NU107_RAT
ID NU107_RAT Reviewed; 926 AA.
AC P52590;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nuclear pore complex protein Nup107;
DE AltName: Full=107 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup107;
DE AltName: Full=p105;
GN Name=Nup107;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Buffalo; TISSUE=Liver;
RX PubMed=8021268; DOI=10.1016/s0021-9258(17)32483-3;
RA Radu A., Blobel G., Wozniak R.W.;
RT "Nup107 is a novel nuclear pore complex protein that contains a leucine
RT zipper.";
RL J. Biol. Chem. 269:17600-17605(1994).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance. Required for the assembly of peripheral proteins
CC into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis.
CC {ECO:0000250|UniProtKB:P57740}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). Forms part of the
CC Nup160 subcomplex in the nuclear pore which is composed of NUP160,
CC NUP133, NUP107 and Nup96; this complex plays a role in RNA export and
CC in tethering Nup98 and NUP153 to the nucleus. Does not interact with
CC TPR. Interacts with ZNF106. {ECO:0000250|UniProtKB:P57740,
CC ECO:0000250|UniProtKB:Q8BH74}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P57740}.
CC Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P57740}.
CC Note=Located on both the cytoplasmic and nuclear sides of the NPC core
CC structure. During mitosis, localizes to the kinetochores. Dissociates
CC from the dissasembled NPC structure late during prophase of mitosis.
CC {ECO:0000250|UniProtKB:P57740}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup84/Nup107 family.
CC {ECO:0000305}.
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DR EMBL; L31840; AAA74476.1; -; mRNA.
DR PIR; A54142; A54142.
DR AlphaFoldDB; P52590; -.
DR SMR; P52590; -.
DR CORUM; P52590; -.
DR STRING; 10116.ENSRNOP00000009203; -.
DR iPTMnet; P52590; -.
DR jPOST; P52590; -.
DR PaxDb; P52590; -.
DR PeptideAtlas; P52590; -.
DR RGD; 621160; Nup107.
DR eggNOG; KOG1964; Eukaryota.
DR InParanoid; P52590; -.
DR PhylomeDB; P52590; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:P52590; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0008585; P:female gonad development; ISO:RGD.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0072006; P:nephron development; ISS:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR007252; Nup84/Nup107.
DR PANTHER; PTHR13003; PTHR13003; 1.
DR Pfam; PF04121; Nup84_Nup100; 1.
PE 1: Evidence at protein level;
KW Acetylation; Centromere; Chromosome; Direct protein sequencing;
KW Kinetochore; Membrane; Methylation; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..926
FT /note="Nuclear pore complex protein Nup107"
FT /id="PRO_0000204833"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 60
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BH74"
FT MOD_RES 60
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 68
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH74"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
SQ SEQUENCE 926 AA; 107209 MW; FB80A42C60F4F3B6 CRC64;
MDRSGFGGMS SPVIRDPEVT RTARKHSAHK RVLIQANQDE NFGTTTPRSQ IIPRTPSSFR
QPFTPPSRSL LRHPDISYIF GTEGRSPRHI QSSGYLGNLS MVTNLDDSNW AAAFSSQRLG
FYTNTEHHSM TEDINLSTVM LREDDPGEAA SMSMFSDFLQ SFLKHSSTTV FDLVEEYENI
CASQVNILSK IVSRATRWDW QKFSKTASML WLLQQEMVTW RLLASLYRDR IQSSLEEENM
FAIAGINASE KTVVEALFQR DSLVRQSQLV VDWLESIAKD EIGDFSDNIE FYAKSVYWEN
TLHSLKQRQL LSYIGSTRPL VTELDPDAPI RQKMPLDDLD REDEVRLLKY LFTLIRAGMT
EEAQRLCKRC GQAWRAATLE GWKLHHDPNV NGGTELEPVE GNPYRRIWKI SCWRMAEDEL
FNKYERAIYA ALSGNLKQLL PVCDTWEDTV WAYFRVMVDS LVEQEIRTSV MTLDETEELP
REYMEANWTL EKVFEELQAT DKKRVLEENQ EHYHVVQKFL ILGDIDGLMD EFSKWLSKSR
SSLPGHLLRF MTHLILFFRT LGLQTKEEVS IEVLKTYIQL LINEKHTNLI AFYTCHLPQD
LAVAQYALFL EGVTECEQRH QCLELAKEAD LDVATITKTV VENIRKKDNG EFSHHDLAPS
LDTATTEEDR LKIDVIDWLV FDPAQRAEAL RQGNAIMRKF LALKKHEAAK EVFVKIPQDS
IAEIYNQWEE QGMESPLPAE DDNAIREHLC IRAYLEAHET FNERFKHMNS APQKPTLLSQ
ATFTEKVAHE HKEKKYEMDH NIWKGHLDAL TADVKEKMYN VLLFVDGGWM VDVREDAEED
PERAHQMVLL RKLCLPMLCF LLHTILHSTG QYQECLQLAD MVSSERHKLY LVFSKEELRK
LLQKLRESSL MLLDQGLDPL GYEIQS
