CEMIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CEMIP_HUMAN
• UniProt AC: Q8WUJ3
• Protein Name: Cell migration-inducing and hyaluronan-binding protein
• Gene Name: CEMIP
• Organism: Homo sapiens (Human).
• Sequence Length: 1361
• Subcellular Localization: Nucleus. Cytoplasm. Endoplasmic reticulum. Cell membrane. Membrane, clathrin-coated pit. Secreted. Retained in the endoplasmic reticulum (ER) in a HSPA5/BIP-dependent manner. Colocalized with clathrin heavy chain/CLTC in clathrin-coated vesicles. Str
• Protein Description: Mediates depolymerization of hyaluronic acid (HA) via the cell membrane-associated clathrin-coated pit endocytic pathway. Binds to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. Involved in hyaluronan catabolism in the dermis of the skin and arthritic synovium. Positively regulates epithelial-mesenchymal transition (EMT), and hence tumor cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-dependent manner. May be involved in hearing..
• Protein Sequence: MGAAGRQDFLFKAMLTISWLTLTCFPGATSTVAAGCPDQSPELQPWNPGHDQDHHVHIGQGKTLLLTSSATVYSIHISEGGKLVIKDHDEPIVLRTRHILIDNGGELHAGSALCPFQGNFTIILYGRADEGIQPDPYYGLKYIGVGKGGALELHGQKKLSWTFLNKTLHPGGMAEGGYFFERSWGHRGVIVHVIDPKSGTVIHSDRFDTYRSKKESERLVQYLNAVPDGRILSVAVNDEGSRNLDDMARKAMTKLGSKHFLHLGFRHPWSFLTVKGNPSSSVEDHIEYHGHRGSAAARVFKLFQTEHGEYFNVSLSSEWVQDVEWTEWFDHDKVSQTKGGEKISDLWKAHPGKICNRPIDIQATTMDGVNLSTEVVYKKGQDYRFACYDRGRACRSYRVRFLCGKPVRPKLTVTIDTNVNSTILNLEDNVQSWKPGDTLVIASTDYSMYQAEEFQVLPCRSCAPNQVKVAGKPMYLHIGEEIDGVDMRAEVGLLSRNIIVMGEMEDKCYPYRNHICNFFDFDTFGGHIKFALGFKAAHLEGTELKHMGQQLVGQYPIHFHLAGDVDERGGYDPPTYIRDLSIHHTFSRCVTVHGSNGLLIKDVVGYNSLGHCFFTEDGPEERNTFDHCLGLLVKSGTLLPSDRDSKMCKMITEDSYPGYIPKPRQDCNAVSTFWMANPNNNLINCAAAGSEETGFWFIFHHVPTGPSVGMYSPGYSEHIPLGKFYNNRAHSNYRAGMIIDNGVKTTEASAKDKRPFLSIISARYSPHQDADPLKPREPAIIRHFIAYKNQDHGAWLRGGDVWLDSCRFADNGIGLTLASGGTFPYDDGSKQEIKNSLFVGESGNVGTEMMDNRIWGPGGLDHSGRTLPIGQNFPIRGIQLYDGPINIQNCTFRKFVALEGRHTSALAFRLNNAWQSCPHNNVTGIAFEDVPITSRVFFGEPGPWFNQLDMDGDKTSVFHDVDGSVSEYPGSYLTKNDNWLVRHPDCINVPDWRGAICSGCYAQMYIQAYKTSNLRMKIIKNDFPSHPLYLEGALTRSTHYQQYQPVVTLQKGYTIHWDQTAPAELAIWLINFNKGDWIRVGLCYPRGTTFSILSDVHNRLLKQTSKTGVFVRTLQMDKVEQSYPGRSHYYWDEDSGLLFLKLKAQNEREKFAFCSMKGCERIKIKALIPKNAGVSDCTATAYPKFTERAVVDVPMPKKLFGSQLKTKDHFLEVKMESSKQHFFHLWNDFAYIEVDGKKYPSSEDGIQVVVIDGNQGRVVSHTSFRNSILQGIPWQLFNYVATIPDNSIVLMASKGRYVSRGPWTRVLEKLGADRGLKLKEQMAFVGFKGSFRPIWVTLDTEDHKAKIFQVVPIPVVKKKKL

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
119	N-linked_Glycosylation	ALCPFQGNFTIILYG EECCCCCCEEEEEEE		UniProtKB CARBOHYD
142	Phosphorylation	DPYYGLKYIGVGKGG CCCCCCEEEEECCCC		17192257
165	N-linked_Glycosylation	KLSWTFLNKTLHPGG EEEEEECCCCCCCCC		UniProtKB CARBOHYD
167	Phosphorylation	SWTFLNKTLHPGGMA EEEECCCCCCCCCHH		-
233	Phosphorylation	VPDGRILSVAVNDEG CCCCCEEEEEECCCC		-
241	Phosphorylation	VAVNDEGSRNLDDMA EEECCCCCCCHHHHH		-
312	N-linked_Glycosylation	TEHGEYFNVSLSSEW CCCCCEEEEEECCCE		UniProtKB CARBOHYD
333	Acetylation	TEWFDHDKVSQTKGG HHCCCCCCCCCCCCC		20167786
348	Acetylation	EKISDLWKAHPGKIC CCHHHHHHHCCCCCC		20167786
364	Phosphorylation	RPIDIQATTMDGVNL CCCCEEEECCCCCCC		25072903
365	Phosphorylation	PIDIQATTMDGVNLS CCCEEEECCCCCCCC		25072903
370	N-linked_Glycosylation	ATTMDGVNLSTEVVY EECCCCCCCCEEEEE		UniProtKB CARBOHYD
372	Phosphorylation	TMDGVNLSTEVVYKK CCCCCCCCEEEEEEC		25072903
373	Phosphorylation	MDGVNLSTEVVYKKG CCCCCCCEEEEEECC		25072903
377	Phosphorylation	NLSTEVVYKKGQDYR CCCEEEEEECCCCEE		25072903
420	N-linked_Glycosylation	VTIDTNVNSTILNLE EEEECCCCCEEEECH		UniProtKB CARBOHYD
606	Phosphorylation	LIKDVVGYNSLGHCF EEEEECCCCCCCCEE		30576142
608	Phosphorylation	KDVVGYNSLGHCFFT EEECCCCCCCCEEEC		30576142
615	Phosphorylation	SLGHCFFTEDGPEER CCCCEEECCCCHHHC		30576142
637	Phosphorylation	GLLVKSGTLLPSDRD HHHHHCCCCCCCCCC		23403867
641	Phosphorylation	KSGTLLPSDRDSKMC HCCCCCCCCCCCCCC		23403867
645	Phosphorylation	LLPSDRDSKMCKMIT CCCCCCCCCCCCCCC		30622161
652	Phosphorylation	SKMCKMITEDSYPGY CCCCCCCCCCCCCCC		30622161
655	Phosphorylation	CKMITEDSYPGYIPK CCCCCCCCCCCCCCC		30622161
656	Phosphorylation	KMITEDSYPGYIPKP CCCCCCCCCCCCCCC		30622161
659	Phosphorylation	TEDSYPGYIPKPRQD CCCCCCCCCCCCCCC		30622161
758	Phosphorylation	KDKRPFLSIISARYS CCCCCEEHHHEECCC		-
761	Phosphorylation	RPFLSIISARYSPHQ CCEEHHHEECCCCCC		24719451
847	Phosphorylation	GESGNVGTEMMDNRI CCCCCCCCCCCCCCC		-
889	N-linked_Glycosylation	DGPINIQNCTFRKFV CCCEEEECCEEEEEE		UniProtKB CARBOHYD
921	N-linked_Glycosylation	WQSCPHNNVTGIAFE HHHCCCCCEEEEEEE		UniProtKB CARBOHYD
1011	Phosphorylation	MYIQAYKTSNLRMKI HHHHHHCCCCCEEEE		-
1012	Phosphorylation	YIQAYKTSNLRMKII HHHHHCCCCCEEEEH		-
1337	Phosphorylation	SFRPIWVTLDTEDHK CEEEEEEEEECCCCE		25690035
1340	Phosphorylation	PIWVTLDTEDHKAKI EEEEEEECCCCEEEE		25690035

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CEMIP_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 CEMIP_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CEMIP_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.