Q9UTH0

PR
Gene name
nup132 (nup133b, SPAC1805.04)
Protein name
Nucleoporin nup132
Names
Nuclear pore protein nup132
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPAC1805.04
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-55 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9UTH0

Entry ID Method Resolution Chain Position Source
AF-Q9UTH0-F1 Predicted AlphaFoldDB

18 variants for Q9UTH0

Variant ID(s) Position Change Description Diseaes Association Provenance
I_2777418_T_A 16 F>L No Jeffares_SNPs
I_2777721_C_T 96 A>V No Jeffares_SNPs
I_2777771_T_A,C 113 F>I No Jeffares_SNPs
I_2777771_T_A,C 113 F>L No Jeffares_SNPs
I_2778414_G_A 327 R>H No Jeffares_SNPs
I_2778425_A_G 331 I>V No Jeffares_SNPs
I_2778594_A_G 387 D>G No Jeffares_SNPs
I_2778926_C_T 498 L>F No Jeffares_SNPs
I_2778957_C_A 508 T>N No Jeffares_SNPs
I_2779064_C_T 544 R>C No Jeffares_SNPs
I_2779113_T_C 560 V>A No Jeffares_SNPs
I_2780022_A_G 863 Y>C No Jeffares_SNPs
I_2780066_G_A 878 D>N No Jeffares_SNPs
I_2780245_G_T 937 M>I No Jeffares_SNPs
I_2780474_G_C 1014 E>Q No Jeffares_SNPs
I_2780597_A_G 1055 I>V No Jeffares_SNPs
I_2780759_G_A 1109 D>N No Jeffares_SNPs
I_2780765_C_G 1111 Q>E No Jeffares_SNPs

No associated diseases with Q9UTH0

2 regional properties for Q9UTH0

Type Name Position InterPro Accession
domain Nucleoporin, Nup133/Nup155-like, C-terminal 515 - 1085 IPR007187
domain Nucleoporin, Nup133/Nup155-like, N-terminal 51 - 440 IPR014908

Functions

Description
EC Number
Subcellular Localization
  • Nucleus envelope
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
mitotic nuclear bridge midzone membrane domain A nuclear membrane part at the midzone of the mitotic nuclear bridge. The midzone forms a bulge that is enriched in nuclear pores that lack baskets.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
nuclear periphery The portion of the nuclear lumen proximal to the inner nuclear membrane.
nuclear pore A protein complex providing a discrete opening in the nuclear envelope of a eukaryotic cell, where the inner and outer nuclear membranes are joined.
nuclear pore outer ring A subcomplex of the nuclear pore complex (NPC) that forms the outer rings of the core scaffold, a lattice-like structure that gives the NPC its shape and strength. In S. cerevisiae, the two outer rings each contain multiple copies of the following proteins: Nup133p, Nup120p, Nup145Cp, Nup85p, Nup84p, Seh1p, and Sec13p. In vertebrates, the two outer rings each contain multiple copies of the following proteins: Nup133, Nup160, Nup96, Nup75, Nup107, Seh1, Sec13, Nup43, Nup37, and ALADIN. Components are arranged in 8-fold symmetrical 'spokes' around the central transport channel. A single 'spoke', can be isolated and is sometimes referred to as the Nup84 complex (S. cerevisiae) or the Nup107-160 complex (vertebrates).
nucleolar ring Ring-like structures located at the nucleolar periphery where several nuclear factors are reversibly aggregated and sequestered during acute heat stress.

1 GO annotations of molecular function

Name Definition
structural constituent of nuclear pore The action of a molecule that contributes to the structural integrity of the nuclear pore complex, a protein-lined channel in the nuclear envelope that allows the transfer of macromolecules.

6 GO annotations of biological process

Name Definition
mitotic recombination-dependent replication fork processing Replication fork processing that includes recombination between DNA near the arrested fork and homologous sequences. Proteins involved in homologous recombination are required for replication restart.
poly(A)+ mRNA export from nucleus The directed movement of poly(A)+ mRNA out of the nucleus into the cytoplasm.
protein import into nucleus The directed movement of a protein from the cytoplasm to the nucleus.
regulation of kinetochore assembly Any process that modulates the rate, frequency, or extent of kinetochore assembly, the aggregation, arrangement and bonding together of a set of components to form the kinetochore, a multisubunit complex that is located at the centromeric region of DNA and provides an attachment point for the spindle microtubules.
replication fork processing The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery The chromosome organization process in which the DNA sequence containing a gene transcribed by RNA polymerase II is maintained in a specific location at the nuclear periphery. In S. cerevisiae, this process involves cis-acting DNA sequences such as the TATA box and upstream activating sequence (UAS) elements, trans-acting transcriptional activators, and also the 3'-UTR of the transcript.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSSILGKRKN EEVVSFSPLK RISVEKSLLD STAYNNSLDW LRSKNFKVSC LLKHFNSKII
70 80 90 100 110 120
NDHPLSGSCY TDIGYALINS RKACFILSYR QSLGTAEPPT ITFPLPEEDS NGFSGQNALT
130 140 150 160 170 180
AFVPSDASDK EPGLLIVMPI SGRIAYWTSI GNALAQSYIC PQGMESLIKL LPKEKCEHLC
190 200 210 220 230 240
CSNPMKFIIS TNFGRLFSVQ LRDPAGQPDV SVQLFASDIS TFSTILQKMK IFNYPSIHII
250 260 270 280 290 300
ALKSPPLFSP YQHLLYVAEA SGLLEIYDLK LENKLVSGMN LSPIFKQVLR EGCPDASGLE
310 320 330 340 350 360
VLDLTICPTN GNLVSFLVCW KNSINYRYMI ISLDFSDISS PSVMNIHPLY SFSSKSLESS
370 380 390 400 410 420
KLHYSSSGNS LFVVLTDAVI IVHVQEDDKD IVSRTSWEEV IRMNTNVSGG IFMSTCYKYV
430 440 450 460 470 480
LGKYSIPTES CFIATPYSGI AEIEVHSLEH PANNESLVKS KLEEAVFYSF LPGNPIDFSC
490 500 510 520 530 540
NYLRSIKKPE LERIIVDLGM DILNSRSTHL PPLFASLMQH LSCRLNSLNN LVRYIRSMSL
550 560 570 580 590 600
DVDRQVLYKL RVMGEKCNSV RYLWNTIDTE FSTVSHSLIF QRIIYRLTQS ASSDNALREW
610 620 630 640 650 660
FLHNIESIDQ LIAQAHEFCI DSGSRVQELP LEVLDVIMEA NEVILAIQSS ALAYRRESQK
670 680 690 700 710 720
IYKLSIDTFG EEVPWTSTPE TLVLLCRQFE LTRSALVQSH QGTSDVENTF KIKDKGVLRN
730 740 750 760 770 780
VVSNLEVQLV ALTEVCFDAY SERIRWIEQR CGKDASEIQD VKEAFAVNRR FWVQTLSDIG
790 800 810 820 830 840
KGSSAIRIAE KYSDYRSLVE LCYQLYEDNE LTDALNNYLD LFGIKFAFIL YDYFVENGMA
850 860 870 880 890 900
LELLNSDRFN KSYLKQFFKS RDYNQISWMH DMRLGDYDAA SHRLLQLATK QEKLVDKKES
910 920 930 940 950 960
ELSLSKLFLY AVPSNSGNIR DLVLVEQKLE QLHIQKMVSK SVMPVVERLR SQGKKYQLVE
970 980 990 1000 1010 1020
AVVDDLIGAK VAPVIARQVM QRVVKKFIAG QVVEATELLE YLSFSLYRRE DLVEGEVTDY
1030 1040 1050 1060 1070 1080
YLALRLLLTT RLTDDAKRFY ENTIWRRAVL HDNWIQVLDT QGKNDAIIET QFRMSALYRT
1090 1100 1110 1120 1130 1140
LEAVTINGLF HEGLIRPGSL SSCKFEGYDP QNLISIYPPA RFGDVTEVTK VLNRESVKLD
1150 1160
HYLTKTNLNT CYISMCLSCD TI