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 Q06625

Entry ID Method Resolution Chain Position Source
AF-Q06625-F1 Predicted AlphaFoldDB

24 variants for Q06625

Variant ID(s) Position Change Description Diseaes Association Provenance
s16-902159 40 D>E No SGRP
s16-902239 67 P>L No SGRP
s16-902264 75 K>N No SGRP
s16-902925 296 V>I No SGRP
s16-903142 368 R>K No SGRP
s16-903229 397 Q>R No SGRP
s16-903411 458 K>Q No SGRP
s16-903688 550 D>G No SGRP
s16-903951 638 S>A No SGRP
s16-904082 681 E>D No SGRP
s16-904224 729 P>S No SGRP
s16-904290 751 A>T No SGRP
s16-904359 774 D>N No SGRP
s16-904485 816 A>S No SGRP
s16-904505 822 D>E No SGRP
s16-904681 881 S>Y No SGRP
s16-905112 1025 A>T No SGRP
s16-905578 1180 R>K No SGRP
s16-905592 1185 S>P No SGRP
s16-905906 1289 K>N No SGRP
s16-905961 1308 D>N No SGRP
s16-906057 1340 A>P No SGRP
s16-906505 1489 F>S No SGRP
s16-906650 1537 S>W No SGRP

No associated diseases with Q06625

4 regional properties for Q06625

Type Name Position InterPro Accession
domain Eukaryotic glycogen debranching enzyme, N-terminal domain 47 - 134 IPR029436
domain Glycogen debranching enzyme, central domain 732 - 975 IPR032788
domain Glycogen debranching enzyme, C-terminal 1045 - 1523 IPR032790
domain Glycogen debranching enzyme, glucanotransferase domain 122 - 592 IPR032792

Functions

Description
EC Number 2.4.1.25 Hexosyltransferases
Subcellular Localization
  • Mitochondrion
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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
4-alpha-glucanotransferase activity Catalysis of the transfer of a segment of a (1->4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1->4)-alpha-D-glucan.
amylo-alpha-1,6-glucosidase activity Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin. Limit dextrin is the highly branched core that remains after exhaustive treatment of glycogen with glycogen phosphorylase. It is formed because these enzymes cannot hydrolyze the (1->6) glycosidic linkages present.
beta-maltose 4-alpha-glucanotransferase activity Catalysis of the reaction: beta-D-glucose + a plant soluble heteroglycan = a plant soluble heteroglycan + maltose.

2 GO annotations of biological process

Name Definition
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 catabolic process The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNRSLLLRLS DTGEPITSCS YGKGVLTLPP IPLPKDAPKD QPLYTVKLLV SAGSPVARDG
70 80 90 100 110 120
LVWTNCPPDH NTPFKRDKFY KKIIHSSFHE DDCIDLNVYA PGSYCFYLSF RNDNEKLETT
130 140 150 160 170 180
RKYYFVALPM LYINDQFLPL NSIALQSVVS KWLGSDWEPI LSKIAAKNYN MVHFTPLQER
190 200 210 220 230 240
GESNSPYSIY DQLQFDQEHF KSPEDVKNLV EHIHRDLNML SLTDIVFNHT ANNSPWLVEH
250 260 270 280 290 300
PEAGYNHITA PHLISAIELD QELLNFSRNL KSWGYPTELK NIEDLFKIMD GIKVHVLGSL
310 320 330 340 350 360
KLWEYYAVNV QTALRDIKAH WNDESNESYS FPENIKDISS DFVKLASFVK DNVTEPNFGT
370 380 390 400 410 420
LGERNSNRIN VPKFIQLLKL INDGGSDDSE SSLATAQNIL NEVNLPLYRE YDDDVSEILE
430 440 450 460 470 480
QLFNRIKYLR LDDGGPKQGP VTVDVPLTEP YFTRFKGKDG TDYALANNGW IWNGNPLVDF
490 500 510 520 530 540
ASQNSRAYLR REVIVWGDCV KLRYGKSPED SPYLWERMSK YIEMNAKIFD GFRIDNCHST
550 560 570 580 590 600
PIHVGEYFLD LARKYNPNLY VVAELFSGSE TLDCLFVERL GISSLIREAM QAWSEEELSR
610 620 630 640 650 660
LVHKHGGRPI GSYKFVPMDD FSYPADINLN EEHCFNDSND NSIRCVSEIM IPKILTATPP
670 680 690 700 710 720
HALFMDCTHD NETPFEKRTV EDTLPNAALV ALCSSAIGSV YGYDEIFPHL LNLVTEKRHY
730 740 750 760 770 780
DISTPTGSPS IGITKVKATL NSIRTSIGEK AYDIEDSEMH VHHQGQYITF HRMDVKSGKG
790 800 810 820 830 840
WYLIARMKFS DNDDPNETLP PVVLNQSTCS LRFSYALERV GDEIPNDDKF IKGIPTKLKE
850 860 870 880 890 900
LEGFDISYDD SKKISTIKLP NEFPQGSIAI FETQQNGVDE SLDHFIRSGA LKATSSLTLE
910 920 930 940 950 960
SINSVLYRSE PEEYDVSAGE GGAYIIPNFG KPVYCGLQGW VSVLRKIVFY NDLAHPLSAN
970 980 990 1000 1010 1020
LRNGHWALDY TISRLNYYSD EAGINEVQNW LRSRFDRVKK LPSYLVPSYF ALIIGILYGC
1030 1040 1050 1060 1070 1080
CRLKAIQLMS RNIGKSTLFV QSLSMTSIQM VSRMKSTSIL PGENVPSMAA GLPHFSVNYM
1090 1100 1110 1120 1130 1140
RCWGRDVFIS LRGMLLTTGR FDEAKAHILA FAKTLKHGLI PNLLDAGRNP RYNARDAAWF
1150 1160 1170 1180 1190 1200
FLQAVQDYVY IVPDGEKILQ EQVTRRFPLD DTYIPVDDPR AFSYSSTLEE IIYEILSRHA
1210 1220 1230 1240 1250 1260
KGIKFREANA GPNLDRVMTD KGFNVEIHVD WSTGLIHGGS QYNCGTWMDK MGESEKAGSV
1270 1280 1290 1300 1310 1320
GIPGTPRDGA AIEINGLLKS ALRFVIELKN KGLFKFSDVE TQDGGRIDFT EWNQLLQDNF
1330 1340 1350 1360 1370 1380
EKRYYVPEDP SQDADYDVSA KLGVNRRGIY RDLYKSGKPY EDYQLRPNFA IAMTVAPELF
1390 1400 1410 1420 1430 1440
VPEHAIKAIT IADEVLRGPV GMRTLDPSDY NYRPYYNNGE DSDDFATSKG RNYHQGPEWV
1450 1460 1470 1480 1490 1500
WLYGYFLRAF HHFHFKTSPR CQNAAKEKPS SYLYQQLYYR LKGHRKWIFE SVWAGLTELT
1510 1520 1530
NKDGEVCNDS SPTQAWSSAC LLDLFYDLWD AYEDDS