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 Q08225

Entry ID Method Resolution Chain Position Source
3CSK X-ray 195 A A 1-711 PDB
AF-Q08225-F1 Predicted AlphaFoldDB

15 variants for Q08225

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-220899 45 R>K No SGRP
s15-220973 70 N>D No SGRP
s15-220985 74 P>S No SGRP
s15-221061 99 G>A No SGRP
s15-221111 116 K>E No SGRP
s15-221191 142 N>K No SGRP
s15-221205 147 S>F No SGRP
s15-221381 206 A>S No SGRP
s15-221474 237 E>K No SGRP
s15-221561 266 L>I No SGRP
s15-221840 359 A>S No SGRP
s15-222128 455 V>I No SGRP
s15-222372 536 I>T No SGRP
s15-222521 586 M>V No SGRP
s15-222851 696 D>N No SGRP

No associated diseases with Q08225

No regional properties for Q08225

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q08225

Functions

Description
EC Number
Subcellular Localization
  • 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.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

4 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
dipeptidyl-peptidase activity Catalysis of the hydrolysis of N-terminal dipeptides from a polypeptide chain.
metal ion binding Binding to a metal ion.
metalloexopeptidase activity Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSHFFADHDA PLSMLSVKTE YFPQLTDKEQ KYAHFMSKAS HAGSRVVMRQ VSHESEPIFD
70 80 90 100 110 120
LILAIHSKLN GKYPEDDITQ KQQTGLYLEY VSQFLSNLGN FKSFGDTKFI PRCEVKFFKQ
130 140 150 160 170 180
LLELAKINPC SSPLTLSPVD VNHEFTSHHL FSTINELIDI GIYHVEEKAA LLGFPSQGYT
190 200 210 220 230 240
SAYYLGLPVT PEDMALLKEQ LFAELAILPE NTRINKVGEN SFQIWVASEN VKNQITETYP
250 260 270 280 290 300
SGQITLSNAV TKVEFIFGDH SREMRLVASY LKEAQKFAAN DTQKAMLQEY INHFVTGSSQ
310 320 330 340 350 360
AHKEAQKLWV KDISPVIETN IGFIETYREP SGIIGEFESL VAIQNKERTA KFSSLVNNAE
370 380 390 400 410 420
EFISLLPWSK DYEKPIFNPP DFTSLEVLTF TGSGIPAGIN IPNYDDVRLK IGFKNVSLGN
430 440 450 460 470 480
ILSAAAKSSS KHPPSFISQE DRPIFEKYQS DSFEVQVGIH ELLGHGSGKL LTEFTDGFNF
490 500 510 520 530 540
DKENPPLGLD GKPVSTYYKV GETWGSKFGQ LAGPFEECRA EVIAMFLLTN KKILDIFGFH
550 560 570 580 590 600
DVESQDKVIY AGYLQMARAG LLALEYWNPK TGKWGQPHMQ ARFSIMKTFM KHSTDKNFLK
610 620 630 640 650 660
LEMNSTNDDF AIKLDKSLIK TAGHECVKDY LKHLHVYKCS GDVEQGSKYF IDRSTVTPDL
670 680 690 700 710
ASLRDIVLSK RLPRRQFIQS NSYIDDNNKV TLKEYDETPQ GMLQSFLDRE L