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

2 structures for Q12216

Entry ID Method Resolution Chain Position Source
6U75 X-ray 263 A A/B 154-420 PDB
AF-Q12216-F1 Predicted AlphaFoldDB

13 variants for Q12216

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-630474 23 N>S No SGRP
s15-629974 190 S>P No SGRP
s15-629804 246 K>N No SGRP
s15-629805 246 K>R No SGRP
s15-629511 344 R>K No SGRP
s15-629359 395 V>L No SGRP
s15-629133 470 P>L No SGRP
s15-629094 483 F>Y No SGRP
s15-629046 499 D>G No SGRP
s15-628690 618 L>F No SGRP
s15-628573 657 V>L No SGRP
s15-628540 668 I>V No SGRP
s15-628417 709 D>N No SGRP

No associated diseases with Q12216

4 regional properties for Q12216

Type Name Position InterPro Accession
domain SAP domain 43 - 77 IPR003034
domain Zinc finger, MIZ-type 323 - 408 IPR004181
domain PINIT domain 139 - 291 IPR023321
domain E3 SUMO-protein ligase SIZ1/2, SP-RING finger 331 - 386 IPR031141

Functions

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

3 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.

3 GO annotations of molecular function

Name Definition
double-stranded DNA binding Binding to double-stranded DNA.
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).

3 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.
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
Q04195 SIZ1 E3 SUMO-protein ligase SIZ1 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
MASVMSNNNN NNNNNNASYM FTNPLSNTGG GLINEIKDAI NEMEQLKVLE LKQICKSLDL
70 80 90 100 110 120
SITGKKAVLQ DRIKQFLRKS CDIGHIDPWR PKAIKILIAK VRINSSLPKY STLWETLKTG
130 140 150 160 170 180
AFKHPVASGQ LPVTALQSTA LPPYSQQQAL AYSFTSPFYK PIVQIPDANK KLKQSAGRGC
190 200 210 220 230 240
TKMKFKVSKS NHDLLKSNKS YKLYLFSGFS IPFIYETVGH EAIDFPYPCE LVFNGTKLED
250 260 270 280 290 300
NVKGLKKQNG TGNPANLTPY LKVPTEMNHL DLHYLNIDKE YSISCFIVEV FSPEALLGKI
310 320 330 340 350 360
LKRPKIIKQA TTAYIKRTLN EQDDDDIITT STVLSLQCPI SCTRMKYPAK TDQCKHIQCF
370 380 390 400 410 420
DALWFLHSQS QVPTWQCPIC QHPIKFDQLK ISEFVDNIIQ NCNEDVEQVE ISVDGSWKPI
430 440 450 460 470 480
HNSSAVITDT VNQNHSVKNE NQGTVKQEQD YDSRNAFDTN LRNGSNHNEP EIISLDSSDD
490 500 510 520 530 540
EAFIPASKSF PTHVNPRNDQ LRADIFPSES EGSSDYNPNH TSTPKGSPTM DQDNYQDAFQ
550 560 570 580 590 600
MRSFLNQGAT TNINDTPTNN SSINSFVTAT NGDSRIFYNR GPSTPLLPAV LQNLTNQTEA
610 620 630 640 650 660
QRNPYGPNYN TTAQDRNLLG IEGDLPPIPP VDPNSEAETE LPTRTTSAAH LPPYIHVSTS
670 680 690 700 710 720
GHGDDGKIRK RRHSNVSIYI PKNPYATLMK RRPQANHAIM NKTLAQTNDF NTSAQDNSEV
VDLTSD