|
|
1)
|
chain |
A |
residue |
429-440 |
type |
prosite |
sequence |
CINTLGSFECQC
|
description |
ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC
|
source |
prosite : PS00010
|
|
2)
|
chain |
A |
residue |
467-478 |
type |
prosite |
sequence |
CLDQIGEFQCIC
|
description |
ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC
|
source |
prosite : PS00010
|
|
3)
|
chain |
A |
residue |
505-516 |
type |
prosite |
sequence |
CLDKINEFQCEC
|
description |
ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC
|
source |
prosite : PS00010
|
|
4)
|
chain |
A |
residue |
438-449 |
type |
prosite |
sequence |
CQCLQGYTGPRC
|
description |
EGF_1 EGF-like domain signature 1. CqClqGytGPrC
|
source |
prosite : PS00022
|
|
5)
|
chain |
A |
residue |
476-487 |
type |
prosite |
sequence |
CICMPGYEGVHC
|
description |
EGF_1 EGF-like domain signature 1. CqClqGytGPrC
|
source |
prosite : PS00022
|
|
6)
|
chain |
A |
residue |
514-525 |
type |
prosite |
sequence |
CECPTGFTGHLC
|
description |
EGF_1 EGF-like domain signature 1. CqClqGytGPrC
|
source |
prosite : PS00022
|
|
7)
|
chain |
A |
residue |
438-449 |
type |
prosite |
sequence |
CQCLQGYTGPRC
|
description |
EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C
|
source |
prosite : PS01186
|
|
8)
|
chain |
A |
residue |
476-487 |
type |
prosite |
sequence |
CICMPGYEGVHC
|
description |
EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C
|
source |
prosite : PS01186
|
|
9)
|
chain |
A |
residue |
514-525 |
type |
prosite |
sequence |
CECPTGFTGHLC
|
description |
EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C
|
source |
prosite : PS01186
|
|
10)
|
chain |
A |
residue |
412-438 |
type |
prosite |
sequence |
DVDECSLGANPCEHAGKCINTLGSFEC
|
description |
EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC
|
source |
prosite : PS01187
|
|
11)
|
chain |
A |
residue |
452-476 |
type |
prosite |
sequence |
DVNECVSNPCQNDATCLDQIGEFQC
|
description |
EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC
|
source |
prosite : PS01187
|
|
12)
|
chain |
A |
residue |
490-514 |
type |
prosite |
sequence |
NTDECASSPCLHNGRCLDKINEFQC
|
description |
EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC
|
source |
prosite : PS01187
|
|
13)
|
chain |
A |
residue |
432 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
14)
|
chain |
A |
residue |
493 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
A |
residue |
507 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
A |
residue |
508 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
435 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
A |
residue |
452 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
19)
|
chain |
A |
residue |
453 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
20)
|
chain |
A |
residue |
455 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
21)
|
chain |
A |
residue |
469 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
22)
|
chain |
A |
residue |
470 |
type |
BINDING |
sequence |
Q
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
23)
|
chain |
A |
residue |
490 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
24)
|
chain |
A |
residue |
491 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
25)
|
chain |
A |
residue |
469 |
type |
SITE |
sequence |
D
|
description |
Interaction with DLL4 => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
26)
|
chain |
A |
residue |
435 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (Glc...) serine => ECO:0000269|PubMed:30127001
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
27)
|
chain |
A |
residue |
458 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
28)
|
chain |
A |
residue |
496 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
29)
|
chain |
A |
residue |
466 |
type |
CARBOHYD |
sequence |
T
|
description |
O-linked (Fuc...) threonine => ECO:0000250|UniProtKB:Q07008
|
source |
Swiss-Prot : SWS_FT_FI5
|
|