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 B8HTK3

Entry ID Method Resolution Chain Position Source
AF-B8HTK3-F1 Predicted AlphaFoldDB

No variants for B8HTK3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B8HTK3

No associated diseases with B8HTK3

3 regional properties for B8HTK3

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 216 - 434 IPR014782
domain ERAP1-like C-terminal domain 507 - 813 IPR024571
domain Aminopeptidase N-like, N-terminal domain 11 - 180 IPR045357

Functions

Description
EC Number 3.4.11.1 Aminopeptidases
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.

2 GO annotations of molecular function

Name Definition
manganese ion binding Binding to a manganese ion (Mn).
metalloaminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from 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
MDIRTTTTTA TDWAGDLLAL GFFEDQVELS GSLAELDQKL DGILQELIAE TEFKGKAGKS
70 80 90 100 110 120
AIARISSKSP IRKIMILGLG KAEDFKLDTL RRTAATIARS AKKEKGKTLG ISLPLWNNDP
130 140 150 160 170 180
TSTTQAIAEG IELALHQDHR FKSNSEDNND NHAPEQIQLL GLGDQTTAIE RAQRICSGVI
190 200 210 220 230 240
LARELVAAPA NVVTPVTLAE TARDLAQEYG LDVEVLGQAE CEALGMGAFL GVALASDLPP
250 260 270 280 290 300
QFIHLTYRPS GTPRRKLAII GKGLTFDSGG LNLKTGGSGI ETMKMDMAGS AATLGAAKVV
310 320 330 340 350 360
GQLKPDVEVH FIVAATENMI SGRAMHPGDI LTASNGKTIE VNNTDAEGRL TLADALVFAE
370 380 390 400 410 420
KLGVDALVDL ATLTGACIVA LGDDIAGLWS SDDALAEQIL QAADHSGEKL WRMPMEEKYF
430 440 450 460 470 480
EGMKSQIADM KNTGPRAGGS ITAALFLKQF VKETPWAHLD VAGPVWADKE NGYNNAGATG
490
YGVRTLVNWV LGS