about
Collagen, type I, alpha 1Serine (or cysteine) peptidase inhibitor, clade H, member 1Collagen, type V, alpha 1Arginase 1ADAM metallopeptidase with thrombospondin type 1 motif 3Reticulocalbin 3Prolyl 3-hydroxylase family member 4 (inactive)Prolyl 3-hydroxylase 3Translocation associated membrane protein 2Arginase, liverReticulocalbin 3, EF-hand calcium binding domainProlyl 3-hydroxylase 3Prolyl 3-hydroxylase family member 4 (non-enzymatic)Translocating chain-associating membrane protein 2Collagen type I alpha 1 chainArginase 1ADAM metallopeptidase with thrombospondin type 1, motif 3Prolyl 3-hydroxylase 3Translocation associated membrane protein 2Procollagen-lysine,2-oxoglutarate 5-dioxygenase CELE_F52H3.1Prolyl 3-hydroxylase family member 4 (non-enzymatic)Collagen type I alpha 1 chainCollagen type V alpha 1 chainCollagen type I alpha 1 chainProlyl 3-hydroxylase family member 4 (inactive)Prolyl 3-hydroxylase 3Reticulocalbin 3Serpin family H member 1Reticulocalbin 3
P682
COL5A1 exon 14 splice acceptor mutation causes a functional null allele, haploinsufficiency of alpha 1(V) and abnormal heterotypic interstitial fibrils in Ehlers-Danlos syndrome IITRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesisReduced type I collagen utilization: a pathogenic mechanism in COL5A1 haplo-insufficient Ehlers-Danlos syndrome
P921
Q14881727-FB142F28-64F5-4C84-A751-52B1539E1BFAQ14911945-EEEE46D1-49C6-4862-9E43-FCE7A557992FQ15311977-A916B8F8-4F32-43D1-8CF8-7FDE12A6EB7EQ21101888-AB826D7C-93FA-42C6-9C0D-0B376ED2DCAFQ21105293-93862129-9DEF-4789-8FAD-F9A36486E2F6Q21119403-8ED39C28-4827-4753-A486-A86A8943941EQ21121380-6525E3D3-2F7B-493D-95E0-795A8EB0F3B9Q21121811-A8177F34-8762-48D4-95BB-6645943B8A8BQ21122219-ACBD5744-612E-40F6-8051-18D64BA7FE76Q21981478-411E6FFE-617F-4556-BB09-2C9A7B8A6D86Q21986382-35A7B45F-0143-41DB-AE27-5CC7620B19E1Q21986382-C865F51A-E6AB-49EC-8B46-F0F4EA16649AQ21990425-6342D15C-F5E7-430D-AB82-FF81FB04C63CQ21991608-5AB17AF8-14B1-4EAB-A46F-4534679D944AQ21992495-0429D19D-2AE0-469E-A593-6BC832506CA4Q28558630-CBC4C6F9-DC01-40AA-8D9D-76D1818D9AF4Q28561907-DD7C16E1-8DFA-40FD-96A5-6534F89809C7Q29518084-4D8D50AD-0515-4C92-8DE7-4348AA938EEBQ29518326-CC52F72A-B519-4B8E-87EE-29B54F0DFE86Q29519142-EAAA5D9F-6BC5-4378-969F-D6B1BC7859F5Q29793990-2FCAFB85-E63B-4AA3-A402-084A38C39EF1Q43374543-12EB208E-B1F1-4F51-B224-0AB85EBEE6B4Q5145884-D8C58631-A035-402B-8866-10ABAEB97729Q5145890-B071ADCB-2DD1-4DDE-9F37-7372D64F5F64Q55203554-A0813EBF-9AB6-494D-BBE8-6CCF20C56B5BQ55204037-8C292CC5-E485-4F58-8F9D-4B8623AB4A06Q55205286-C7138386-F81C-48F1-9B0C-8EFB75B550ADQ55205656-A81C0946-FF96-429D-8197-F4DF3CBF0988Q5693330-036A1A8D-91E4-4F4F-ADB3-517762CB9F7FQ57612214-B10834C5-D3C2-4DE5-9A72-C704DFC28347
P682
description
The chemical reactions and pat ...... y enriched in glycine (some re
@en
biologisch proces
@nl
name
collagen biosynthetic process
@en
type
label
collagen biosynthetic process
@en
altLabel
GO:0032964
@en
collagen anabolism
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collagen biosynthesis
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collagen formation
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collagen synthesis
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prefLabel
collagen biosynthetic process
@en
P2888
P686
GO:0032964