Q05682

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession CALD1_HUMAN; Q05682;
Entrez ID 800
GenBank Protein ID NM_004342.6; NM_033138.3; NM_033139.3; NM_033140.3; NM_033157.3; XM_017012651.1; XM_017012652.1;
GenBank Nucleotide ID NP_004333.1; NP_149129.2; NP_149130.1; NP_149131.1; NP_149347.2; XP_016868140.1; XP_016868141.1;
Protein Name Caldesmon (CDM)
Gene Name CALD1; CAD; CDM
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionActin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity).
Sequence
(Fasta)
MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG 60
QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE 120
FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA 180
EENKKEDKEK EEEEEEKPKR GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ 240
EEEREQGSDE ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK 300
AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK RAAEERQRIK 360
EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKHAMQ ETKIKGEKVE QKIEGKWVNE 420
KKAQEDKLQT AVLKKQGEEK GTKVQAKREK LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS 480
FMDRKKGFTE VKSQNGEFMT HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR 540
RRRGETESEE FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE 600
KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA EFLNKSVQKS 660
SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS DLPVPAEGVR NIKSMWEKGN 720
VFSSPTAAGT PNKETAGLKV GVSSRINEWL TKTPDGNKSP APKPSDLRPG DVSSKRNLWE 780
KQSVDKVTSP TKV 794

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Serine PhosphorylationBreast cancer/tumor/carcinomatumor tissueNS1223418348
[Reference]: Caldesmon containing a phosphomimetic S12E substitution fails to inhibit migration of human breast cancer cells
2Serine PhosphorylationProstate cancer/carcinoma/adenocarcinomaUS78922197205
[Reference]: Stimulation of prostate tissue with noradrenaline (30 ?M, n = 6 patients) or the ?1-adrenergic agonist phenylephrine (10 ?M, n = 6 patients) resulted in progressive phosphorylation of caldesmon at serine-789.?

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 2)
MESH:D001171 ; Arthritis, Juvenile
MESH:D001172 ; Arthritis, Rheumatoid
GWASdb
(count: 17)
(view all)
rs2347896; Alcohol dependence; alcohol dependence
rs6467557; Leukocyte Counts; leukemia|lymphoma|cardiovascular system disease
rs1470841; Coronary restenosis; coronary artery disease
rs17169635; Response to anti-retroviral therapy (ddI/d4T) in HIV-1 infection (Grade 1 peripheral neuropathy); Human immunodeficiency virus infectious disease
rs12707180; Mammographic density; female breast cancer
rs759987; Coronary restenosis; coronary artery disease

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 53)
(view all)
126       KEFDPTITDASLSLP     dbPAF
129       DPTITDASLSLPSRR     dbPAF
131       TITDASLSLPSRRMQ     dbPAF
141       SRRMQNDTAENETTE     dbPAF
153       TTEKEEKSESRQERY     dbPAF
160       SESRQERYEIEETET     dbPAF
Acetylation
(count: 14)
(view all)
149       AENETTEKEEKSESR     PLMD
152       ETTEKEEKSESRQER     PLMD
174       TVTKSYQKNDWRDAE     PLMD
504       EFMTHKLKHTENTFS     PLMD
53        RQERLRQKQEEESLG     PLMD
553       TESEEFEKLKQKQQE     PLMD
Ubiquitination
(count: 8)
(view all)
170       EETETVTKSYQKNDW     PLMD
522       GRASVDTKEAEGAPQ     PLMD
53        RQERLRQKQEEESLG     PLMD
534       APQVEAGKRLEELRR     PLMD
655       ERAEFLNKSVQKSSG     PLMD
718       NIKSMWEKGNVFSSP     PLMD
Sumoylation
(count: 3)
152       ETTEKEEKSESRQER     PLMD
631       EDGLSDDKKPFKCFT     PLMD
645       TPKGSSLKIEERAEF     PLMD
Malonylation
(count: 14)
(view all)
479       KEPKEEVKSFMDRKK     PLMD
502       NGEFMTHKLKHTENT     PLMD
522       GRASVDTKEAEGAPQ     PLMD
553       TESEEFEKLKQKQQE     PLMD
605       EEEKRRLKEEIERRR     PLMD
631       EDGLSDDKKPFKCFT     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource