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 Q2JZH2

Entry ID Method Resolution Chain Position Source
AF-Q2JZH2-F1 Predicted AlphaFoldDB

No variants for Q2JZH2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2JZH2

No associated diseases with Q2JZH2

1 regional properties for Q2JZH2

Type Name Position InterPro Accession
domain Heat shock protein Hsp90, N-terminal 10 - 215 IPR020575

Functions

Description
EC Number
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
unfolded protein binding Binding to an unfolded protein.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTTTVEQTAE SHVFEADVAR LLHMMVHSVY SDKGVFLREL ISNGADACEK LRYEAIETPS
70 80 90 100 110 120
LLAADAESRI MLRLDEESRQ LVVEDNGIGM RRDEMIEALG TIARSGTRAF MERIAENKAA
130 140 150 160 170 180
EGAQFIGQFG VGFYSCFMVA EHVDVISRRA GSEEAWKWSS DGKGSYSVEA ANLVEAPARG
190 200 210 220 230 240
TRIVLHLMED AKTYTSRWTV ERIVKEQSGH VPVAIRIVDK PGGEPVQITD GTALWTKSKS
250 260 270 280 290 300
EVSKEDYTDF YRGLSGQYDE PALTVHFRAE GRHEYTALAF VPGTQPFDMF DPERKGRMKL
310 320 330 340 350 360
YVKRVFITDD AELMPRYLRF VRGLIDTADL PLNVSREMIQ ESPILAAIRK GVTNRVITAI
370 380 390 400 410 420
EKLADGESET YLTFWKNFGP VLKEGIYEDY ERRAQLMALA RFHTSASPEG HRSLAEYVKD
430 440 450 460 470 480
AKEGQDAIYY LAGGSLDQLK ASPQLEGFRA RGIEVLLLTD SVDSFWVVNA PEFEGKAFKS
490 500 510 520 530 540
ITQGTADLAQ FPRLDNQTPP EQDSAGLATF IGFAREKLAG QVADVRASDR LTESAVCLVA
550 560 570 580 590 600
PEDGYDRQME KILQNAGRLQ GATKPILEIN LAHPVIKAIA AVEDDASYQE DATFLLLDQA
610 620
RILDGERPQD PRKFAQRLAR VFERSVRSEG