP_dom.
IPR017859. Treacle-like_TCS.
[Graphical view]
PfamiPF11467. LEDGF. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
PRINTSiPR01503. TREACLE.
SMARTiSM00293. PWWP. 1 hit.
[Graphical view]
PROSITEiPS50812. PWWP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99JF8-1) [UniParc]FASTAAdd to basket

Also known as: Ledgfa, p75

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
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET
60 70 80 90 100
AFLGPKDIFP YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQASTK
110 120 130 140 150
QSNASSDVEV EEKETNVSKE DTDQEEKASN EDVTKAVDIT TPKAARRGRK
160 170 180 190 200
RKAEKQVDTE EAGMVTAATA SNVKASPKRG RPAATEVKIP KPRGRPKVVK
210 220 230 240 250
QPCPSDGDMV IDEDKSKKKG PEEKQPKKQL KKEEEGQKEE EKPRKEPDKK
260 270 280 290 300
EGKKEVESKR KNLAKPGVTS TSDSEDEDDQ EGEKKRKGGR NFQAAHRRNM
310 320 330 340 350
LKGQHEKEAG DRKRKQEEQM ETEQQNKDEG KKPEVKKVEK KRETSMDSRL
360 370 380 390 400
QRIHAEIKNS LKIDNLDVNR CIEALDELAS LQVTMQQAQK HTEMITTLKK
410 420 430 440 450
IRRFKVSQVI MEKSTMLYNK FKNMFLVGEG DSVITQVLNK SLAEQRQHEE
460 470 480 490 500
ANKTKDQGKK GPNKKLEKEP TGTKSLNGGS DAQESNHPQH NGDSNEDGKD
510 520
SREASSKTKP PGEEREAEIS LKESTLDN
Length:528
Mass (Da):59,697
Last modified:June 1, 2001 - v1
Checksum:i4A9AE28245843AB6
GO
Isoform 2 (identifier: Q99JF8-2) [UniParc]FASTAAdd to basket

Also known as: Ledgfb, p52

The sequence of this isoform differs from the canonical sequence as follows:
     324-331: QQNKDEGK → HQTTCNLQ
     332-528: Missing.

Show »
Length:331
Mass (Da):37,426
Checksum:i516F01D99A5DD5A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: Q99JF8-2)
Sequence conflicti324 – 3318HQTTCNLQ → QLKALIQ in AAH52177 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei324 – 3318QQNKDEGK → HQTTCNLQ in isoform 2. 3 PublicationsVSP_014299
Alternative sequencei332 – 528197Missing in isoform 2. 3 PublicationsVSP_014300Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ308965 mRNA. Translation: CAC34944.1.
AJ308966 mRNA. Translation: CAC34945.1.
AF339082 mRNA. Translation: AAO32949.1.
AF339083 mRNA. Translation: AAO32950.1.
BX682545 Genomic DNA. Translation: CAM20466.1.
BX682545 Genomic DNA. Translation: CAM20467.1.
BC002260 mRNA. Translation: AAH02260.1.
BC043079 mRNA. Translation: AAH43079.1.
BC052177 mRNA. Translation: AAH52177.1.
AK011572 mRNA. Translation: BAB27707.3.
AK139598 mRNA. Translation: BAE24079.1.
AK161426 mRNA. Translation: BAE36388.1.
AK169600 mRNA. Translation: BAE41251.1.
CCDSiCCDS18299.1. [Q99JF8-1]
CCDS71412.1. [Q99JF8-2]
RefSeqiNP_001277456.1. NM_001290527.1. [Q99JF8-2]
NP_598709.1. NM_133948.5. [Q99JF8-1]
UniGeneiMm.105331.
Mm.260943.
Mm.448301.
Mm.451848.

Genome annotation databases

EnsembliENSMUST00000030207; ENSMUSP00000030207; ENSMUSG00000028484. [Q99JF8-1]
ENSMUST00000107215; ENSMUSP00000102833; ENSMUSG00000028484. [Q99JF8-2]
GeneIDi101739.
KEGGimmu:101739.
UCSCiuc008tkw.2. mouse. [Q99JF8-1]
uc008tkx.2. mouse. [Q99JF8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ308965 mRNA. Translation: CAC34944.1.
AJ308966 mRNA. Translation: CAC34945.1.
AF339082 mRNA. Translation: AAO32949.1.
AF339083 mRNA. Translation: AAO32950.1.
BX682545 Genomic DNA. Translation: CAM20466.1.
BX682545 Genomic DNA. Translation: CAM20467.1.
BC002260 mRNA. Translation: AAH02260.1.
BC043079 mRNA. Translation: AAH43079.1.
BC052177 mRNA. Translation: AAH52177.1.
AK011572 mRNA. Translation: BAB27707.3.
AK139598 mRNA. Translation: BAE24079.1.
AK161426 mRNA. Translation: BAE36388.1.
AK169600 mRNA. Translation: BAE41251.1.
CCDSiCCDS18299.1. [Q99JF8-1]
CCDS71412.1. [Q99JF8-2]
RefSeqiNP_001277456.1. NM_001290527.1. [Q99JF8-2]
NP_598709.1. NM_133948.5. [Q99JF8-1]
UniGeneiMm.105331.
Mm.260943.
Mm.448301.
Mm.451848.

3D structure databases

ProteinModelPortaliQ99JF8.
SMRiQ99JF8. Positions 1-93, 346-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221716. 3 interactions.
IntActiQ99JF8. 2 interactions.
MINTiMINT-4123368.
STRINGi10090.ENSMUSP00000030207.

PTM databases

iPTMnetiQ99JF8.
PhosphoSiteiQ99JF8.

Proteomic databases

EPDiQ99JF8.
MaxQBiQ99JF8.
PaxDbiQ99JF8.
PRIDEiQ99JF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030207; ENSMUSP00000030207; ENSMUSG00000028484. [Q99JF8-1]
ENSMUST00000107215; ENSMUSP00000102833; ENSMUSG00000028484. [Q99JF8-2]
GeneIDi101739.
KEGGimmu:101739.
UCSCiuc008tkw.2. mouse. [Q99JF8-1]
uc008tkx.2. mouse. [Q99JF8-2]

Organism-specific databases

CTDi11168.
MGIiMGI:2142116. Psip1.

Phylogenomic databases

eggNOGiKOG1904. Eukaryota.
ENOG410Y5WD. LUCA.
GeneTreeiENSGT00530000063013.
HOVERGENiHBG108300.
InParanoidiQ99JF8.
OMAiESKDSHE.
OrthoDBiEOG7NKKMQ.
PhylomeDBiQ99JF8.
TreeFamiTF105385.

Miscellaneous databases

ChiTaRSiPsip1. mouse.
PROiQ99JF8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JF8.
CleanExiMM_PSIP1.
ExpressionAtlasiQ99JF8. baseline and differential.
GenevisibleiQ99JF8. MM.

Family and domain databases

InterProiIPR021567. LEDGF.
IPR000313. PWWP_dom.
IPR017859. Treacle-like_TCS.
[Graphical view]
PfamiPF11467. LEDGF. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
PRINTSiPR01503. TREACLE.
SMARTiSM00293. PWWP. 1 hit.
[Graphical view]
PROSITEiPS50812. PWWP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Bashein A.M., Brady G.
    Thesis (2000), University of Manchester, United Kingdom
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  2. Yu L.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and Czech II.
    Tissue: Brain, Limb and Mammary gland.
  5. "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] OF 1-248.
    Strain: C57BL/6J and NOD.
    Tissue: Egg, Embryo, Testis and Thymus.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-176; SER-272 AND SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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-106; SER-176; SER-272 AND SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-106; THR-115; THR-122; SER-129; THR-141; SER-176; SER-270; THR-271; SER-272; SER-274 AND SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. Cited for: CITRULLINATION AT ARG-515.

Entry informationi

Entry nameiPSIP1_MOUSE
AccessioniPrimary (citable) accession number: Q99JF8
Secondary accession number(s): A2BI10
, A2BI11, Q3TEJ7, Q3TTD7, Q3UTA1, Q80WQ7, Q99JF7, Q99LR4, Q9CT03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 123 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

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.