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

1 structures for O35218

Entry ID Method Resolution Chain Position Source
AF-O35218-F1 Predicted AlphaFoldDB

32 variants for O35218

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389258531 28 F>C No EVA
rs3389187287 69 G>V No EVA
rs3389254106 89 P>L No EVA
rs3389215709 93 M>L No EVA
rs3389228530 113 L>F No EVA
rs3389256722 120 D>E No EVA
rs3389256645 158 T>S No EVA
rs3389252001 207 Y>H No EVA
rs3389254381 220 L>P No EVA
rs3389266200 221 T>R No EVA
rs3389263476 233 V>M No EVA
rs3389258465 235 I>V No EVA
rs3389266260 250 L>M No EVA
rs3389254392 251 D>N No EVA
rs3389258504 299 R>G No EVA
rs3389271369 334 E>D No EVA
rs3389258511 350 K>* No EVA
rs3389254031 358 R>K No EVA
rs3389271318 399 E>* No EVA
rs3389256647 403 K>R No EVA
rs3389266234 601 S>G No EVA
rs3389215669 606 Y>F No EVA
rs3389258520 614 L>F No EVA
rs3389257253 646 V>A No EVA
rs3403655571 675 Q>L No EVA
rs3403564846 676 Q>L No EVA
rs3389266204 688 K>N No EVA
rs3389258505 694 T>I No EVA
rs3389271312 728 L>P No EVA
rs3389257208 739 G>W No EVA
rs3389215694 774 L>P No EVA
rs3389258502 779 Y>F No EVA

No associated diseases with O35218

5 regional properties for O35218

Type Name Position InterPro Accession
domain Metallo-beta-lactamase 22 - 198 IPR001279
domain Zn-dependent metallo-hydrolase, RNA specificity domain 529 - 591 IPR011108
domain Beta-Casp domain 243 - 368 IPR022712
domain Cleavage and polyadenylation specificity factor 2, C-terminal 608 - 779 IPR025069
domain CPSF2, metallo-hydrolase domain 7 - 204 IPR035639

Functions

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

1 GO annotations of cellular component

Name Definition
mRNA cleavage and polyadenylation specificity factor complex A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.

1 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.

3 GO annotations of biological process

Name Definition
mRNA 3'-end processing by stem-loop binding and cleavage Any mRNA 3'-end processing that involves the binding to and cleavage of a stem-loop structure. For example, histone mRNAs contain a highly conserved stem-loop sequence at the 3' end of the mRNA with a 6 base pairs (bp) stem and a 4-nt loop. The mRNA is cleaved between these two elements, after the fourth or fifth nucleotide, which is typically an adenosine.
mRNA polyadenylation The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.
pre-mRNA cleavage required for polyadenylation The targeted, endonucleolytic cleavage of a pre-mRNA, required for polyadenylation of the 3' end. This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12102 CFT2 Cleavage factor two protein 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9V3D6 Cpsf100 Probable cleavage and polyadenylation specificity factor subunit 2 Drosophila melanogaster (Fruit fly) PR
Q9P2I0 CPSF2 Cleavage and polyadenylation specificity factor subunit 2 Homo sapiens (Human) PR
O17403 cpsf-2 Probable cleavage and polyadenylation specificity factor subunit 2 Caenorhabditis elegans PR
10 20 30 40 50 60
MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SVDIIDSLRK HVHQIDAVLL
70 80 90 100 110 120
SHPDPLHLGA LPFAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD
130 140 150 160 170 180
AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR
190 200 210 220 230 240
EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA
250 260 270 280 290 300
GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
310 320 330 340 350 360
NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT
370 380 390 400 410 420
PGTLARFLID NPTEKVTEIE LRKRVKLEGK ELEEYVEKEK LKKEAAKKLE QSKEADIDSS
430 440 450 460 470 480
DESDVEEDVD QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII
490 500 510 520 530 540
KPEDFLVPEL QATEEEKSKL ESGLTNGEEP MDQDLSDVPT KCVSATESIE IKARVTYIDY
550 560 570 580 590 600
EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT
610 620 630 640 650 660
SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS
670 680 690 700 710 720
EMQVDAPSDS SAMAQQKAMK SLFGEDEKEL GEETEIIPTL EPLPPHEVPG HQSVFMNEPR
730 740 750 760 770 780
LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA
IV