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

2 structures for Q5UQC3

Entry ID Method Resolution Chain Position Source
6AX6 X-ray 224 A A/B 680-895 PDB
6AX7 X-ray 200 A A/B 680-895 PDB

No variants for Q5UQC3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5UQC3

No associated diseases with Q5UQC3

2 regional properties for Q5UQC3

Type Name Position InterPro Accession
domain Oxoglutarate/iron-dependent dioxygenase 805 - 895 IPR005123
domain Prolyl 4-hydroxylase, alpha subunit 722 - 895 IPR006620

Functions

Description
EC Number 1.14.11.4 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
iron ion binding Binding to an iron (Fe) ion.
L-ascorbic acid binding Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
procollagen-lysine 5-dioxygenase activity Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
transferase activity Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MISRTYVINL ARRPDKKDRI LAEFLKLKEK GVELNCVIFE AVDGNNPEHL SRFNFKIPNW
70 80 90 100 110 120
TDLNSGKPMT NGEVGCALSH WSVWKDVVDC VENGTLDKDC RILVLEDDVV FLDNFMERYQ
130 140 150 160 170 180
TYTSEITYNC DLLYLHRKPL NPYTETKIST HIVKPNKSYW ACAYVITYQC AKKFMNANYL
190 200 210 220 230 240
ENLIPSDEFI PIMHGCNVYG FEKLFSNCEK IDCYAVQPSL VKLTSNAFND SETFHSGSYV
250 260 270 280 290 300
PSNKFNFDTD KQFRIVYIGP TKGNSFHRFT EYCKLYLLPY KVIDEKETND FVSLRSELQS
310 320 330 340 350 360
LSEQDLNTTL MLVVSVNHND FCNTIPCAPT NEFIDKYKQL TTDTNSIVSA VQNGTNKTMF
370 380 390 400 410 420
IGWANKISEF INHYHQKLTE SNAETDINLA NLLLISSISS DFNCVVEDVE GNLFQLINEE
430 440 450 460 470 480
SDIVFSTTTS RVNNKLGKTP SVLYANSDSS VIVLNKVENY TGYGWNEYYG YHVYPVKFDV
490 500 510 520 530 540
LPKIYLSIRI VKNANVTKIA ETLDYPKELI TVSISRSEHD SFYQADIQKF LLSGADYYFY
550 560 570 580 590 600
ISGDCIITRP TILKELLELN KDFVGPLMRK GTESWTNYWG DIDPSNGYYK RSFDYFDIIG
610 620 630 640 650 660
RDRVGCWNVP YLASVYLIKK SVIEQVPNLF TENSHMWNGS NIDMRLCHNL RKNNVFMYLS
670 680 690 700 710 720
NLRPYGHIDD SINLEVLSGV PTEVTLYDLP TRKEEWEKKY LHPEFLSHLQ NFKDFDYTEI
730 740 750 760 770 780
CNDVYSFPLF TPAFCKEVIE VMDKANLWSK GGDSYFDPRI GGVESYPTQD TQLYEVGLDK
790 800 810 820 830 840
QWHYVVFNYV APFVRHLYNN YKTKDINLAF VVKYDMERQS ELAPHHDSST YTLNIALNEY
850 860 870 880 890
GKEYTAGGCE FIRHKFIWQG QKVGYATIHA GKLLAYHRAL PITSGKRYIL VSFVN