Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

4 structures for Q04195

Entry ID Method Resolution Chain Position Source
2RNN NMR - A 1-111 PDB
3I2D X-ray 260 A A 112-465 PDB
5JNE X-ray 285 A A/E 167-449 PDB
AF-Q04195-F1 Predicted AlphaFoldDB

35 variants for Q04195

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-1289482 29 E>K No SGRP
s04-1289806 137 R>G No SGRP
s04-1289877 160 N>K No SGRP
s04-1289948 184 K>R No SGRP
s04-1290065 223 N>T No SGRP
s04-1290391 332 Q>E No SGRP
s04-1290499 368 M>L No SGRP
s04-1290739 448 D>N No SGRP
s04-1290860 488 D>G No SGRP
s04-1290878 494 G>E No SGRP
s04-1290928 511 N>D No SGRP
s04-1291001 535 N>S No SGRP
s04-1291007 537 N>I No SGRP
s04-1291015 540 D>N No SGRP
s04-1291028 544 S>N No SGRP
s04-1291063 556 H>N No SGRP
s04-1291072 559 G>S No SGRP
s04-1291076 560 S>N No SGRP
s04-1291100 568 N>S No SGRP
s04-1291105 570 T>A No SGRP
s04-1291150 585 L>F No SGRP
s04-1291157 587 A>V No SGRP
s04-1291169 591 S>N No SGRP
s04-1291199 601 I>T No SGRP
s04-1291427 677 V>A No SGRP
s04-1291475 693 A>V No SGRP
s04-1291529 711 T>I No SGRP
s04-1291531 712 V>I No SGRP
s04-1291634 746 R>H No SGRP
s04-1291646 750 M>T No SGRP
s04-1291714 773 P>S No SGRP
s04-1291780 795 L>V No SGRP
s04-1291861 822 V>L No SGRP
s04-1291879 828 S>A No SGRP
s04-1292020 875 Q>K No SGRP

No associated diseases with Q04195

4 regional properties for Q04195

Type Name Position InterPro Accession
domain SAP domain 34 - 68 IPR003034
domain Zinc finger, MIZ-type 344 - 431 IPR004181
domain PINIT domain 162 - 314 IPR023321
domain E3 SUMO-protein ligase SIZ1/2, SP-RING finger 354 - 409 IPR031141

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Bud neck
  • Present at the bud neck in early M-phase
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cellular bud neck The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
septin ring A tight ring-shaped structure that forms in the division plane at the site of cytokinesis; composed of members of the conserved family of filament-forming proteins called septins as well as septin-associated proteins. This type of septin structure is observed at the bud neck of budding fungal cells, at the site of cell division in animal cells, at the junction between the mother cell and a pseudohyphal projection, and also within hyphae of filamentous fungi at sites where a septum will form.

2 GO annotations of molecular function

Name Definition
SUMO transferase activity Catalysis of the transfer of SUMO from one protein to another via the reaction X-SUMO + Y --> Y-SUMO + X, where both X-SUMO and Y-SUMO are covalent linkages.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
chromosome segregation The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. In eukaryotes, chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles.
DNA double-strand break attachment to nuclear envelope A process in which the DNA double-strand breaks are attached to the inner surface of the nuclear envelope proximal to the spindle pole body, or iMTOCs.
negative regulation of protein ubiquitination Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
protein sumoylation The process in which a SUMO protein (small ubiquitin-related modifier) is conjugated to a target protein via an isopeptide bond between the carboxy-terminus of SUMO with an epsilon-amino group of a lysine residue of the target protein.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12216 NFI1 E3 SUMO-protein ligase SIZ2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q8N2W9 PIAS4 E3 SUMO-protein ligase PIAS4 Homo sapiens (Human) PR
O75925 PIAS1 E3 SUMO-protein ligase PIAS1 Homo sapiens (Human) PR
10 20 30 40 50 60
MINLEDYWED ETPGPDREPT NELRNEVEET ITLMELLKVS ELKDICRSVS FPVSGRKAVL
70 80 90 100 110 120
QDLIRNFLQN ALVVGKSDPY RVQAVKFLIE RIRKNEPLPV YKDLWNALRK GTPLSAITVR
130 140 150 160 170 180
SMEGPPTVQQ QSPSVIRQSP TQRRKTSTTS STSRAPPPTN PDASSSSSSF AVPTIHFKES
190 200 210 220 230 240
PFYKIQRLIP ELVMNVEVTG GRGMCSAKFK LSKADYNLLS NPNSKHRLYL FSGMINPLGS
250 260 270 280 290 300
RGNEPIQFPF PNELRCNNVQ IKDNIRGFKS KPGTAKPADL TPHLKPYTQQ NNVELIYAFT
310 320 330 340 350 360
TKEYKLFGYI VEMITPEQLL EKVLQHPKII KQATLLYLKK TLREDEEMGL TTTSTIMSLQ
370 380 390 400 410 420
CPISYTRMKY PSKSINCKHL QCFDALWFLH SQLQIPTWQC PVCQIDIALE NLAISEFVDD
430 440 450 460 470 480
ILQNCQKNVE QVELTSDGKW TAILEDDDDS DSDSNDGSRS PEKGTSVSDH HCSSSHPSEP
490 500 510 520 530 540
IIINLDSDDD EPNGNNPHVT NNHDDSNRHS NDNNNNSIKN NDSHNKNNNN NNNNNNNNND
550 560 570 580 590 600
NNNSIENNDS NSNNKHDHGS RSNTPSHNHT KNLMNDNDDD DDDRLMAEIT SNHLKSTNTD
610 620 630 640 650 660
ILTEKGSSAP SRTLDPKSYN IVASETTTPV TNRVIPEYLG NSSSYIGKQL PNILGKTPLN
670 680 690 700 710 720
VTAVDNSSHL ISPDVSVSSP TPRNTASNAS SSALSTPPLI RMSSLDPRGS TVPDKTIRPP
730 740 750 760 770 780
INSNSYTASI SDSFVQPQES SVFPPREQNM DMSFPSTVNS RFNDPRLNTT RFPDSTLRGA
790 800 810 820 830 840
TILSNNGLDQ RNNSLPTTEA ITRNDVGRQN STPVLPTLPQ NVPIRTNSNK SGLPLINNEN
850 860 870 880 890 900
SVPNPPNTAT IPLQKSRLIV NPFIPRRPYS NVLPQKRQLS NTSSTSPIMG TWKTQDYGKK
YNSG