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 O42649

Entry ID Method Resolution Chain Position Source
6YUF EM 394 A C 1-1194 PDB
AF-O42649-F1 Predicted AlphaFoldDB

15 variants for O42649

Variant ID(s) Position Change Description Diseaes Association Provenance
I_1224579_G_A 72 T>I No Jeffares_SNPs
I_1224199_G_A 199 R>W No Jeffares_SNPs
I_1224152_G_T 214 H>Q No Jeffares_SNPs
I_1223737_C_T 353 A>T No Jeffares_SNPs
I_1223541_G_T 418 T>N No Jeffares_SNPs
I_1223527_T_A 423 M>L No Jeffares_SNPs
I_1222771_T_C 675 T>A No Jeffares_SNPs
I_1222754_G_T 680 F>L No Jeffares_SNPs
I_1222624_G_A 724 P>S No Jeffares_SNPs
I_1222587_G_A 736 T>I No Jeffares_SNPs
I_1222492_T_C 768 K>E No Jeffares_SNPs
I_1222383_A_C 804 I>S No Jeffares_SNPs
I_1221979_C_T 939 E>K No Jeffares_SNPs
I_1221870_T_A 975 Y>F No Jeffares_SNPs
I_1221630_A_G 1055 I>T No Jeffares_SNPs

No associated diseases with O42649

3 regional properties for O42649

Type Name Position InterPro Accession
domain RecF/RecN/SMC, N-terminal 2 - 1177 IPR003395
domain SMCs flexible hinge 522 - 634 IPR010935
domain Structural maintenance of chromosomes 3, ABC domain, eukaryotic 3 - 166 IPR041741

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Chromosome
  • Associates with chromatin
  • Before prophase it is scattered along chromosome arms
  • At anaphase, the rad21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
cohesin complex A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
condensed chromosome, centromeric region The region of a condensed chromosome that includes the centromere and associated proteins, including the kinetochore. In monocentric chromosomes, this region corresponds to a single area of the chromosome, whereas in holocentric chromosomes, it is evenly distributed along the chromosome.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitotic cohesin complex A cohesin complex that mediates sister chromatid cohesion during mitosis; has a subunit composition distinct from that of the meiotic cohesin complex.
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
cohesin loading activity Facilitating a conformational change to load a cohesin complex around sister chromatids, driven by ATP hydrolysis.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

5 GO annotations of biological process

Name Definition
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
chromatin looping A chromatin organization process that starts with the loading of an extrusion motor (by an SMC family complex) onto the chromatin, followed by chromatin extrusion that stops at loop anchoring sites on the chromosome.
mitotic cohesin loading The protein localization to chromatin by which a cohesin ring complex is topologically linked to DNA as part of the mitotic cell cycle.
mitotic cohesin ssDNA (lagging strand) loading The ATP-dependent protein localization to chromatin by which a cohesin ring complex is topologically linked to ssDNA (lagging strand) which is already linked to a dsDNA (leading strand) molecule as part of the mitotic cell cycle.
mitotic sister chromatid cohesion The cell cycle process in which the sister chromatids of a replicated chromosome are joined along the entire length of the chromosome, from their formation in S phase through metaphase during a mitotic cell cycle. This cohesion cycle is critical for high fidelity chromosome transmission.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MYITKIVIQG FKSYKDYTVI EPLSPHHNVI VGRNGSGKSN FFAAIRFVLS DAYTHLSREE
70 80 90 100 110 120
RQALLHEGPG ATVMSAYVEV TFANADNRFP TGKSEVVLRR TIGLKKDEYS LDKKTVSKTE
130 140 150 160 170 180
VINLLESAGF SRSNPYYIVP QGRVTSLTNA KDSERLELLK EVAGTQIYEN RRAESNKIMD
190 200 210 220 230 240
ETIQKSEKID ELLQYIEERL RELEEEKNDL AVYHKKDNER RCLEYAIYSR EHDEINSVLD
250 260 270 280 290 300
ALEQDRIAAL ERNDDDSGAF IQREERIERI KAEITELNHS LELLRVEKQQ NDEDYTNIMK
310 320 330 340 350 360
SKVALELQSS QLSRQIEFSK KDESSKLNIL SELESKISEK ENELSEILPK YNAIVSEADD
370 380 390 400 410 420
LNKRIMLLKN QKQSLLDKQS RTSQFTTKKE RDEWIRNQLL QINRNINSTK ENSDYLKTEY
430 440 450 460 470 480
DEMENELKAK LSRKKEIEIS LESQGDRMSQ LLANITSINE RKENLTDKRK SLWREEAKLK
490 500 510 520 530 540
SSIENVKDDL SRSEKALGTT MDRNTSNGIR AVKDIAERLK LEGYYGPLCE LFKVDNRFKV
550 560 570 580 590 600
AVEATAGNSL FHIVVDNDET ATQILDVIYK ENAGRVTFMP LNKLRPKAVT YPDASDALPL
610 620 630 640 650 660
IQYLEFDPKF DAAIKQVFSK TIVCPSIETA SQYARSHQLN GITLSGDRSD KKGALTAGYR
670 680 690 700 710 720
DYRNSRLDAI KNVKTYQIKF SDLQESLEKC RSEIESFDQK ITACLDDLQK AQLSLKQFER
730 740 750 760 770 780
DHIPLKDELV TITGETTDLQ ESMHHKSRML ELVVLELHTL EQQANDLKSE LSSEMDELDP
790 800 810 820 830 840
KDVEALKSLS GQIENLSHEF DAIIKERAHI EARKTALEYE LNTNLYLRRN PLKAEIGSDN
850 860 870 880 890 900
RIDESELNSV KRSLLKYENK LQIIKSSSSG LEEQMQRINS EISDKRNELE SLEELQHEVA
910 920 930 940 950 960
TRIEQDAKIN ERNAAKRSLL LARKKECNEK IKSLGVLPEE AFIKYVSTSS NAIVKKLHKI
970 980 990 1000 1010 1020
NEALKDYGSV NKKAYEQFNN FTKQRDSLLA RREELRRSQE SISELTTVLD QRKDEAIERT
1030 1040 1050 1060 1070 1080
FKQVAKSFSE IFVKLVPAGR GELVMNRRSE LSQSIEQDIS MDIDTPSQKS SIDNYTGISI
1090 1100 1110 1120 1130 1140
RVSFNSKDDE QLNINQLSGG QKSLCALTLI FAIQRCDPAP FNILDECDAN LDAQYRSAIA
1150 1160 1170 1180 1190
AMVKEMSKTS QFICTTFRPE MVKVADNFYG VMFNHKVSTV ESISKEEAMA FVEG