UniProtKB - P11021 (GRP78_HUMAN)
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Protein
78 kDa glucose-regulated protein
Gene
HSPA5
Organism
Homo sapiens (Human)
Status
Functioni
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate.3 Publications
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Binding sitei | 96 | ATP | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Nucleotide bindingi | 36 – 39 | ATP | 4 | |
| Nucleotide bindingi | 227 – 229 | ATP | 3 | |
| Nucleotide bindingi | 293 – 300 | ATP | 8 | |
| Nucleotide bindingi | 364 – 367 | ATP | 4 |
GO - Molecular functioni
- ATPase activity Source: AgBase
- ATP binding Source: UniProtKB-KW
- cadherin binding Source: BHF-UCL
- calcium ion binding Source: UniProtKB
- chaperone binding Source: BHF-UCL
- enzyme binding Source: BHF-UCL
- glycoprotein binding Source: UniProtKB
- misfolded protein binding Source: UniProtKB
- protein domain specific binding Source: UniProtKB
- ribosome binding Source: Ensembl
- ubiquitin protein ligase binding Source: UniProtKB
- unfolded protein binding Source: UniProtKB
GO - Biological processi
- activation of signaling protein activity involved in unfolded protein response Source: Ensembl
- ATF6-mediated unfolded protein response Source: Reactome
- cellular response to antibiotic Source: Ensembl
- cellular response to calcium ion Source: Ensembl
- cellular response to cAMP Source: Ensembl
- cellular response to drug Source: Ensembl
- cellular response to glucose starvation Source: UniProtKB
- cellular response to interleukin-4 Source: Ensembl
- cellular response to manganese ion Source: Ensembl
- cellular response to nerve growth factor stimulus Source: Ensembl
- cerebellar Purkinje cell layer development Source: Ensembl
- cerebellum structural organization Source: Ensembl
- endoplasmic reticulum unfolded protein response Source: BHF-UCL
- ER overload response Source: Ensembl
- IRE1-mediated unfolded protein response Source: Reactome
- maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of protein homodimerization activity Source: ParkinsonsUK-UCL
- negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
- neuron apoptotic process Source: Ensembl
- neuron differentiation Source: Ensembl
- PERK-mediated unfolded protein response Source: Reactome
- positive regulation of cell migration Source: UniProtKB
- positive regulation of neuron projection development Source: Ensembl
- positive regulation of protein ubiquitination Source: Ensembl
- positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
- protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
- regulation of ATF6-mediated unfolded protein response Source: ParkinsonsUK-UCL
- regulation of IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
- regulation of PERK-mediated unfolded protein response Source: ParkinsonsUK-UCL
- regulation of protein folding in endoplasmic reticulum Source: BHF-UCL
- response to cocaine Source: Ensembl
- response to methamphetamine hydrochloride Source: Ensembl
- response to radiation Source: Ensembl
- stress response to metal ion Source: Ensembl
- substantia nigra development Source: UniProtKB
- toxin transport Source: Ensembl
- ubiquitin-dependent ERAD pathway Source: BHF-UCL
Keywordsi
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
| Reactomei | R-HSA-114608. Platelet degranulation. R-HSA-3371453. Regulation of HSF1-mediated heat shock response. R-HSA-381033. ATF6 (ATF6-alpha) activates chaperones. R-HSA-381042. PERK regulates gene expression. R-HSA-381070. IRE1alpha activates chaperones. R-HSA-381183. ATF6 (ATF6-alpha) activates chaperone genes. R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC. |
Names & Taxonomyi
| Protein namesi | Recommended name: 78 kDa glucose-regulated proteinShort name: GRP-78 Alternative name(s): Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78 Heat shock 70 kDa protein 5 Immunoglobulin heavy chain-binding protein Short name: BiP |
| Gene namesi | Name:HSPA5 Synonyms:GRP78 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| HGNCi | HGNC:5238. HSPA5. |
Subcellular locationi
- Endoplasmic reticulum lumen 3 Publications
- Melanosome
- Cytoplasm By similarity
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
GO - Cellular componenti
- cell surface Source: Ensembl
- endoplasmic reticulum Source: MGI
- endoplasmic reticulum chaperone complex Source: UniProtKB
- endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
- endoplasmic reticulum lumen Source: Reactome
- endoplasmic reticulum membrane Source: Reactome
- extracellular exosome Source: UniProtKB
- extracellular matrix Source: BHF-UCL
- focal adhesion Source: UniProtKB
- integral component of endoplasmic reticulum membrane Source: BHF-UCL
- melanosome Source: UniProtKB-SubCell
- membrane Source: UniProtKB
- midbody Source: UniProtKB
- mitochondrion Source: Ensembl
- myelin sheath Source: Ensembl
- nucleus Source: UniProtKB
- plasma membrane Source: Ensembl
- smooth endoplasmic reticulum Source: Ensembl
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulumPathology & Biotechi
Involvement in diseasei
Autoantigen in rheumatoid arthritis.1 Publication
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 585 | K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications | 1 |
Organism-specific databases
| DisGeNETi | 3309. |
| OpenTargetsi | ENSG00000044574. |
| PharmGKBi | PA29504. |
Chemistry databases
| ChEMBLi | CHEMBL1781865. |
| DrugBanki | DB00945. Acetylsalicylic acid. DB00025. Antihemophilic Factor (Recombinant). |
Polymorphism and mutation databases
| BioMutai | HSPA5. |
| DMDMi | 14916999. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Signal peptidei | 1 – 18 | 2 PublicationsAdd BLAST | 18 | |
| ChainiPRO_0000013566 | 19 – 654 | 78 kDa glucose-regulated proteinAdd BLAST | 636 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 86 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 125 | N6-acetyllysineBy similarity | 1 | |
| Modified residuei | 160 | Nitrated tyrosineBy similarity | 1 | |
| Modified residuei | 213 | N6-acetyllysineBy similarity | 1 | |
| Modified residuei | 271 | N6-acetyllysineBy similarity | 1 | |
| Modified residuei | 326 | N6-acetyllysineBy similarity | 1 | |
| Cross-linki | 352 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
| Modified residuei | 353 | N6-acetyllysine; alternateBy similarity | 1 | |
| Cross-linki | 353 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources | ||
| Modified residuei | 447 | N6-succinyllysineBy similarity | 1 | |
| Modified residuei | 492 | Omega-N-methylarginineBy similarity | 1 | |
| Modified residuei | 518 | PhosphothreonineCombined sources | 1 | |
| Modified residuei | 585 | N6,N6,N6-trimethyllysine; by METTL21A; in vitroCombined sources2 Publications | 1 | |
| Modified residuei | 585 | N6,N6-dimethyllysine; alternateCombined sources | 1 | |
| Modified residuei | 585 | N6-methyllysine; alternateCombined sources | 1 | |
| Modified residuei | 591 | N6-methyllysineCombined sources | 1 | |
| Modified residuei | 643 | PhosphothreonineBy similarity | 1 | |
| Modified residuei | 648 | PhosphothreonineBy similarity | 1 |
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugationProteomic databases
| EPDi | P11021. |
| PaxDbi | P11021. |
| PeptideAtlasi | P11021. |
| PRIDEi | P11021. |
| TopDownProteomicsi | P11021. |
2D gel databases
| DOSAC-COBS-2DPAGEi | P11021. |
| OGPi | P11021. |
| REPRODUCTION-2DPAGEi | P11021. |
| SWISS-2DPAGEi | P11021. |
| UCD-2DPAGEi | P11021. |
PTM databases
| iPTMneti | P11021. |
| PhosphoSitePlusi | P11021. |
| SwissPalmi | P11021. |
Expressioni
Inductioni
By endoplasmic reticulum stress.1 Publication
Gene expression databases
| Bgeei | ENSG00000044574. |
| CleanExi | HS_HSPA5. |
| ExpressionAtlasi | P11021. baseline and differential. |
| Genevisiblei | P11021. HS. |
Organism-specific databases
| HPAi | CAB005221. HPA038845. HPA038846. |
Interactioni
Subunit structurei
Interacts with DNAJC1 (via J domain) (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (By similarity). Interacts with TMEM132A and TRIM21 (PubMed:12699405). May form a complex with ERLEC1, OS9, SEL1L and SYVN1 (PubMed:18264092,PubMed:18502753). Interacts with DNAJC10 (PubMed:12411443, PubMed:23769672). Interacts with MX1 (By similarity). Interacts with METTL23 (PubMed:23349634). Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration (PubMed:23990668). Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum (PubMed:21080038). Interacts with CIPC (PubMed:26657846). Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis (PubMed:21289099).By similarity10 Publications
Binary interactionsi
GO - Molecular functioni
- cadherin binding Source: BHF-UCL
- chaperone binding Source: BHF-UCL
- enzyme binding Source: BHF-UCL
- glycoprotein binding Source: UniProtKB
- misfolded protein binding Source: UniProtKB
- protein domain specific binding Source: UniProtKB
- ubiquitin protein ligase binding Source: UniProtKB
- unfolded protein binding Source: UniProtKB
Protein-protein interaction databases
| BioGridi | 109541. 469 interactors. |
| DIPi | DIP-33189N. |
| IntActi | P11021. 180 interactors. |
| MINTi | MINT-1135308. |
| STRINGi | 9606.ENSP00000324173. |
Chemistry databases
| BindingDBi | P11021. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Beta strandi | 31 – 34 | Combined sources | 4 | |
| Beta strandi | 37 – 45 | Combined sources | 9 | |
| Beta strandi | 47 – 52 | Combined sources | 6 | |
| Beta strandi | 60 – 63 | Combined sources | 4 | |
| Beta strandi | 66 – 68 | Combined sources | 3 | |
| Beta strandi | 74 – 76 | Combined sources | 3 | |
| Helixi | 78 – 82 | Combined sources | 5 | |
| Helixi | 84 – 86 | Combined sources | 3 | |
| Helixi | 88 – 90 | Combined sources | 3 | |
| Beta strandi | 91 – 93 | Combined sources | 3 | |
| Helixi | 95 – 97 | Combined sources | 3 | |
| Turni | 98 – 100 | Combined sources | 3 | |
| Helixi | 106 – 114 | Combined sources | 9 | |
| Beta strandi | 116 – 122 | Combined sources | 7 | |
| Beta strandi | 125 – 131 | Combined sources | 7 | |
| Beta strandi | 137 – 140 | Combined sources | 4 | |
| Helixi | 142 – 161 | Combined sources | 20 | |
| Beta strandi | 167 – 172 | Combined sources | 6 | |
| Helixi | 178 – 190 | Combined sources | 13 | |
| Beta strandi | 194 – 200 | Combined sources | 7 | |
| Helixi | 201 – 208 | Combined sources | 8 | |
| Turni | 209 – 212 | Combined sources | 4 | |
| Beta strandi | 215 – 225 | Combined sources | 11 | |
| Beta strandi | 230 – 238 | Combined sources | 9 | |
| Beta strandi | 241 – 250 | Combined sources | 10 | |
| Helixi | 255 – 274 | Combined sources | 20 | |
| Helixi | 278 – 280 | Combined sources | 3 | |
| Helixi | 282 – 298 | Combined sources | 17 | |
| Turni | 299 – 301 | Combined sources | 3 | |
| Beta strandi | 302 – 313 | Combined sources | 12 | |
| Beta strandi | 316 – 323 | Combined sources | 8 | |
| Helixi | 324 – 337 | Combined sources | 14 | |
| Helixi | 339 – 348 | Combined sources | 10 | |
| Helixi | 353 – 355 | Combined sources | 3 | |
| Beta strandi | 358 – 363 | Combined sources | 6 | |
| Helixi | 364 – 367 | Combined sources | 4 | |
| Helixi | 369 – 378 | Combined sources | 10 | |
| Turni | 379 – 381 | Combined sources | 3 | |
| Turni | 390 – 392 | Combined sources | 3 | |
| Helixi | 393 – 405 | Combined sources | 13 | |
| Beta strandi | 415 – 419 | Combined sources | 5 | |
| Beta strandi | 424 – 428 | Combined sources | 5 | |
| Turni | 429 – 431 | Combined sources | 3 | |
| Beta strandi | 432 – 437 | Combined sources | 6 | |
| Beta strandi | 442 – 455 | Combined sources | 14 | |
| Beta strandi | 460 – 467 | Combined sources | 8 | |
| Helixi | 473 – 475 | Combined sources | 3 | |
| Beta strandi | 476 – 485 | Combined sources | 10 | |
| Beta strandi | 491 – 493 | Combined sources | 3 | |
| Beta strandi | 497 – 503 | Combined sources | 7 | |
| Beta strandi | 509 – 515 | Combined sources | 7 | |
| Turni | 516 – 518 | Combined sources | 3 | |
| Beta strandi | 521 – 526 | Combined sources | 6 | |
| Turni | 528 – 531 | Combined sources | 4 | |
| Helixi | 535 – 547 | Combined sources | 13 | |
| Helixi | 549 – 577 | Combined sources | 29 | |
| Turni | 579 – 581 | Combined sources | 3 | |
| Helixi | 582 – 585 | Combined sources | 4 | |
| Helixi | 590 – 606 | Combined sources | 17 | |
| Helixi | 613 – 634 | Combined sources | 22 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 3IUC | X-ray | 2.40 | A/C | 26-410 | [»] | |
| 3LDL | X-ray | 2.30 | A/B | 26-407 | [»] | |
| 3LDN | X-ray | 2.20 | A/B | 26-407 | [»] | |
| 3LDO | X-ray | 1.95 | A/B | 26-407 | [»] | |
| 3LDP | X-ray | 2.20 | A/B | 26-407 | [»] | |
| 5E84 | X-ray | 2.99 | A/B/C/D/E/F | 25-633 | [»] | |
| 5E85 | X-ray | 2.57 | A | 418-637 | [»] | |
| 5E86 | X-ray | 2.68 | A | 418-637 | [»] | |
| 5EVZ | X-ray | 1.85 | A/B | 26-407 | [»] | |
| 5EX5 | X-ray | 1.90 | A/B | 26-407 | [»] | |
| 5EXW | X-ray | 1.90 | A/B | 26-407 | [»] | |
| 5EY4 | X-ray | 1.86 | A/B | 26-407 | [»] | |
| 5F0X | X-ray | 1.60 | A/B | 26-407 | [»] | |
| 5F1X | X-ray | 1.90 | A/B | 26-407 | [»] | |
| 5F2R | X-ray | 2.15 | A/B | 26-407 | [»] | |
| ProteinModelPortali | P11021. | |||||
| SMRi | P11021. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | P11021. |
Family & Domainsi
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Motifi | 651 – 654 | Prevents secretion from ER | 4 |
Sequence similaritiesi
Belongs to the heat shock protein 70 family.Curated
Keywords - Domaini
SignalPhylogenomic databases
| eggNOGi | KOG0101. Eukaryota. COG0443. LUCA. |
| GeneTreei | ENSGT00870000136409. |
| HOGENOMi | HOG000228135. |
| HOVERGENi | HBG051845. |
| InParanoidi | P11021. |
| KOi | K09490. |
| OMAi | CVGVMQK. |
| OrthoDBi | EOG091G0352. |
| PhylomeDBi | P11021. |
| TreeFami | TF105044. |
Family and domain databases
| Gene3Di | 1.20.1270.10. 1 hit. 2.60.34.10. 1 hit. |
| InterProi | View protein in InterPro IPR018181. Heat_shock_70_CS. IPR029048. HSP70_C. IPR029047. HSP70_peptide-bd. IPR013126. Hsp_70_fam. |
| Pfami | View protein in Pfam PF00012. HSP70. 1 hit. |
| PRINTSi | PR00301. HEATSHOCK70. |
| SUPFAMi | SSF100920. SSF100920. 1 hit. SSF100934. SSF100934. 1 hit. |
| PROSITEi | View protein in PROSITE PS00014. ER_TARGET. 1 hit. PS00297. HSP70_1. 1 hit. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. |
Sequencei
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
P11021-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV
60 70 80 90 100
EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG
110 120 130 140 150
RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL
160 170 180 190 200
TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN
210 220 230 240 250
EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD
260 270 280 290 300
THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS
310 320 330 340 350
SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD
360 370 380 390 400
LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV
410 420 430 440 450
QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI
460 470 480 490 500
FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT
510 520 530 540 550
FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE
560 570 580 590 600
EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE
610 620 630 640 650
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE
KDEL
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 297 | Missing in AAA52614 (PubMed:2840249).Curated | 1 | |
| Sequence conflicti | 297 | Missing in CAA61201 (Ref. 2) Curated | 1 | |
| Sequence conflicti | 418 | D → H in AAA52614 (PubMed:2840249).Curated | 1 | |
| Sequence conflicti | 418 | D → H in CAA61201 (Ref. 2) Curated | 1 | |
| Sequence conflicti | 439 | R → S in AAA52614 (PubMed:2840249).Curated | 1 | |
| Sequence conflicti | 439 | R → S in CAA61201 (Ref. 2) Curated | 1 | |
| Sequence conflicti | 447 | K → N in AAA52614 (PubMed:2840249).Curated | 1 | |
| Sequence conflicti | 447 | K → N in CAA61201 (Ref. 2) Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_025815 | 543 | N → H1 PublicationCorresponds to variant dbSNP:rs35356639Ensembl. | 1 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M19645 Genomic DNA. Translation: AAA52614.1. X87949 mRNA. Translation: CAA61201.1. AJ271729 mRNA. Translation: CAB71335.1. AF216292 mRNA. Translation: AAF42836.1. DQ385847 Genomic DNA. Translation: ABD04090.1. AL354710 Genomic DNA. No translation available. CH471090 Genomic DNA. Translation: EAW87620.1. BC020235 mRNA. Translation: AAH20235.1. X59969 Genomic DNA. Translation: CAA42595.1. AF188611 mRNA. Translation: AAF13605.1. Sequence problems. |
| CCDSi | CCDS6863.1. |
| PIRi | A29821. |
| RefSeqi | NP_005338.1. NM_005347.4. |
| UniGenei | Hs.743241. |
Genome annotation databases
| Ensembli | ENST00000324460; ENSP00000324173; ENSG00000044574. |
| GeneIDi | 3309. |
| KEGGi | hsa:3309. |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | GRP78_HUMAN | |
| Accessioni | P11021Primary (citable) accession number: P11021 Secondary accession number(s): B0QZ61 Q9UK02 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
| Last sequence update: | July 11, 2001 | |
| Last modified: | July 5, 2017 | |
| This is version 204 of the entry and version 2 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
