CIB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CIB1_HUMAN
• UniProt AC: Q99828
• Protein Name: Calcium and integrin-binding protein 1
• Gene Name: CIB1
• Organism: Homo sapiens (Human).
• Sequence Length: 191
• Subcellular Localization: Membrane; Lipid-anchor. Cell membrane, sarcolemma. Cell membrane. Apical cell membrane. Cell projection, ruffle membrane. Cell projection, filopodium tip. Cell projection, growth cone. Cell projection, lamellipodium. Cytoplasm. Cytoplasm, cytoskeleton. Cy
• Protein Description: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin-mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation-dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells.; Isoform 2: Plays a regulatory role in angiogenesis and tumor growth by mediating PKD/PRKD2-induced vascular endothelial growth factor A (VEGFA) secretion..
• Protein Sequence: MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEQRSVESSLRAQVPFEQILSLPELKANPFKERICRVFSTSPAKDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSRLVNCLTGEGEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL

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
2	N-myristoyl glycine	------MGGSGSRLS ------CCCCCCHHC	38.69	-
2	Myristoylation	------MGGSGSRLS ------CCCCCCHHC	38.69	10366599
10	Ubiquitination	GSGSRLSKELLAEYQ CCCCHHCHHHHHHHC	57.90	21890473
16	Phosphorylation	SKELLAEYQDLTFLT CHHHHHHHCCHHHHC	11.17	-
24	Ubiquitination	QDLTFLTKQEILLAH CCHHHHCHHHHHHHH	48.34	21890473
65	Ubiquitination	ILSLPELKANPFKER HHCCHHHCCCCCHHH	44.44	21890473
70	Ubiquitination	ELKANPFKERICRVF HHCCCCCHHHHHHHH	47.54	-
78	Phosphorylation	ERICRVFSTSPAKDS HHHHHHHCCCCCCCC	25.72	23503467
118 (in isoform 2)	Phosphorylation	-	55.74	23503467
150	Ubiquitination	RLSASEMKQLIDNIL CCCHHHHHHHHHHHH	37.59	-
167	Phosphorylation	SDIDRDGTINLSEFQ CCCCCCCCCCHHHHH	15.81	26074081
171	Phosphorylation	RDGTINLSEFQHVIS CCCCCCHHHHHHHHH	31.70	26074081
178	Phosphorylation	SEFQHVISRSPDFAS HHHHHHHHCCCCHHH	26.14	26074081
180	Phosphorylation	FQHVISRSPDFASSF HHHHHHCCCCHHHHC	23.25	25159151
185	Phosphorylation	SRSPDFASSFKIVL- HCCCCHHHHCCCCC-	35.98	25159151
186	Phosphorylation	RSPDFASSFKIVL-- CCCCHHHHCCCCC--	27.42	25159151
188	Ubiquitination	PDFASSFKIVL---- CCHHHHCCCCC----	33.58	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
78	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
118	S	Phosphorylation	Phosphorylation of isoform 2 at Ser-118 by PRKD2 increases its ability to stimulate tumor angiogenesis.	23503467

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CIB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FAK1_HUMAN	PTK2	physical	12881299
PLK3_HUMAN	PLK3	physical	11039900
RAC3_HUMAN	RAC3	physical	11756406
UBR5_HUMAN	UBR5	physical	12011095
PSN2_HUMAN	PSEN2	physical	10366599
PSN2_HUMAN	PSEN2	genetic	10366599
PRKDC_HUMAN	PRKDC	physical	9372844
PAX3_MOUSE	Pax3	physical	11997098
TERT_HUMAN	TERT	physical	20959453
TERT_HUMAN	TERT	physical	15190070
PRKDC_HUMAN	PRKDC	physical	15190070
ITA2B_HUMAN	ITGA2B	physical	24163826
ITA5_HUMAN	ITGA5	physical	24163826
ITB3_HUMAN	ITGB3	physical	24163826
M3K5_HUMAN	MAP3K5	physical	19805025

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.

Related Literatures of Post-Translational Modification

Myristoylation

"A myristoylated calcium-binding protein that preferentially interactswith the Alzheimer's disease presenilin 2 protein.";
Stabler S.M., Ostrowski L.L., Janicki S.M., Monteiro M.J.;
J. Cell Biol. 145:1277-1292(1999).
Cited for: MYRISTOYLATION AT GLY-2, AND INTERACTION WITH PSEN2.
PubMed: 10366599