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

3 structures for P70303

Entry ID Method Resolution Chain Position Source
7MIU EM 260 A C/D/G/H 1-586 PDB
7MIV EM 280 A C/D/G/H 1-586 PDB
AF-P70303-F1 Predicted AlphaFoldDB

35 variants for P70303

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3412450990 65 G>E No EVA
rs3389582180 85 D>G No EVA
rs3389593217 109 K>I No EVA
rs3389585981 120 A>T No EVA
rs31369473 172 K>R No EVA
rs3412451015 180 V>GLLTWR* No EVA
rs3389560979 193 K>T No EVA
rs3412562962 223 E>V No EVA
rs3412137722 231 S>P No EVA
rs3412448564 247 V>D No EVA
rs3412653141 264 K>* No EVA
rs245842496 267 Q>R No EVA
rs3389560918 318 F>L No EVA
rs3389582664 320 A>S No EVA
rs3389560923 346 T>I No EVA
rs3412734883 388 A>V No EVA
rs31367730 393 I>T No EVA
rs3389593151 402 M>K No EVA
rs3412448540 404 L>Q No EVA
rs3412653258 409 F>L No EVA
rs3411265512 411 R>N* No EVA
rs3412358261 411 R>T No EVA
rs3412451089 415 N>K No EVA
rs3411265475 417 K>Q No EVA
rs3389575575 424 F>I No EVA
rs3389582128 427 N>D No EVA
rs3389533402 446 G>E No EVA
rs3389580791 475 E>* No EVA
rs3389491380 478 H>Q No EVA
rs3389550546 499 F>I No EVA
rs3389550556 506 G>V No EVA
rs3411267080 532 R>M No EVA
rs3389582242 532 R>S No EVA
rs3389574936 574 S>R No EVA
rs3389591563 576 P>Q No EVA

No associated diseases with P70303

3 regional properties for P70303

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

3 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.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

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
Q1RMS2 CTPS2 CTP synthase 2 Bos taurus (Bovine) PR
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
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
IQEWVMNQAK VSVDGNKEDP QICVIELGGT IGDIEGMAFV EAFRQFQFKA KKENFYNIHV
190 200 210 220 230 240
SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
250 260 270 280 290 300
VICIHDVSSI YRVPLLLEEQ GVVKYFQERL GLPINDCSSN LLFKWKAMAD RYERLQKICS
310 320 330 340 350 360
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEPVTKAED PVKFHEAWQK
370 380 390 400 410 420
LCLADGILVP GGFGIRGTLG KLQAISWART KKIPFLGICL GMQLAVIEFA RNCLNLKDAN
430 440 450 460 470 480
STEFEPNTPV PLVIDMPEHN PGDLGGTMRL GLRRTVFTTE NSILKKLYGD VPYIEERHRH
490 500 510 520 530 540
RYEVNPNLIN QFENKDLCFV GEDVDGKRME IVELTSHPYF IGVQFHPEFS SRPMKPSPPY
550 560 570 580
LGLLLAATGN LNAHLQQMNK LPYSDGYSDA SDDSFPEAKL AELDLN