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

4 structures for P16522

Entry ID Method Resolution Chain Position Source
8A3T EM 350 A D/P 1-626 PDB
8A5Y EM 490 A D/P 1-626 PDB
8A61 EM 540 A D/P 1-626 PDB
AF-P16522-F1 Predicted AlphaFoldDB

3 variants for P16522

Variant ID(s) Position Change Description Diseaes Association Provenance
s08-438577 159 S>N No SGRP
s08-438222 277 Q>H No SGRP
s08-437581 491 A>G No SGRP

No associated diseases with P16522

7 regional properties for P16522

Type Name Position InterPro Accession
domain Cdc23 13 - 145 IPR007192
repeat Tetratricopeptide repeat 215 - 248 IPR019734-1
repeat Tetratricopeptide repeat 397 - 430 IPR019734-2
repeat Tetratricopeptide repeat 431 - 464 IPR019734-3
repeat Tetratricopeptide repeat 465 - 498 IPR019734-4
repeat Tetratricopeptide repeat 499 - 532 IPR019734-5
repeat Tetratricopeptide repeat 536 - 569 IPR019734-6

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Chromosome, centromere, kinetochore
  • Associated with the kinetochore
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
anaphase-promoting complex A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
kinetochore A multisubunit complex that is located at the centromeric region of DNA and provides an attachment point for the spindle microtubules.

1 GO annotations of molecular function

Name Definition
cyclin binding Binding to cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis.

7 GO annotations of biological process

Name Definition
anaphase-promoting complex-dependent catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
metaphase/anaphase transition of mitotic cell cycle The cell cycle process in which a cell progresses from metaphase to anaphase during mitosis, triggered by the activation of the anaphase promoting complex by Cdc20/Sleepy homolog which results in the degradation of Securin.
positive regulation of mitotic metaphase/anaphase transition Any process that activates or increases the frequency, rate or extent of the cell cycle process in which a cell progresses from metaphase to anaphase during mitosis, triggered by the activation of the anaphase promoting complex by Cdc20/Sleepy homolog which results in the degradation of Securin.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
regulation of meiotic cell cycle Any process that modulates the rate or extent of progression through the meiotic cell cycle.
regulation of mitotic cell cycle Any process that modulates the rate or extent of progress through the mitotic cell cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNDDSQDKII HDIRIQLRKA ATELSRWKLY GSSKWAAEAL AGLAEAIDVD QTHSLADESP
70 80 90 100 110 120
LRNKQGVPKQ MFEIPQNGFG LSETEYDLYL LGSTLFDAKE FDRCVFFLKD VTNPYLKFLK
130 140 150 160 170 180
LYSKFLSWDK KSQESMENIL TTGKFTDEMY RANKDGDGSG NEDINQSGHQ RANLKMVSNE
190 200 210 220 230 240
HESQSNISSI LKEINTFLES YEIKIDDDEA DLGLALLYYL RGVILKQEKN ISKAMSSFLK
250 260 270 280 290 300
SLSCYSFNWS CWLELMDCLQ KVDDALLLNN YLYQNFQFKF SENLGSQRTI EFNIMIKFFK
310 320 330 340 350 360
LKVFEELNGQ LEDYFEDLEF LLQVFPNFTF LKAYNATISY NNLDYVTAES RFDDIVKQDP
370 380 390 400 410 420
YRLNDLETYS NILYVMQKNS KLAYLAQFVS QIDRFRPETC CIIANYYSAR QEHEKSIMYF
430 440 450 460 470 480
RRALTLDKKT TNAWTLMGHE FVELSNSHAA IECYRRAVDI CPRDFKAWFG LGQAYALLDM
490 500 510 520 530 540
HLYSLYYFQK ACTLKPWDRR IWQVLGECYS KTGNKVEAIK CYKRSIKASQ TVDQNTSIYY
550 560 570 580 590 600
RLAQLYEELE DLQECKKFMM KCVDVEELLE GIVTDETVKA RLWLAIFEIK AGNYQLAYDY
610 620
AMGVSSGTSQ EIEEARMLAR ECRRHM