KEGG   ORTHOLOGY: K09490
Entry
K09490                      KO                                     

Name
HSPA5, BIP
Definition
endoplasmic reticulum chaperone BiP [EC:3.6.4.10]
Pathway
ko03060  Protein export
ko04141  Protein processing in endoplasmic reticulum
ko04612  Antigen processing and presentation
ko04918  Thyroid hormone synthesis
ko05012  Parkinson disease
ko05014  Amyotrophic lateral sclerosis
ko05020  Prion disease
ko05022  Pathways of neurodegeneration - multiple diseases
Brite
KEGG Orthology (KO) [BR:ko00001]
 09120 Genetic Information Processing
  09123 Folding, sorting and degradation
   03060 Protein export
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
   04141 Protein processing in endoplasmic reticulum
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
 09150 Organismal Systems
  09151 Immune system
   04612 Antigen processing and presentation
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
  09152 Endocrine system
   04918 Thyroid hormone synthesis
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
 09160 Human Diseases
  09164 Neurodegenerative disease
   05012 Parkinson disease
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
   05014 Amyotrophic lateral sclerosis
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
   05020 Prion disease
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
   05022 Pathways of neurodegeneration - multiple diseases
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
 09180 Brite Hierarchies
  09182 Protein families: genetic information processing
   03110 Chaperones and folding catalysts
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
   04131 Membrane trafficking
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
  09183 Protein families: signaling and cellular processes
   04147 Exosome
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
Enzymes [BR:ko01000]
 3. Hydrolases
  3.6  Acting on acid anhydrides
   3.6.4  Acting on acid anhydrides to facilitate cellular and subcellular movement
    3.6.4.10  non-chaperonin molecular chaperone ATPase
     K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
Chaperones and folding catalysts [BR:ko03110]
 Heat shock proteins
  HSP70 / DNAK
   K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
Membrane trafficking [BR:ko04131]
 Endoplasmic reticulum (ER) - Golgi transport
  Forward pathways
   ER-Golgi intermediate compartment (ERGIC) proteins
    K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
Exosome [BR:ko04147]
 Exosomal proteins
  Exosomal proteins of haemopoietic cells  (B-cell, T-cell, DC-cell, reticulocyte, and mast cell)
   K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
  Exosomal proteins of other body fluids (saliva and urine)
   K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
  Exosomal proteins of colorectal cancer cells
   K09490  HSPA5, BIP; endoplasmic reticulum chaperone BiP
Other DBs
TC: 1.A.33
Genes
HSA: 3309(HSPA5)
PTR: 464733(HSPA5)
PPS: 100987715(HSPA5)
GGO: 101125975(HSPA5)
PON: 100173944(HSPA5)
NLE: 100599238(HSPA5)
MCC: 703193(HSPA5)
MCF: 102140826(HSPA5)
CSAB: 103239874(HSPA5)
RRO: 104664383(HSPA5)
RBB: 108531361(HSPA5)
CJC: 100389117(HSPA5)
SBQ: 101050180(HSPA5)
MMU: 14828(Hspa5)
MCAL: 110308976(Hspa5)
MPAH: 110319438(Hspa5)
RNO: 25617(Hspa5)
MUN: 110563757(Hspa5)
CGE: 100689305(Hspa5)
NGI: 103727040(Hspa5)
HGL: 101713339(Hspa5)
CCAN: 109683432(Hspa5)
OCU: 100008764(HSPA5)
TUP: 102498137(HSPA5)
CFA: 480726(HSPA5)
VVP: 112927875(HSPA5)
AML: 100480574(HSPA5)
UMR: 103670323(HSPA5)
UAH: 113266410(HSPA5)
ORO: 101381213(HSPA5)
ELK: 111146005
FCA: 101083630(HSPA5)
PTG: 102953749(HSPA5)
PPAD: 109250165(HSPA5)
AJU: 106965381(HSPA5)
BTA: 415113(HSPA5)
BOM: 102283374(HSPA5)
BIU: 109566467(HSPA5)
BBUB: 102412431(HSPA5)
CHX: 102185663(HSPA5)
OAS: 780447(HSPA5)
SSC: 407060(HSPA5)
CFR: 102515954(HSPA5)
CDK: 105092624(HSPA5)
BACU: 103018736(HSPA5)
LVE: 103072929(HSPA5)
OOR: 101289151(HSPA5)
DLE: 111177217(HSPA5)
ECB: 100067235(HSPA5)
EPZ: 103552124(HSPA5)
EAI: 106830826(HSPA5)
MYB: 102251472(HSPA5)
MYD: 102764844(HSPA5)
MNA: 107535485(HSPA5)
HAI: 109379563
DRO: 112306383(HSPA5)
PALE: 102895517(HSPA5)
RAY: 107506635(HSPA5)
MJV: 108398314(HSPA5)
LAV: 100664821(HSPA5)
TMU: 101340706
MDO: 100015941(HSPA5)
SHR: 100923558(HSPA5)
PCW: 110194947(HSPA5)
OAA: 100681083(HSPA5)
GGA: 396487(HSPA5)
MGP: 100538701(HSPA5)
CJO: 107321942(HSPA5)
NMEL: 110406904(HSPA5)
ACYG: 106040714(HSPA5)
TGU: 100218236(HSPA5)
LSR: 110477678(HSPA5)
SCAN: 103818919(HSPA5)
GFR: 102035853(HSPA5)
FAB: 101812124(HSPA5)
PHI: 102106132(HSPA5)
PMAJ: 107212050(HSPA5)
CCAE: 111937129(HSPA5)
CCW: 104688520(HSPA5)
ETL: 114061986(HSPA5)
FPG: 101913530(HSPA5)
FCH: 102047849(HSPA5)
CLV: 102089896(HSPA5)
EGZ: 104134062(HSPA5)
NNI: 104023331(HSPA5)
ACUN: 113486422(HSPA5)
PADL: 103925616(HSPA5)
AAM: 106495036(HSPA5)
ASN: 102382114(HSPA5)
AMJ: 106737030(HSPA5)
PSS: 102459918(HSPA5)
CMY: 102940886(HSPA5)
CPIC: 101940302(HSPA5)
ACS: 100558585(hspa5)
PVT: 110082947(HSPA5)
PBI: 103048115(HSPA5)
PMUR: 107296774(HSPA5)
TSR: 106540102(HSPA5)
PMUA: 114589526(HSPA5)
GJA: 107119964(HSPA5)
XLA: 100337562(hspa5b) 379756(hspa5.S) 397850(hspa5)
XTR: 100492570(hspa5)
NPR: 108799174(HSPA5)
DRE: 378848(hspa5)
IPU: 108260227(hspa5)
PHYP: 113531242(hspa5)
AMEX: 103030781(hspa5)
EEE: 113587096(hspa5)
TRU: 101063130(hspa5)
LCO: 104925213(hspa5)
NCC: 104953687(hspa5)
OLA: 101157378(hspa5)
XMA: 102235487(hspa5)
XCO: 114150012(hspa5)
PRET: 103473829(hspa5)
CVG: 107095989(hspa5)
NFU: 107374516(hspa5)
KMR: 108231027(hspa5)
ALIM: 106518224(hspa5)
AOCE: 111579823(hspa5) 111579828
CSEM: 103390212(hspa5)
POV: 109626157(hspa5)
LCF: 108874458(hspa5)
SDU: 111239560(hspa5)
SLAL: 111653971 111664776(hspa5)
HCQ: 109521641(hspa5)
BPEC: 110160447(hspa5)
MALB: 109960600(hspa5)
SASA: 100196613(grp78) 106567149
ELS: 105015002(hspa5)
PKI: 111842682(hspa5) 111843454
LCM: 102359987(HSPA5)
CMK: 103189196(hspa5)
RTP: 109913839(hspa5)
BFO: 118420822
SPU: 584585
DME: Dmel_CG4147(Hsc70-3)
DER: 6551261
DSE: 6619913
DSI: Dsimw501_GD15970(Dsim_GD15970)
DYA: Dyak_GE17597(Dyak_Hsc70-3)
DAN: 6502959
DSR: 110179613
DPE: 6598353
DMN: 108152903
DWI: 6652915
DAZ: 108619158
DNV: 108656817
DHE: 111605302
DVI: 6633411
MDE: 101887458
LCQ: 111689731
AME: 409587(Hsc70-3)
BIM: 100740224
CCAL: 108625330
OBB: 114877568
SOC: 105201924
MPHA: 105830816
AEC: 105149703
ACEP: 105627133
PBAR: 105424179
VEM: 105559488
HST: 105181048
DQU: 106749868
CFO: 105257249
LHU: 105677531
PGC: 109854120
OBO: 105280944
PCF: 106786492
NVI: 100120866
CSOL: 105368890
MDL: 103580512
TCA: 659147
DPA: 109539187
ATD: 109602923
NVL: 108557894
BMOR: 692373(HSP70)
BMAN: 114242575
PMAC: 106711633
PRAP: 110991823
HAW: 110374656
TNL: 113494618
API: 100166283(Hsc70-3)
DNX: 107166789
AGS: 114123932
RMD: 113554771
BTAB: 109032808
CLEC: 106669548
ZNE: 110836546
TUT: 107362423
DPTE: 113791035
CEL: CELE_C15H9.6(hsp-3) CELE_F43E2.8(hsp-4)
CBR: CBG13144(Cbr-hsp-4) CBG14829(Cbr-hsp-3)
BMY: Bm1_07645
TSP: Tsp_03312
OBI: 106880098
LAK: 106154702
SHX: MS3_10713
EGL: EGR_06658
NVE: 5504498
EPA: 110254908
ADF: 107342073
AMIL: 114955027
PDAM: 113673571
SPIS: 111345883
DGT: 114519155
HMG: 100200137
AQU: 100637629
ATH: AT1G09080(BIP3) AT5G28540(BIP1) AT5G42020(BIP2)
CPAP: 110820053
GMX: 100803843 547838 547839(GMBIP4) 547840(GMBIP2)
VRA: 106779998
LJA: Lj1g3v4921040.1(Lj1g3v4921040.1) Lj4g3v3014490.1(Lj4g3v3014490.1)
CSV: 101207505
CMO: 103482828
MCHA: 111015251
JRE: 109002071
SLY: 101252822 101263797 543957(BiP/grp78)
DOSA: Os01t0517900-00(Os01g0517900) Os02t0115900-01(Os02g0115900) Os03t0710500-00(Os03g0710500) Os05t0367800-00(Os05g0367800) Os05t0428600-01(Os05g0428600) Os05t0591400-01(Os05g0591400) Os06t0212900-01(Os06g0212900) Os08t0197700-00(Os08g0197700) Os12t0153600-00(Os12g0153600)
ATS: 109738229(LOC109738229) 109748672(LOC109748672) 109753491(LOC109753491) 109764454(LOC109764454) 109765529(LOC109765529) 109782483(LOC109782483)
PEQ: 110022492
APRO: F751_3275
OLU: OSTLU_119566(bip)
SCE: YJL034W(KAR2)
ERC: Ecym_8263
KMX: KLMA_20691(GRP78)
NCS: NCAS_0A01220(NCAS0A01220)
NDI: NDAI_0C02310(NDAI0C02310)
TPF: TPHA_0N00920(TPHA0N00920)
TBL: TBLA_0D03380(TBLA0D03380)
TDL: TDEL_0E03870(TDEL0E03870)
KAF: KAFR_0E01650(KAFR0E01650) KAFR_0J01060(KAFR0J01060)
PIC: PICST_69996(KAR2)
CAL: CAALFM_C201120WA(KAR2)
CDU: CD36_16010(CaKAR2)
SLB: AWJ20_718(KAR2)
NCR: NCU03982(grp78)
NTE: NEUTE1DRAFT69229(NEUTE1DRAFT_69229)
MGR: MGG_02503
SSCK: SPSK_04019
TRE: TRIREDRAFT_122920(bip1)
MAW: MAC_02661
MAJ: MAA_02142
CMT: CCM_05087
BFU: BCIN_13g00960(Bckar2)
ANI: AN2062.2
ANG: ANI_1_578094(An11g04180)
ABE: ARB_05266
TVE: TRV_02305
PTE: PTT_13087
ZTR: MYCGRDRAFT_83835(MgKAR2)
SPO: SPAC22A12.15c(bip1)
CNE: CNN01680
CNB: CNBN1630
TASA: A1Q1_02366
ABP: AGABI1DRAFT115984(AGABI1DRAFT_115984)
ABV: AGABI2DRAFT195173(hspD)
MGL: MGL_2666
MRT: MRET_1298
DFA: DFA_10906
EHI: EHI_001950(90.t00019) EHI_043000(111.t00021) EHI_130160 EHI_133950 EHI_185120(450.t00003) EHI_199590(45.t00004)
PCB: PCHAS_081920(PC302190.00.0)
TAN: TA10500
TPV: TP04_0683
BBO: BBOV_III007800(17.m07684)
CPV: cgd7_360
SMIN: v1.2.000034.t1(symbB.v1.2.000034.t1) v1.2.006004.t1(symbB.v1.2.006004.t1) v1.2.009726.t1(symbB.v1.2.009726.t1) v1.2.018267.t1(symbB.v1.2.018267.t1) v1.2.019009.t1(symbB.v1.2.019009.t1) v1.2.028589.t1(symbB.v1.2.028589.t1) v1.2.034171.t1(symbB.v1.2.034171.t1) v1.2.034323.t1(symbB.v1.2.034323.t1)
PTI: PHATRDRAFT_54246(BiP)
TPS: THAPSDRAFT_27656(hsp70_4) THAPSDRAFT_38578(BIP2)
SPAR: SPRG_00333
TCR: 506585.40
 » show all
Reference
  Authors
Dudek J, Benedix J, Cappel S, Greiner M, Jalal C, Muller L, Zimmermann R
  Title
Functions and pathologies of BiP and its interaction partners.
  Journal
Cell Mol Life Sci 66:1556-69 (2009)
DOI:10.1007/s00018-009-8745-y
  Sequence
[hsa:3309]
Reference
PMID:2840249
  Authors
Ting J, Lee AS
  Title
Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation.
  Journal
DNA 7:275-86 (1988)
DOI:10.1089/dna.1988.7.275
  Sequence
[hsa:3309]
Reference
  Authors
Kimura T, Hosoda Y, Sato Y, Kitamura Y, Ikeda T, Horibe T, Kikuchi M
  Title
Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.
  Journal
J Biol Chem 280:31438-41 (2005)
DOI:10.1074/jbc.M503377200
  Sequence
[sce:YJL034W]
Reference
  Authors
Yang J, Nune M, Zong Y, Zhou L, Liu Q
  Title
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
  Journal
Structure 23:2191-2203 (2015)
DOI:10.1016/j.str.2015.10.012
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