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 P40462

Entry ID Method Resolution Chain Position Source
AF-P40462-F1 Predicted AlphaFoldDB

22 variants for P40462

Variant ID(s) Position Change Description Diseaes Association Provenance
s09-92620 57 T>S No SGRP
s09-92563 76 G>R No SGRP
s09-92242 183 A>S No SGRP
s09-92229 187 A>V No SGRP
s09-92103 229 F>Y No SGRP
s09-91834 319 T>S No SGRP
s09-91756 345 S>A No SGRP
s09-91633 386 P>S No SGRP
s09-91579 404 A>S No SGRP
s09-91444 449 V>I No SGRP
s09-91116 558 K>T No SGRP
s09-91112 559 F>L No SGRP
s09-90988 601 L>F No SGRP
s09-90952 613 G>R No SGRP
s09-90897 631 N>T No SGRP
s09-90765 675 K>I No SGRP
s09-90720 690 E>G No SGRP
s09-90695 698 H>Q No SGRP
s09-90546 748 S>L No SGRP
s09-90521 756 Q>H No SGRP
s09-90180 870 T>I No SGRP
s09-90025 922 D>N No SGRP

No associated diseases with P40462

3 regional properties for P40462

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 257 - 486 IPR014782
domain ERAP1-like C-terminal domain 565 - 929 IPR024571
domain Aminopeptidase N-like, N-terminal domain 13 - 218 IPR045357

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.
nascent polypeptide-associated complex A heterodimeric protein complex that can reversibly bind to ribosomes, and is located in direct proximity to newly synthesized polypeptide chains as they emerge from the ribosome.

4 GO annotations of molecular function

Name Definition
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.
nascent polypeptide-associated complex binding Binding to nascent polypeptide-associated complex, a heterodimeric protein complex that can reversibly bind to ribosomes and is located in direct proximity to newly synthesized polypeptide chains as they emerge from the ribosome.
peptide binding Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
peptide catabolic process The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
regulation of cytoplasmic translation Any process that modulates the frequency, rate or extent of cytoplasmic translation.
ribosome biogenesis A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits; includes transport to the sites of protein synthesis.

22 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32454 APE2 Aminopeptidase 2, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P79171 ANPEP Aminopeptidase N Felis catus (Cat) (Felis silvestris catus) PR
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme Homo sapiens (Human) PR
P15144 ANPEP Aminopeptidase N Homo sapiens (Human) PR
Q9UIQ6 LNPEP Leucyl-cystinyl aminopeptidase Homo sapiens (Human) PR
Q9NZ08 ERAP1 Endoplasmic reticulum aminopeptidase 1 Homo sapiens (Human) PR
P55786 NPEPPS Puromycin-sensitive aminopeptidase Homo sapiens (Human) PR
Q8K093 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Mus musculus (Mouse) PR
P97449 Anpep Aminopeptidase N Mus musculus (Mouse) PR
Q8C129 Lnpep Leucyl-cystinyl aminopeptidase Mus musculus (Mouse) PR
Q9EQH2 Erap1 Endoplasmic reticulum aminopeptidase 1 Mus musculus (Mouse) PR
Q11011 Npepps Puromycin-sensitive aminopeptidase Mus musculus (Mouse) PR
P15145 ANPEP Aminopeptidase N Sus scrofa (Pig) PR
Q10836 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Rattus norvegicus (Rat) PR
P15684 Anpep Aminopeptidase N Rattus norvegicus (Rat) PR
P97629 Lnpep Leucyl-cystinyl aminopeptidase Rattus norvegicus (Rat) PR
Q9JJ22 Erap1 Endoplasmic reticulum aminopeptidase 1 Rattus norvegicus (Rat) PR
Q0J5V5 Os08g0398700 Aminopeptidase M1-B Oryza sativa subsp japonica (Rice) PR
Q6Z6L4 Os02g0218200 Aminopeptidase M1-A Oryza sativa subsp japonica (Rice) PR
Q6K4E7 Os09g0362800 Aminopeptidase M1-D Oryza sativa subsp japonica (Rice) PR
Q17405 AC3.5 Aminopeptidase-like protein AC3.5 Caenorhabditis elegans PR
Q8VZH2 APM1 Aminopeptidase M1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSDNLLSLEN PVVPSHYELR LEIDPKQSSP NFKGSAIIHL KFNPNSTTLA SIEDSFTQFK
70 80 90 100 110 120
LHSKDLIVLS AHATIGSTKF DLKISQDTGK HLSIFNSESP IQLSNDCPLI LSVQYVGKIR
130 140 150 160 170 180
DIKTHHDKTF GIFKTNFMDR KTGTANNHVV ATHCQPFSAS NIFPCIDEPS NKSTFQLNIA
190 200 210 220 230 240
TDAQYKAVSN TPVEMVEALD SSQKHLVKFA KTPLMTTSVF GFSIGDLEFL KTEIKLEGDR
250 260 270 280 290 300
TIPVSIYAPW DIANAAFTLD TVQKYLPLLE SYFKCPYPLP KLDFVLLPYL SDMAMENFGM
310 320 330 340 350 360
ITIQLNHLLI PPNALANETV REQAQQLIVH ELVHQWMGNY ISFDSWESLW FNESFATWLA
370 380 390 400 410 420
CHILEQNGDL SHYWTSEPYL LQQVEPTMCR DAADVNGRSI FQIAQRNTGI DSQTSDIFDP
430 440 450 460 470 480
EAYTKGIIML RSLQLATGES HLQKGLESVF EDTKTFHARS VKPMDIWNHI GKFLKSQNIT
490 500 510 520 530 540
NFVSSWTRTP GLPVVKVEVE EKDGKTQTKL TQHRFINQLS TEEKDQLEDV PYQVPLFGVL
550 560 570 580 590 600
PDGKMDTKNV LLTDRTLKFD YPILVINHLA QGYYRVSYES EECYALINDK ITEETLSEID
610 620 630 640 650 660
LRKIFLDLSQ FIGDEGFQNS IHLHGLFKIL NHIASPSTKI ASKYWDPLSK GLEVLQTIDR
670 680 690 700 710 720
ASLTSSKLQS FLKKKIVIPL FNKIDWPHGE FDKSTNPHEL KVMSQVLFLN KNSAKCAELC
730 740 750 760 770 780
QIYFKHLLQG PRSSVPLELV NSILVVVSQH CANIKQWKKI FDLVKRSSCT GITNHVINMY
790 800 810 820 830 840
DQNSSETAML IQNGAIESLG FCLDSDIVKK TLNFITSNIE SEGMELALFG FNYNFKKRLN
850 860 870 880 890 900
KNEKPQDQVV RETIWEWYMG NFDQWARKAT RKGTTTGDHL HKALRSISLI IFQMFVADEP
910 920 930 940
QKIEKFINLE KEKLGQSLLS LDDIWASVQQ DEESRKTIRR DLASLV