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Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]

 NOTC1_CRIGR             Reviewed;        2527 AA.
G3I6Z6;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 2.
12-SEP-2018, entry version 43.
RecName: Full=Neurogenic locus notch homolog protein 1;
Short=Notch 1;
Contains:
RecName: Full=Notch 1 extracellular truncation;
Short=NEXT;
Contains:
RecName: Full=Notch 1 intracellular domain;
Short=NICD;
Flags: Precursor;
Name=NOTCH1;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21804562; DOI=10.1038/nbt.1932;
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
Quake S.R., Famili I., Palsson B.O., Wang J.;
"The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
line.";
Nat. Biotechnol. 29:735-741(2011).
[2]
GLYCOSYLATION.
PubMed=10734111; DOI=10.1074/jbc.275.13.9604;
Moloney D.J., Shair L.H., Lu F.M., Xia J., Locke R., Matta K.L.,
Haltiwanger R.S.;
"Mammalian Notch1 is modified with two unusual forms of O-linked
glycosylation found on epidermal growth factor-like modules.";
J. Biol. Chem. 275:9604-9611(2000).
-!- FUNCTION: Functions as a receptor for membrane-bound ligands
Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate
cell-fate determination. Upon ligand activation through the
released notch intracellular domain (NICD) it forms a
transcriptional activator complex with RBPJ/RBPSUH and activates
genes of the enhancer of split locus. Affects the implementation
of differentiation, proliferation and apoptotic programs. Involved
in angiogenesis; negatively regulates endothelial cell
proliferation and migration and angiogenic sprouting. Involved in
the maturation of both CD4(+) and CD8(+) cells in the thymus.
Important for follicular differentiation and possibly cell fate
selection within the follicle. During cerebellar development,
functions as a receptor for neuronal DNER and is involved in the
differentiation of Bergmann glia. Represses neuronal and myogenic
differentiation. May play an essential role in postimplantation
development, probably in some aspect of cell specification and/or
differentiation. May be involved in mesoderm development, somite
formation and neurogenesis. May enhance HIF1A function by
sequestering HIF1AN away from HIF1A (By similarity). Required for
the THBS4 function in regulating protective astrogenesis from the
subventricular zone (SVZ) niche after injury. Involved in
determination of left/right symmetry by modulating the balance
between motile and immotile (sensory) cilia at the left-right
organiser (LRO) (By similarity). {ECO:0000250|UniProtKB:Q01705}.
-!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-
terminal fragment N(EC) which are probably linked by disulfide
bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also
interacts with MAML1, MAML2 and MAML3 which act as transcriptional
coactivators for NOTCH1. Notch 1 intracellular domain interacts
with SNW1; the interaction involves multimerized NOTCH1 NICD and
is implicated in a formation of an intermediate preactivation
complex which associates with DNA-bound CBF-1/RBPJ. The activated
membrane-bound form interacts with AAK1 which promotes NOTCH1
stabilization. Forms a trimeric complex with FBXW7 and SGK1.
Interacts with HIF1AN. HIF1AN negatively regulates the function of
notch intracellular domain (NICD), accelerating myogenic
differentiation. Interacts (via NICD) with SNAI1 (via zinc
fingers); the interaction induces SNAI1 degradation via MDM2-
mediated ubiquitination and inhibits SNAI1-induced cell invasion.
Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6;
the interaction decreases MAML1 recruitment by NOTCH1 NICD on
target genes DNA and inhibits NOTCH1 transcractivation activity
(By similarity). Interacts with THBS4 (By similarity). Interacts
(via the EGF-like repeat region) with NOV (via CTCK domain).
Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and
MNNL domains). Interacts with ZMIZ1. Interacts (via NICD domain)
with MEGF10 (via the cytoplasmic domain). Interacts with DLL1 and
JAG1 (By similarity). Interacts (via NICD domain) with PRAG1 (By
similarity). Forms a complex with PRAG1, N1ICD and MAML1, in a
MAML1-dependent manner (By similarity).
{ECO:0000250|UniProtKB:P46531, ECO:0000250|UniProtKB:Q01705,
ECO:0000250|UniProtKB:Q07008}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q01705}.
-!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus
{ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical
processing NICD is translocated to the nucleus. Nuclear location
may require MEGF10. {ECO:0000250|UniProtKB:Q01705}.
-!- PTM: Synthesized in the endoplasmic reticulum as an inactive form
which is proteolytically cleaved by a furin-like convertase in the
trans-Golgi network before it reaches the plasma membrane to yield
an active, ligand-accessible form. Cleavage results in a C-
terminal fragment N(TM) and a N-terminal fragment N(EC). Following
ligand binding, it is cleaved by ADAM17 to yield a membrane-
associated intermediate fragment called notch extracellular
truncation (NEXT). Following endocytosis, this fragment is then
cleaved by presenilin dependent gamma-secretase to release a
notch-derived peptide containing the intracellular domain (NICD)
from the membrane. {ECO:0000250|UniProtKB:Q01705}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- PTM: O-linked glycosylation by GALNT11 is involved in
determination of left/right symmetry: glycosylation promotes
activation of NOTCH1, possibly by promoting cleavage by ADAM17,
modulating the balance between motile and immotile (sensory) cilia
at the left-right organiser (LRO) (By similarity). O-glycosylated
on the EGF-like domains (PubMed:10734111). Contains both O-linked
fucose and O-linked glucose in the EGF-like domains 11, 12 and 13,
which are interacting with the residues on DLL4. MFNG-, RFNG- and
LFNG-mediated modification of O-fucose residues at specific EGF-
like domains results in inhibition of its activation by JAG1 and
enhancement of its activation by DLL1 via an increased binding to
DLL1 (By similarity). {ECO:0000250|UniProtKB:P46531,
ECO:0000250|UniProtKB:Q01705, ECO:0000250|UniProtKB:Q07008,
ECO:0000269|PubMed:10734111}.
-!- PTM: Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination
by ITCH; promotes the lysosomal degradation of non-activated
internalized NOTCH1. Monoubiquitination at Lys-1765 is required
for activation by gamma-secretase cleavage, it promotes
interaction with AAK1, which stabilizes it. Deubiquitination by
EIF3F is necessary for nuclear import of activated Notch.
{ECO:0000250|UniProtKB:Q01705}.
-!- PTM: Hydroxylated at Asn-1961 by HIF1AN. Hydroxylated at Asn-2028
by HIF1AN (By similarity). Hydroxylation reduces affinity for
HI1AN and may thus indirectly modulate negative regulation of NICD
(By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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EMBL; JH001398; EGW12778.1; -; Genomic_DNA.
RefSeq; XP_003510910.1; XM_003510862.3.
PRIDE; G3I6Z6; -.
GeneID; 100761880; -.
KEGG; cge:100761880; -.
CTD; 4851; -.
InParanoid; G3I6Z6; -.
KO; K02599; -.
Proteomes; UP000001075; Unassembled WGS sequence.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
GO; GO:0061314; P:Notch signaling involved in heart development; ISS:UniProtKB.
GO; GO:0050793; P:regulation of developmental process; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR024600; DUF3454_notch.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR008297; Notch.
InterPro; IPR035993; Notch-like_dom_sf.
InterPro; IPR022362; Notch_1.
InterPro; IPR000800; Notch_dom.
InterPro; IPR010660; Notch_NOD_dom.
InterPro; IPR011656; Notch_NODP_dom.
Pfam; PF12796; Ank_2; 2.
Pfam; PF11936; DUF3454; 1.
Pfam; PF00008; EGF; 20.
Pfam; PF07645; EGF_CA; 5.
Pfam; PF12661; hEGF; 3.
Pfam; PF06816; NOD; 1.
Pfam; PF07684; NODP; 1.
Pfam; PF00066; Notch; 3.
PIRSF; PIRSF002279; Notch; 1.
PRINTS; PR01452; LNOTCHREPEAT.
PRINTS; PR01984; NOTCH1.
SMART; SM00248; ANK; 6.
SMART; SM01334; DUF3454; 1.
SMART; SM00181; EGF; 36.
SMART; SM00179; EGF_CA; 33.
SMART; SM00004; NL; 3.
SMART; SM01338; NOD; 1.
SMART; SM01339; NODP; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57184; SSF57184; 5.
SUPFAM; SSF90193; SSF90193; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
PROSITE; PS00010; ASX_HYDROXYL; 22.
PROSITE; PS00022; EGF_1; 35.
PROSITE; PS01186; EGF_2; 28.
PROSITE; PS50026; EGF_3; 36.
PROSITE; PS01187; EGF_CA; 21.
PROSITE; PS50258; LNR; 3.
1: Evidence at protein level;
Activator; Angiogenesis; ANK repeat; Calcium; Cell membrane;
Complete proteome; Developmental protein; Differentiation;
Disulfide bond; EGF-like domain; Glycoprotein; Hydroxylation;
Isopeptide bond; Membrane; Metal-binding; Notch signaling pathway;
Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 36 {ECO:0000255}.
CHAIN 37 2527 Neurogenic locus notch homolog protein 1.
/FTId=PRO_0000424013.
CHAIN 1727 2527 Notch 1 extracellular truncation.
{ECO:0000250}.
/FTId=PRO_0000424014.
CHAIN 1760 2527 Notch 1 intracellular domain.
{ECO:0000250}.
/FTId=PRO_0000424015.
TOPO_DOM 37 1741 Extracellular. {ECO:0000255}.
TRANSMEM 1742 1762 Helical. {ECO:0000255}.
TOPO_DOM 1763 2527 Cytoplasmic. {ECO:0000255}.
DOMAIN 75 115 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 118 155 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 156 192 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 194 232 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 234 271 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 273 309 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 311 349 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 351 387 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 388 426 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 428 466 EGF-like 10; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 468 504 EGF-like 11; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 506 542 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 544 580 EGF-like 13; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 582 617 EGF-like 14; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 619 655 EGF-like 15; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 657 692 EGF-like 16; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 694 730 EGF-like 17; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 732 767 EGF-like 18; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 769 805 EGF-like 19. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 807 843 EGF-like 20; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 845 883 EGF-like 21. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 885 921 EGF-like 22; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 923 959 EGF-like 23. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 961 997 EGF-like 24; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 999 1035 EGF-like 25. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1037 1073 EGF-like 26. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1075 1111 EGF-like 27. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1113 1159 EGF-like 28. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1161 1197 EGF-like 29. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1199 1235 EGF-like 30; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1237 1281 EGF-like 31; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1283 1321 EGF-like 32. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1323 1362 EGF-like 33. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1364 1400 EGF-like 34. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1403 1442 EGF-like 35. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1465 1505 LNR 1.
REPEAT 1506 1547 LNR 2.
REPEAT 1548 1587 LNR 3.
REPEAT 1933 1962 ANK 1.
REPEAT 1966 1996 ANK 2.
REPEAT 2000 2029 ANK 3.
REPEAT 2033 2062 ANK 4.
REPEAT 2066 2095 ANK 5.
REGION 436 437 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
REGION 464 468 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
REGION 1953 1961 HIF1AN-binding. {ECO:0000250}.
REGION 2020 2028 HIF1AN-binding. {ECO:0000250}.
METAL 448 448 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 451 451 Calcium 1; via amide nitrogen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 468 468 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 469 469 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 471 471 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 485 485 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 486 486 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 506 506 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 507 507 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 509 509 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 523 523 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 524 524 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 1473 1473 Calcium 4; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00525}.
METAL 1476 1476 Calcium 4. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 1491 1491 Calcium 4. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 1494 1494 Calcium 4. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
SITE 485 485 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
SITE 1670 1671 Cleavage; by furin-like protease.
{ECO:0000250|UniProtKB:Q01705}.
SITE 1726 1727 Cleavage; by ADAM17.
{ECO:0000250|UniProtKB:Q01705}.
MOD_RES 1867 1867 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01705}.
MOD_RES 1961 1961 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000250}.
MOD_RES 2028 2028 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 81 81 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 89 89 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 132 132 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 162 162 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 210 210 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 248 248 O-linked (Fuc...) threonine; alternate.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 248 248 O-linked (GalNAc...) threonine;
alternate.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 327 327 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 357 357 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 365 365 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 394 394 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 451 451 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 474 474 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 482 482 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 512 512 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 550 550 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 625 625 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 633 633 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 663 663 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 708 708 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 738 738 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 775 775 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 783 783 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 800 800 O-linked (GlcNAc) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 813 813 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 821 821 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 904 904 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 916 916 O-linked (GlcNAc) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 937 937 O-linked (Fuc) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 967 967 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 975 975 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1013 1013 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1043 1043 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1051 1051 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1081 1081 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1175 1175 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1195 1195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1205 1205 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1213 1213 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1257 1257 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1289 1289 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1378 1378 O-linked (Fuc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1395 1395 O-linked (GlcNAc...) threonine.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1418 1418 O-linked (Fuc...) threonine; alternate.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1418 1418 O-linked (GalNAc...) threonine;
alternate.
{ECO:0000250|UniProtKB:Q01705}.
CARBOHYD 1505 1505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1603 1603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1731 1731 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P46531}.
DISULFID 40 53 {ECO:0000250}.
DISULFID 47 62 {ECO:0000250}.
DISULFID 64 73 {ECO:0000250}.
DISULFID 79 90 {ECO:0000250}.
DISULFID 84 103 {ECO:0000250}.
DISULFID 105 114 {ECO:0000250}.
DISULFID 122 133 {ECO:0000250}.
DISULFID 127 143 {ECO:0000250}.
DISULFID 145 154 {ECO:0000250}.
DISULFID 160 171 {ECO:0000250}.
DISULFID 165 180 {ECO:0000250}.
DISULFID 182 191 {ECO:0000250}.
DISULFID 198 211 {ECO:0000250}.
DISULFID 205 220 {ECO:0000250}.
DISULFID 222 231 {ECO:0000250}.
DISULFID 238 249 {ECO:0000250}.
DISULFID 243 259 {ECO:0000250}.
DISULFID 261 270 {ECO:0000250}.
DISULFID 277 288 {ECO:0000250}.
DISULFID 282 297 {ECO:0000250}.
DISULFID 299 308 {ECO:0000250}.
DISULFID 315 328 {ECO:0000250}.
DISULFID 322 337 {ECO:0000250}.
DISULFID 339 348 {ECO:0000250}.
DISULFID 355 366 {ECO:0000250}.
DISULFID 360 375 {ECO:0000250}.
DISULFID 377 386 {ECO:0000250}.
DISULFID 392 403 {ECO:0000250}.
DISULFID 397 414 {ECO:0000250}.
DISULFID 416 425 {ECO:0000250}.
DISULFID 432 445 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 439 454 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 456 465 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 472 483 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 477 492 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 494 503 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 510 521 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 515 530 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 532 541 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 548 559 {ECO:0000250}.
DISULFID 553 568 {ECO:0000250}.
DISULFID 570 579 {ECO:0000250}.
DISULFID 586 596 {ECO:0000250}.
DISULFID 591 605 {ECO:0000250}.
DISULFID 607 616 {ECO:0000250}.
DISULFID 623 634 {ECO:0000250}.
DISULFID 628 643 {ECO:0000250}.
DISULFID 645 654 {ECO:0000250}.
DISULFID 661 671 {ECO:0000250}.
DISULFID 666 680 {ECO:0000250}.
DISULFID 682 691 {ECO:0000250}.
DISULFID 698 709 {ECO:0000250}.
DISULFID 703 718 {ECO:0000250}.
DISULFID 720 729 {ECO:0000250}.
DISULFID 736 746 {ECO:0000250}.
DISULFID 741 755 {ECO:0000250}.
DISULFID 757 766 {ECO:0000250}.
DISULFID 773 784 {ECO:0000250}.
DISULFID 778 793 {ECO:0000250}.
DISULFID 795 804 {ECO:0000250}.
DISULFID 811 822 {ECO:0000250}.
DISULFID 816 831 {ECO:0000250}.
DISULFID 833 842 {ECO:0000250}.
DISULFID 849 860 {ECO:0000250}.
CROSSLNK 1765 1765 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q01705}.
SEQUENCE 2527 AA; 270858 MW; 5E20EC5287850426 CRC64;
MGRSDSRAGA LLEGGCEQNI DPRRAAHCHH PRLATSSLRC SQPSGTCLNG GRCEVANGTE
ACVCSGPFVG QRCQDPNPCL STPCKNAGTC HVVEHGGTVN YACSCPLGFS GPLCLTPLDN
ACLANPCRNG GTCDLLTLTE YKCRCPPGWS GKSCQQADPC ASNPCANGGQ CLPFESSYIC
GCPPGFHGPT CRQDVNECSQ NPGLCRHGGT CHNEIGSYRC VCRATHTGPH CELPYVPCSP
SPCQNGGTCR PTGDTTHECA CLPGFAGQNC EENVDDCPGN NCKNGGACVD GVNTYNCRCP
PEWTGQYCTE DVDECQLMPN ACQNGGTCHN THGGYNCVCV NGWTGEDCSE NIDDCASAAC
FQGATCHDRV ASFYCECPHG RTGLLCHLND ACISNPCNEG SNCDTNPVNG KAICTCPSGY
TGPACSQDVD ECALGANPCE HAGKCLNTLG SFECQCLQGY TGPRCEIDVN ECISNPCQND
ATCLDQIGEF QCICMPGYEG VYCEINTDEC ASSPCLHNGH CMDKINEFLC QCPKGFSGHL
CQYDVDECAS TPCKNGAKCL DGPNTYTCVC TEGYTGTHCE VDIDECDPDP CHYGFCKDGV
ATFTCLCQPG YTGHHCETNI NECHSQPCRH GGTCQDRDNS YLCLCLKGTT GPNCEINLDD
CASNPCDSGT CLDKIDGYEC ACEPGYTGSM CNVNIDECAG SPCHNGGTCE DGIAGFTCRC
PEGYHDPTCL SEVNECNSNP CIHGACRDGL NGYKCDCAPG WSGTNCDINN NECESNPCVN
GGTCKDMTSG YVCTCREGFS GPNCQTNINE CASNPCLNQG TCIDDVAGYK CNCPLPYTGA
TCEVVLAPCA TSPCKNSGVC KESEDYESFS CVCPTGWQGQ TCEIDINECV KSPCRHGASC
QNTNGSYRCL CQAGYTGRNC ESDIDDCRPN PCHNGGSCTD GINMAFCDCL PGFQGAFCEE
DINECASNPC RNGANCTDCV DSYTCTCPAG FNGIHCENNT PDCTESSCFN GGTCVDGINS
FTCLCPPGFT GSYCQYDVNE CDSRPCLHGG TCQDSYGTYK CTCPQGYTGL NCQNLVHWCD
SAPCKNGGKC WQTNTQYHCE CRSGWTGFNC DVLSVSCEVA AQKRGIDVTL LCQHGGLCVD
EEDKHYCHCQ AGYTGSYCED EVDECSPNPC QNGATCTDYL GGFSCKCVAG YHGSNCSEEI
NECLSQPCQN GGTCIDLTNT YKCSCPRGTQ GVHCEINVDD CHPHLDPASR SPKCFNNGTC
VDQVGGYSCT CPPGFVGERC EGDINECLSN PCDPRGTQDC VQRVNDFHCE CRAGHTGRRC
ESVINGCRGK PCKNGGVCAV ASNTARGFIC RCPAGFEGAT CENDARTCGS LRCLNGGTCI
SGPRSPTCLC LGSFTGPECQ FPASSPCVGS NPCYNQGTCE PTSESPFYRC LCPAKFNGLL
CHILDYSFTG GAGRDIPPPQ IEEACELPEC QEDAGNKVCN LQCNNHACGW DGGDCSLNFN
DPWKNCTQSL QCWKYFSDGH CDSQCNSASC LFDGFDCQRT EGQCNPLYDQ YCKDHFSDGH
CDQGCNSAEC DWDGLDCADH VPERLAAGTL VLVVLLPPEQ LRNNSFHFLR ELSHVLHTNV
VFKRDAEGQQ MIFPYYGHEE ELRKHPIKRS AVGWTTSSLL PSTNGGRQRR ELDPMDIRGS
IVYLEIDNRQ CVQSSSQCFQ SATDVAAFLG ALASLGNLNI PYKIEAVKSE TVEPPLPSQL
HLMYLAAAAF VLLFFVGCGV LLSRKRRRQH GQLWFPEGFK VSEASKKKRR EPLGEDSVGL
KPLKNASDGA LMDDNQNEWG DEDLETKKFR FEEPVVVPDL DDQTDHRQWT QQHLDAADLR
MSAMAPTPPQ GEVDADCMDV NVRGPDGFTP LMIASCSGGG LETGNSEEEE DAPAVISDFI
YQGASLHNQT DRTGETALHL AARYSRSDAA KRLLEASADA NIQDNMGRTP LHAAVSADAQ
GVFQILLRNR ATDLDARMHD GTTPLILAAR LAVEGMLEDL INSHADVNAV DDLGKSALHW
AAAVNNVDAA VVLLKNGANK DMQNNKEETP LFLAAREGSY ETAKVLLDHF ANRDITDHMD
RLPRDIAQER MHHDIVRLLD EYNLVRSPQL HGTALGGTPT LSPTLCSPNG YLGNLKSATQ
GKKARKPSTK GLACGSKEAK DLKARRKKSQ DGKGCLLDSS SMLSPVDSLE SPHGYLSDVA
SPPLLPSPFQ QSPSMPLSHL PGMPDTHLGI SHLNVAAKPE MAALAGSSRL AFEPPPPRLP
HLPVASSAST VLSTNGSXGE EEWLAPSQYN PLRPGVASGT LSTQAAGLQH GMMGPLHSSL
STNTLSPMIY QGLPNTRLAT QPHLVQTQQV QPQNLQIQPQ NLQPPSQPHL SVSSAANGHL
GRSFLGGEHS QADVQPLGPS SLPVHTILPQ ESQALPTSLP SSMVPPMTTT QFLTPPSQHS
YSSSPVDNTP SHQLQVPEHP FLTPSPESPD QWSSSSPHSN ISDWSEGISS PPTSMPSQIT
HIPEAFK


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