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 Q1RMS2

Entry ID Method Resolution Chain Position Source
AF-Q1RMS2-F1 Predicted AlphaFoldDB

91 variants for Q1RMS2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs450295585 15 G>C No EVA
rs454299390 42 Y>D No EVA
rs470314047 57 E>* No EVA
rs436742966 57 E>V No EVA
rs445644517 58 V>G No EVA
rs464201009 63 D>A No EVA
rs434514862 68 D>E No EVA
rs453021097 72 G>V No EVA
rs474844303 74 Y>* No EVA
rs435381031 77 F>I No EVA
rs457184447 80 I>L No EVA
rs475716180 82 L>R No EVA
rs443571882 85 D>Y No EVA
rs458979301 90 T>S No EVA
rs471059318 90 T>S No EVA
rs441342768 93 I>T No EVA
rs459777709 98 I>T No EVA
rs481376515 99 N>K No EVA
rs448605637 102 R>G No EVA
rs463862999 103 R>G No EVA
rs445574457 104 G>C No EVA
rs434474058 105 D>V No EVA
rs468277558 106 Y>F No EVA
rs446508745 106 Y>H No EVA
rs468277558 106 Y>S No EVA
rs435346437 110 T>K No EVA
rs469234336 111 V>E No EVA
rs457151622 111 V>L No EVA
rs433108783 112 Q>K No EVA
rs461776631 116 H>P No EVA
rs449009864 151 I>M No EVA
rs461050331 152 G>V No EVA
rs482752614 153 D>A No EVA
rs450856091 153 D>E No EVA
rs482752614 153 D>V No EVA
rs469400241 155 E>K No EVA
rs478350449 156 G>E No EVA
rs467077310 157 M>R No EVA
rs467077310 157 M>T No EVA
rs455951134 159 F>L No EVA
rs468048744 161 E>V No EVA
rs438322777 162 A>E No EVA
rs471324166 164 R>S No EVA
rs438393743 165 Q>P No EVA
rs453644457 166 F>I No EVA
rs472123925 167 Q>P No EVA
rs461017271 168 F>S No EVA
rs442553691 168 F>V No EVA
rs482960251 172 R>* No EVA
rs443545395 173 E>D No EVA
rs458852549 180 V>F No EVA
rs454574463 192 Q>H No EVA
rs443424017 195 K>N No EVA
rs438803632 209 L>R No EVA
rs442823634 232 M>R No EVA
rs433112979 243 C>F No EVA
rs445999532 260 Q>H No EVA
rs464442463 263 I>F No EVA
rs434752238 274 I>S No EVA
rs453247407 279 S>C No EVA
rs475127900 280 S>R No EVA
rs435759891 285 W>C No EVA
rs457497849 286 R>S No EVA
rs472162670 300 S>C No EVA
rs471754333 341 D>E No EVA
rs438842374 345 T>I No EVA
rs460610878 346 T>P No EVA
rs479189895 350 D>A No EVA
rs449383916 358 W>L No EVA
rs461600702 361 L>I No EVA
rs483268127 365 D>G No EVA
rs437305200 367 V>D No EVA
rs438617164 431 P>R No EVA
rs474057382 432 V>M No EVA
rs467215754 442 G>S No EVA
rs440760420 476 E>G No EVA
rs459456046 480 H>P No EVA
rs473175976 515 A>V No EVA
rs456351057 518 P>R No EVA
rs439554107 519 Y>S No EVA
rs458243248 521 V>F No EVA
rs479865630 531 S>P No EVA
rs440540510 535 K>R No EVA
rs462384488 546 A>G No EVA
rs451211932 555 L>H No EVA
rs480800639 555 L>I No EVA
rs469630514 558 G>V No EVA
rs477856430 564 S>T No EVA
rs456596517 574 S>I No EVA
rs465437181 577 E>G No EVA
rs465437181 577 E>V No EVA

No associated diseases with Q1RMS2

3 regional properties for Q1RMS2

Type Name Position InterPro Accession
domain CTP synthase, N-terminal 2 - 272 IPR017456
domain Glutamine amidotransferase 310 - 543 IPR017926
domain CTP synthase GATase domain 299 - 544 IPR033828

Functions

Description
EC Number 6.3.4.2 Other carbon--nitrogen ligases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoophidium A subcellular filamentary structure where CTP synthase is compartmentalized in a range of organisms including bacteria, yeast, fruit fly, rat and human.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
CTP synthase activity Catalysis of the reaction: ATP + UTP + glutamine + H20= ADP + phosphate + CTP + glutamate.
identical protein binding Binding to an identical protein or proteins.

4 GO annotations of biological process

Name Definition
'de novo' CTP biosynthetic process The chemical reactions and pathways resulting in the formation of cytidine 5'-triphosphate (CTP) from simpler components.
CTP biosynthetic process The chemical reactions and pathways resulting in the formation of CTP, cytidine 5'-triphosphate.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
pyrimidine nucleobase biosynthetic process The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5F3Z1 CTPS2 CTP synthase 2 Gallus gallus (Chicken) PR
P17812 CTPS1 CTP synthase 1 Homo sapiens (Human) PR
Q9NRF8 CTPS2 CTP synthase 2 Homo sapiens (Human) PR
P70698 Ctps1 CTP synthase 1 Mus musculus (Mouse) PR
P70303 Ctps2 CTP synthase 2 Mus musculus (Mouse) PR
Q5U2N0 Ctps2 CTP synthase 2 Rattus norvegicus (Rat) PR
Q6PEI7 ctps1 CTP synthase 1 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
70 80 90 100 110 120
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA
130 140 150 160 170 180
VQEWVMNQAM VPVDGHKEEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV
190 200 210 220 230 240
SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
250 260 270 280 290 300
VICIHDVSST YRVPVLLEEQ GIIKYFKERL DLPIGDSASS LLSKWRNMAD RYERLQKTCS
310 320 330 340 350 360
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEQTTEVED PVKFHEAWQK
370 380 390 400 410 420
LCKADGVLVP GGFGIRGTLG KLQAISWARS RKIPFLGVCL GMQLAVIEFA RNCLNLKDAD
430 440 450 460 470 480
STEFEPNARV PVVIDMPEHN PGNLGGTMRL GIRRTVFKTE NSILRKLYGD VPFIEERHRH
490 500 510 520 530 540
RYEVNPSLIS QLEQKDLSFV GQDVDGERME IIELANHPYF VGVQFHPEFS SRPMKPSPPY
550 560 570 580
LGLLLAATGN LNAYLLQGCK LSSSDRYSDA SDDSFSEPRL AELEIS