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 Q91ZJ5

Entry ID Method Resolution Chain Position Source
AF-Q91ZJ5-F1 Predicted AlphaFoldDB

27 variants for Q91ZJ5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389147717 47 E>D No EVA
rs3389150955 72 S>Y No EVA
rs3389146334 99 D>E No EVA
rs3389139286 112 K>I No EVA
rs3389145161 162 M>I No EVA
rs3389144105 188 F>S No EVA
rs3389084167 196 I>T No EVA
rs3389145170 205 A>V No EVA
rs3389109561 206 K>N No EVA
rs3389147648 206 K>T No EVA
rs3389139212 223 H>L No EVA
rs3389143873 225 D>E No EVA
rs3389145198 263 I>F No EVA
rs3389117284 276 C>Y No EVA
rs3389144100 286 T>A No EVA
rs3389109569 297 Q>H No EVA
rs3389143855 300 G>C No EVA
rs3389143888 331 N>K No EVA
rs3389147670 336 L>H No EVA
rs3401823029 342 L>F No EVA
rs3402003903 349 D>H No EVA
rs3389156799 362 G>S No EVA
rs3389121820 376 I>F No EVA
rs3389146323 423 E>D No EVA
rs3389109573 436 F>L No EVA
rs3401333274 438 K>Q No EVA
rs3389147694 463 D>Y No EVA

No associated diseases with Q91ZJ5

No regional properties for Q91ZJ5

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q91ZJ5

Functions

Description
EC Number 2.7.7.9 Nucleotidyltransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 GO annotations of molecular function

Name Definition
glucose binding Binding to D- or L-enantiomers of glucose.
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
pyrimidine ribonucleotide binding Binding to a pyrimidine ribonucleotide, any compound consisting of a pyrimidine ribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
UTP:glucose-1-phosphate uridylyltransferase activity Catalysis of the reaction: alpha-D-glucose 1-phosphate + UTP = diphosphate + UDP-D-glucose.

5 GO annotations of biological process

Name Definition
brain development The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.).
glucose 1-phosphate metabolic process The chemical reactions and pathways involving glucose 1-phosphate, a monophosphorylated derivative of glucose with the phosphate group attached to C-1.
glycogen biosynthetic process The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
glycogen metabolic process The chemical reactions and pathways involving glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues in alpha-(1->4) glycosidic linkage, joined together by alpha-(1->6) glycosidic linkages.
UDP-glucose metabolic process The chemical reactions and pathways involving UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32861 UGP1 UTP--glucose-1-phosphate uridylyltransferase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q07130 UGP2 UTP--glucose-1-phosphate uridylyltransferase Bos taurus (Bovine) PR
Q16851 UGP2 UTP--glucose-1-phosphate uridylyltransferase Homo sapiens (Human) PR
10 20 30 40 50 60
MSRFVQDLSK AMSQDGASQF QEVILQELEL SVKKELEKIL TTAASHEFEH TKKDLDGFRK
70 80 90 100 110 120
LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS
130 140 150 160 170 180
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYNTDVPLV LMNSFNTDED TKKILQKYNH
190 200 210 220 230 240
CRVKIYTFNQ SRYPRINKES LLPIAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI
250 260 270 280 290 300
EEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG
310 320 330 340 350 360
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLGAVK RLQEQNAIDM EIIVNPKTLD
370 380 390 400 410 420
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE
430 440 450 460 470 480
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA
490 500
NHGDRIDIPP GAVLENKIVS GNLRILDH