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 P38274

Entry ID Method Resolution Chain Position Source
AF-P38274-F1 Predicted AlphaFoldDB

11 variants for P38274

Variant ID(s) Position Change Description Diseaes Association Provenance
s02-503396 296 S>P No SGRP
s02-503345 313 L>V No SGRP
s02-503304 326 D>E No SGRP
s02-503158 375 A>V No SGRP
s02-502670 538 V>I No SGRP
s02-502621 554 V>A No SGRP
s02-502417 622 E>G No SGRP
s02-502396 629 D>V No SGRP
s02-502286 666 D>N No SGRP
s02-502015 756 D>G No SGRP
s02-501968 772 I>V No SGRP

No associated diseases with P38274

3 regional properties for P38274

Type Name Position InterPro Accession
domain PRMT5 arginine-N-methyltransferase 318 - 493 IPR035075
domain PRMT5, TIM barrel domain 38 - 308 IPR035247
domain PRMT5, oligomerisation domain 496 - 824 IPR035248

Functions

Description
EC Number 2.1.1.320 Methyltransferases
Subcellular Localization
  • Bud neck
  • Associates with the septin ring of the bud neck during cell division
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 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.
cellular bud neck septin collar A tubular structure with flared ends, shaped like an hourglass and composed of highly ordered arrays of septin filaments, that forms at the bud neck of a dividing cell. In S. cerevisiae, this structure is located at the bud neck throughout most of the cell cycle and the septins are fixed within the structure, not exchanging with soluble septins. This septin structure acts as a scaffold for other proteins that function at the bud neck.
cellular bud neck septin ring A ring-shaped structure that forms at the site of cytokinesis in the bud neck of a budding cell; composed of members of the conserved family of filament forming proteins called septins as well as septin-associated proteins. In S. cerevisiae, this structure forms at the time of bud emergence and the septins show a high rate of exchange.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
outer plaque of spindle pole body One of three laminate structures that form the spindle pole body; the outer plaque is in the cytoplasm.

4 GO annotations of molecular function

Name Definition
histone methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue.
histone-arginine N-methyltransferase activity Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
protein-arginine omega-N monomethyltransferase activity Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue. The reaction is S-adenosyl-L-methionine
protein-arginine omega-N symmetric methyltransferase activity +Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the terminal nitrogen (omega nitrogen) residue that is not already methylated, resulting in symmetrical peptidyl-N(omega),N'(omega)-dimethyled arginine residues.

9 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.
cell morphogenesis The developmental process in which the size or shape of a cell is generated and organized.
G2/M transition of mitotic cell cycle The mitotic cell cycle transition by which a cell in G2 commits to M phase. The process begins when the kinase activity of M cyclin/CDK complex reaches a threshold high enough for the cell cycle to proceed. This is accomplished by activating a positive feedback loop that results in the accumulation of unphosphorylated and active M cyclin/CDK complex.
histone arginine methylation The modification of a histone by addition of a methyl group to an arginine residue.
peptidyl-arginine N-methylation The addition of a methyl group onto a nitrogen atom of an arginine residue in a protein.
positive regulation of mitotic nuclear division Any process that activates or increases the frequency, rate or extent of mitosis.
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
regulation of cell cycle Any process that modulates the rate or extent of progression through the cell cycle.
regulation of DNA-templated transcription Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P46580 prmt-5 Protein arginine N-methyltransferase 5 Caenorhabditis elegans PR
10 20 30 40 50 60
MHSNVFVGVK PGFNHKQHSK KSRFLENVSS HSPELPSNYD YVLLPITTPR YKEIVGQVFK
70 80 90 100 110 120
DFQRQSIQNW KPLQIPEPQL QDICIPPFNV KKLDNDDTPS YIGLLSSWLE LESRDPNVRD
130 140 150 160 170 180
LGLKVLLNEC KYARFVGINK LILAPPRDLS NLQLYGQMIY RLLQNRIVFA APALTISISL
190 200 210 220 230 240
PLYEDSDPLA TWELWNTVRK QCEYHPSLTI SLALPRTRTP SYVLNRWLAE PVSCLLVSSS
250 260 270 280 290 300
IFASNQYDYP VLHKFNQNLI LKFQKVNGDS QILGNELCVI LHGMEKYANN VKGGESAYLE
310 320 330 340 350 360
YINYLLKKGD KVLNSNSNHQ FLLQEDSRIM PPLKPHSDNL LNSTYLTFEK DLVKYDLYES
370 380 390 400 410 420
AILEALQDLA PRASAKRPLV ILVAGAGRGP LVDRTFKIIS MLFMDSKVSI IAIEKNPQAY
430 440 450 460 470 480
LYLQKRNFDC WDNRVKLIKE DMTKWQINEP SEKRIQIDLC ISELLGSFGC NELSPECLWS
490 500 510 520 530 540
IEKYHSHNDT IFIPRSYSSY IAPISSPLFY QKLSQTNRSL EAPWIVHRVP YCILSSRVNE
550 560 570 580 590 600
VWRFEHPMAQ KDTVQDEDDF TVEFSQSSLN EFKIKHRGEI HGFIGFFSAN LYNNIFLSTL
610 620 630 640 650 660
PNDSTVRLKF SEETLMNTRR EENLIKKCDH TPNMTSWSPI IFPLKQPISF IDDSELSVLM
670 680 690 700 710 720
SRIHSDTEQK VWYEWSLESF IYLMLSNYTS AVTAASMTIP RSIVTDDTKT LAHNRHYSAT
730 740 750 760 770 780
TNQKLDNQID LDQDIENEEE QGFLSNLETG WQSVQDIHGL SETAKPDHLD SINKPMFDLK
790 800 810 820
STKALEPSNE LPRHEDLEED VPEVHVRVKT SVSTLHNVCG RAFSLPL