CILP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CILP1_HUMAN
• UniProt AC: O75339
• Protein Name: Cartilage intermediate layer protein 1
• Gene Name: CILP
• Organism: Homo sapiens (Human).
• Sequence Length: 1184
• Subcellular Localization: Secreted, extracellular space, extracellular matrix .
• Protein Description: Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage..
• Protein Sequence: MVGTKAWVFSFLVLEVTSVLGRQTMLTQSVRRVQPGKKNPSIFAKPADTLESPGEWTTWFNIDYPGGKGDYERLDAIRFYYGDRVCARPLRLEARTTDWTPAGSTGQVVHGSPREGFWCLNREQRPGQNCSNYTVRFLCPPGSLRRDTERIWSPWSPWSKCSAACGQTGVQTRTRICLAEMVSLCSEASEEGQHCMGQDCTACDLTCPMGQVNADCDACMCQDFMLHGAVSLPGGAPASGAAIYLLTKTPKLLTQTDSDGRFRIPGLCPDGKSILKITKVKFAPIVLTMPKTSLKAATIKAEFVRAETPYMVMNPETKARRAGQSVSLCCKATGKPRPDKYFWYHNDTLLDPSLYKHESKLVLRKLQQHQAGEYFCKAQSDAGAVKSKVAQLIVIASDETPCNPVPESYLIRLPHDCFQNATNSFYYDVGRCPVKTCAGQQDNGIRCRDAVQNCCGISKTEEREIQCSGYTLPTKVAKECSCQRCTETRSIVRGRVSAADNGEPMRFGHVYMGNSRVSMTGYKGTFTLHVPQDTERLVLTFVDRLQKFVNTTKVLPFNKKGSAVFHEIKMLRRKKPITLEAMETNIIPLGEVVGEDPMAELEIPSRSFYRQNGEPYIGKVKASVTFLDPRNISTATAAQTDLNFINDEGDTFPLRTYGMFSVDFRDEVTSEPLNAGKVKVHLDSTQVKMPEHISTVKLWSLNPDTGLWEEEGDFKFENQRRNKREDRTFLVGNLEIRERRLFNLDVPESRRCFVKVRAYRSERFLPSEQIQGVVISVINLEPRTGFLSNPRAWGRFDSVITGPNGACVPAFCDDQSPDAYSAYVLASLAGEELQAVESSPKFNPNAIGVPQPYLNKLNYRRTDHEDPRVKKTAFQISMAKPRPNSAEESNGPIYAFENLRACEEAPPSAAHFRFYQIEGDRYDYNTVPFNEDDPMSWTEDYLAWWPKPMEFRACYIKVKIVGPLEVNVRSRNMGGTHRQTVGKLYGIRDVRSTRDRDQPNVSAACLEFKCSGMLYDQDRVDRTLVKVIPQGSCRRASVNPMLHEYLVNHLPLAVNNDTSEYTMLAPLDPLGHNYGIYTVTDQDPRTAKEIALGRCFDGTSDGSSRIMKSNVGVALTFNCVERQVGRQSAFQYLQSTPAQSPAAGTVQGRVPSRRQQRASRGGQRQGGVVASLRFPRVAQQPLIN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Phosphorylation	TSVLGRQTMLTQSVR HHHHCCHHHHHHHHH	16.88	23403867
27	Phosphorylation	LGRQTMLTQSVRRVQ HCCHHHHHHHHHCCC	14.15	-
29	Phosphorylation	RQTMLTQSVRRVQPG CHHHHHHHHHCCCCC	16.62	-
96	O-linked_Glycosylation	PLRLEARTTDWTPAG CEEEEEEECCCCCCC	35.83	55834997
97	O-linked_Glycosylation	LRLEARTTDWTPAGS EEEEEEECCCCCCCC	24.80	55835003
105	O-linked_Glycosylation	DWTPAGSTGQVVHGS CCCCCCCCCCEEECC	30.62	55835009
129	N-linked_Glycosylation	REQRPGQNCSNYTVR CCCCCCCCCCCEEEE	36.78	UniProtKB CARBOHYD
132	N-linked_Glycosylation	RPGQNCSNYTVRFLC CCCCCCCCEEEEEEC	38.40	UniProtKB CARBOHYD
273	Phosphorylation	GLCPDGKSILKITKV EECCCCCCEEEEEEE	38.39	24719451
288	Phosphorylation	KFAPIVLTMPKTSLK EECCEEEECCCCCCC	22.12	-
292	Phosphorylation	IVLTMPKTSLKAATI EEEECCCCCCCEEEE	33.16	30576142
293	Phosphorylation	VLTMPKTSLKAATIK EEECCCCCCCEEEEE	33.72	28555341
298	Phosphorylation	KTSLKAATIKAEFVR CCCCCEEEEEEEEEE	28.06	-
310	Phosphorylation	FVRAETPYMVMNPET EEECCCCEEEECHHH	15.12	25884760
341	Phosphorylation	GKPRPDKYFWYHNDT CCCCCCCEEEECCCC	13.51	-
346	N-linked_Glycosylation	DKYFWYHNDTLLDPS CCEEEECCCCCCCHH	28.41	9722584
348	Phosphorylation	YFWYHNDTLLDPSLY EEEECCCCCCCHHHH	34.24	-
360	Ubiquitination	SLYKHESKLVLRKLQ HHHHHCHHHHHHHHH	39.36	29967540
374	Phosphorylation	QQHQAGEYFCKAQSD HHHHCCCCCHHHHCC	17.23	-
400	Phosphorylation	IVIASDETPCNPVPE EEEECCCCCCCCCCH	37.83	21060948
420	N-linked_Glycosylation	LPHDCFQNATNSFYY CCCHHHCCCCCCCCC	28.60	UniProtKB CARBOHYD
550	N-linked_Glycosylation	DRLQKFVNTTKVLPF HHHHHHHCCCCEECC	45.20	UniProtKB CARBOHYD
551	Phosphorylation	RLQKFVNTTKVLPFN HHHHHHCCCCEECCC	23.77	-
552	Phosphorylation	LQKFVNTTKVLPFNK HHHHHCCCCEECCCC	17.60	-
631	N-linked_Glycosylation	VTFLDPRNISTATAA EEEECCCCCCCCCEE	37.64	UniProtKB CARBOHYD
694	Phosphorylation	VKMPEHISTVKLWSL CCCCCCEEEEEEEEE	29.11	26437602
755	Methylation	ESRRCFVKVRAYRSE HHHEEEEEEEEEECC	13.02	-
755	Trimethylation	ESRRCFVKVRAYRSE HHHEEEEEEEEEECC	13.02	-
784	Phosphorylation	VINLEPRTGFLSNPR EEECCCCCCCCCCCC	42.89	-
1000	N-linked_Glycosylation	TRDRDQPNVSAACLE CCCCCCCCCCHHHEE	34.44	UniProtKB CARBOHYD
1056	N-linked_Glycosylation	HLPLAVNNDTSEYTM HCCEEECCCCCCEEE	47.54	UniProtKB CARBOHYD
1135	Phosphorylation	SAFQYLQSTPAQSPA HHHHHHHCCCCCCCC	33.49	-
1135	O-linked_Glycosylation	SAFQYLQSTPAQSPA HHHHHHHCCCCCCCC	33.49	55827085
1136	Phosphorylation	AFQYLQSTPAQSPAA HHHHHHCCCCCCCCC	15.07	-
1136	O-linked_Glycosylation	AFQYLQSTPAQSPAA HHHHHHCCCCCCCCC	15.07	55827091
1140	O-linked_Glycosylation	LQSTPAQSPAAGTVQ HHCCCCCCCCCCCCC	20.72	46187943
1140	Phosphorylation	LQSTPAQSPAAGTVQ HHCCCCCCCCCCCCC	20.72	-
1145	Phosphorylation	AQSPAAGTVQGRVPS CCCCCCCCCCCCCCC	12.62	-
1145	O-linked_Glycosylation	AQSPAAGTVQGRVPS CCCCCCCCCCCCCCC	12.62	55827103

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CILP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CILP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CILP1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CILP1_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 603932: Intervertebral disc disease (IDD)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.