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Q9R1C7

- PR40A_MOUSE

UniProt

Q9R1C7 - PR40A_MOUSE

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Protein

Pre-mRNA-processing factor 40 homolog A

Gene
Prpf40a, Fbp11, Fnbp3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.1 Publication

GO - Molecular functioni

  1. proline-rich region binding Source: MGI
  2. protein binding Source: MGI

GO - Biological processi

  1. cell migration Source: UniProtKB
  2. cytoskeleton organization Source: UniProtKB
  3. mRNA processing Source: UniProtKB-KW
  4. regulation of cell shape Source: UniProtKB
  5. regulation of cytokinesis Source: UniProtKB
  6. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing factor 40 homolog A
Alternative name(s):
Formin-binding protein 11
Short name:
FBP-11
Formin-binding protein 3
Gene namesi
Name:Prpf40a
Synonyms:Fbp11, Fnbp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1860512. Prpf40a.

Subcellular locationi

Nucleus speckle. Nucleus matrix
Note: Colocalizes with AKAP8L in the nuclear matrix.2 Publications

GO - Cellular componenti

  1. nuclear matrix Source: UniProtKB
  2. nuclear speck Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 953953Pre-mRNA-processing factor 40 homolog APRO_0000076086Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511Phosphoserine By similarity
Modified residuei196 – 1961N6-acetyllysine1 Publication
Modified residuei369 – 3691Phosphothreonine By similarity
Modified residuei879 – 8791Phosphoserine By similarity
Modified residuei881 – 8811Phosphoserine By similarity
Modified residuei884 – 8841Phosphoserine By similarity
Modified residuei928 – 9281Phosphothreonine1 Publication
Modified residuei929 – 9291Phosphoserine1 Publication
Modified residuei931 – 9311Phosphoserine1 Publication
Modified residuei934 – 9341Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9R1C7.
PaxDbiQ9R1C7.
PRIDEiQ9R1C7.

PTM databases

PhosphoSiteiQ9R1C7.

Expressioni

Gene expression databases

ArrayExpressiQ9R1C7.
BgeeiQ9R1C7.
GenevestigatoriQ9R1C7.

Interactioni

Subunit structurei

Interacts with the N-terminus of HTT and with the phosphorylated C-terminal domain of POLR2A By similarity. Interacts with AKAP8L, SF1, SRPK1, CARD8, ATBF1 and MECP2. Interacts through the WW domains with formin proline-rich regions and with WASL/N-WASP.4 Publications

Protein-protein interaction databases

BioGridi207833. 5 interactions.
IntActiQ9R1C7. 4 interactions.
MINTiMINT-1525232.
STRINGi10090.ENSMUSP00000075655.

Structurei

3D structure databases

ProteinModelPortaliQ9R1C7.
SMRiQ9R1C7. Positions 133-222, 378-446, 739-802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 17334WW 1Add
BLAST
Domaini181 – 21434WW 2Add
BLAST
Domaini389 – 44355FF 1Add
BLAST
Domaini456 – 51055FF 2Add
BLAST
Domaini523 – 58361FF 3Add
BLAST
Domaini603 – 66361FF 4Add
BLAST
Domaini668 – 72356FF 5Add
BLAST
Domaini738 – 79558FF 6Add
BLAST

Domaini

The WW domains are essential for localization to nuclear speckles.

Sequence similaritiesi

Belongs to the PRPF40 family.
Contains 6 FF domains.
Contains 2 WW domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5104.
GeneTreeiENSGT00740000115182.
HOGENOMiHOG000231802.
HOVERGENiHBG059634.
InParanoidiQ9R1C7.
KOiK12821.
OMAiERGGLMM.
OrthoDBiEOG77Q4X2.
PhylomeDBiQ9R1C7.
TreeFamiTF318732.

Family and domain databases

Gene3Di1.10.10.440. 4 hits.
InterProiIPR002713. FF_domain.
IPR001202. WW_dom.
[Graphical view]
PfamiPF01846. FF. 5 hits.
PF00397. WW. 2 hits.
[Graphical view]
SMARTiSM00441. FF. 5 hits.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
SSF81698. SSF81698. 5 hits.
PROSITEiPS51676. FF. 6 hits.
PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9R1C7-1) [UniParc]FASTAAdd to Basket

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

MRPGTGAERG GLMVSEMESQ PPSRGPGDGE RRLSGSNLCS SSWVSADGFL    50
RRRPSMGHPG MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM 100
PGMMSSVMSG MMMSHMSQAS MQPALPPGVN SMDVAAGAAS GAKSMWTEHK 150
SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ LLSKCPWKEY KSDSGKPYYY 200
NSQTKESRWA KPKELEDLEG YQNTIVAGGL ITKSNLHAMI KAEESSKQEE 250
CTTASTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA ANANTSTTPT 300
NTVGSVPVAP EPEVTSIVAT AVDNENTVTV STEEQAQLAN TTAIQDLSGD 350
ISSNTGEEPA KQETVSDFTP KKEEEESQPA KKTYTWNTKE EAKQAFKELL 400
KEKRVPSNAS WEQAMKMIIN DPRYSALAKL SEKKQAFNAY KVQTEKEEKE 450
EARSKYKEAK ESFQRFLENH EKMTSTTRYK KAEQMFGEME VWNAISERDR 500
LEIYEDVLFF LSKKEKEQAK QLRKRNWEAL KNILDNMANV TYSTTWSEAQ 550
QYLMDNPTFA EDEELQNMDK EDALICFEEH IRALEKEEEE EKQKTLLRER 600
RRQRKNRESF QIFLDELHEH GQLHSMSSWM ELYPTISSDI RFTNMLGQPG 650
STALDLFKFY VEDLKARYHD EKKIIKDILK DKGFVVEVNT TFEDFVAIIS 700
STKRSTTLDA GNIKLAFNSL LEKAEARERE REKEEARKMK RKESAFKSML 750
KQATPPIELD AVWEDIRERF VKEPAFEDIT LESERKRIFK DFMHVLEHEC 800
QHHHSKNKKH SKKSKKHHRK RSRSRSGSES DDDDSHSKKK RQRSESHSAS 850
ERSSSAESER SYKKSKKHKK KSKKRRHKSD SPESDTEREK DKKEKDRDSE 900
KDRSRQRSES KHKSPKKKTG KDSGNWDTSG SELSEGELEK RRRTLLEQLD 950
DDQ 953
Length:953
Mass (Da):108,481
Last modified:May 1, 2000 - v1
Checksum:i3C627AB7404D2285
GO
Isoform 2 (identifier: Q9R1C7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     14-55: Missing.

Note: No experimental confirmation available.

Show »
Length:911
Mass (Da):103,963
Checksum:i7BE2E454CC5365CA
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei14 – 5542Missing in isoform 2. VSP_008049Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti334 – 3341E → A in BAC40061. 1 Publication
Sequence conflicti355 – 3551T → I in BAC40061. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135439 mRNA. Translation: AAD39463.1.
AK041205 mRNA. Translation: BAC30863.1.
AK051375 mRNA. Translation: BAC34617.1.
AK087963 mRNA. Translation: BAC40061.2.
U40747 mRNA. Translation: AAC52475.1.
CCDSiCCDS16038.1. [Q9R1C7-1]
PIRiS64713.
RefSeqiNP_061255.1. NM_018785.2. [Q9R1C7-1]
UniGeneiMm.257474.
Mm.392945.
Mm.393219.

Genome annotation databases

EnsembliENSMUST00000076313; ENSMUSP00000075655; ENSMUSG00000061136. [Q9R1C7-1]
GeneIDi56194.
KEGGimmu:56194.
UCSCiuc008jrk.2. mouse. [Q9R1C7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135439 mRNA. Translation: AAD39463.1 .
AK041205 mRNA. Translation: BAC30863.1 .
AK051375 mRNA. Translation: BAC34617.1 .
AK087963 mRNA. Translation: BAC40061.2 .
U40747 mRNA. Translation: AAC52475.1 .
CCDSi CCDS16038.1. [Q9R1C7-1 ]
PIRi S64713.
RefSeqi NP_061255.1. NM_018785.2. [Q9R1C7-1 ]
UniGenei Mm.257474.
Mm.392945.
Mm.393219.

3D structure databases

ProteinModelPortali Q9R1C7.
SMRi Q9R1C7. Positions 133-222, 378-446, 739-802.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207833. 5 interactions.
IntActi Q9R1C7. 4 interactions.
MINTi MINT-1525232.
STRINGi 10090.ENSMUSP00000075655.

PTM databases

PhosphoSitei Q9R1C7.

Proteomic databases

MaxQBi Q9R1C7.
PaxDbi Q9R1C7.
PRIDEi Q9R1C7.

Protocols and materials databases

DNASUi 56194.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000076313 ; ENSMUSP00000075655 ; ENSMUSG00000061136 . [Q9R1C7-1 ]
GeneIDi 56194.
KEGGi mmu:56194.
UCSCi uc008jrk.2. mouse. [Q9R1C7-1 ]

Organism-specific databases

CTDi 55660.
MGIi MGI:1860512. Prpf40a.

Phylogenomic databases

eggNOGi COG5104.
GeneTreei ENSGT00740000115182.
HOGENOMi HOG000231802.
HOVERGENi HBG059634.
InParanoidi Q9R1C7.
KOi K12821.
OMAi ERGGLMM.
OrthoDBi EOG77Q4X2.
PhylomeDBi Q9R1C7.
TreeFami TF318732.

Miscellaneous databases

NextBioi 312006.
PROi Q9R1C7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9R1C7.
Bgeei Q9R1C7.
Genevestigatori Q9R1C7.

Family and domain databases

Gene3Di 1.10.10.440. 4 hits.
InterProi IPR002713. FF_domain.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF01846. FF. 5 hits.
PF00397. WW. 2 hits.
[Graphical view ]
SMARTi SM00441. FF. 5 hits.
SM00456. WW. 2 hits.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 2 hits.
SSF81698. SSF81698. 5 hits.
PROSITEi PS51676. FF. 6 hits.
PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "FBP11, a mammalian ortholog of the essential yeast splicing factor PRP40."
    Bedford M.T., Das R., Reed R., Leder P.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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.
    , 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 1-380 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-953.
    Strain: C57BL/6J and NOD.
    Tissue: Aorta, Embryonic spinal ganglion, Thymus and Vein.
  3. "Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains."
    Chan D.C., Bedford M.T., Leder P.
    EMBO J. 15:1045-1054(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 146-212, INTERACTION WITH FORMIN.
    Strain: FVB.
  4. "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands."
    Bedford M.T., Chan D.C., Leder P.
    EMBO J. 16:2376-2383(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SF1; SRPK1; CARD8; ATBF1 AND MECP2.
  5. "FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-dependent microspike formation."
    Mizutani K., Suetsugu S., Takenawa T.
    Biochem. Biophys. Res. Commun. 313:468-474(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASL.
  6. "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: implications for nuclear toxicity in Huntington's disease pathogenesis."
    Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.
    NeuroMolecular Med. 7:297-310(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP8L, SUBCELLULAR LOCATION.
  7. "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 THR-928; SER-929; SER-931 AND SER-934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPR40A_MOUSE
AccessioniPrimary (citable) accession number: Q9R1C7
Secondary accession number(s): Q61049
, Q8BQ76, Q8BRW4, Q8C2U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 121 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

External Data

Dasty 3

Similar proteinsi