CASA1_HUMAN - dbPTM
CASA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASA1_HUMAN
UniProt AC P47710
Protein Name Alpha-S1-casein
Gene Name CSN1S1
Organism Homo sapiens (Human).
Sequence Length 185
Subcellular Localization Secreted.
Protein Description Important role in the capacity of milk to transport calcium phosphate.; Casoxin D acts as opioid antagonist and has vasorelaxing activity mediated by bradykinin B1 receptors..
Protein Sequence MRLLILTCLVAVALARPKLPLRYPERLQNPSESSEPIPLESREEYMNGMNRQRNILREKQTDEIKDTRNESTQNCVVAEPEKMESSISSSSEEMSLSKCAEQFCRLNEYNQLQLQAAHAQEQIRRMNENSHVQVPFQQLNQLAAYPYAVWYYPQIMQYVPFPPFSDISNPTAHENYEKNNVMLQW
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 Orthologous
Protein Cluster
31PhosphorylationPERLQNPSESSEPIP
HHHHCCCCCCCCCCC
58.6320068231
33PhosphorylationRLQNPSESSEPIPLE
HHCCCCCCCCCCCCC
44.3217646876
34PhosphorylationLQNPSESSEPIPLES
HCCCCCCCCCCCCCH
43.2520068231
41PhosphorylationSEPIPLESREEYMNG
CCCCCCCHHHHHHHH
53.3117646876
71PhosphorylationIKDTRNESTQNCVVA
HHHCCCHHCCCEEEE
38.5527251275
72PhosphorylationKDTRNESTQNCVVAE
HHCCCHHCCCEEEEC
20.0227251275
85PhosphorylationAEPEKMESSISSSSE
ECHHHHHHHCCCCCH
29.4928450419
86PhosphorylationEPEKMESSISSSSEE
CHHHHHHHCCCCCHH
17.1228450419
88PhosphorylationEKMESSISSSSEEMS
HHHHHHCCCCCHHHC
26.5617646876
89PhosphorylationKMESSISSSSEEMSL
HHHHHCCCCCHHHCH
35.8928450419
90PhosphorylationMESSISSSSEEMSLS
HHHHCCCCCHHHCHH
34.6717646876
91PhosphorylationESSISSSSEEMSLSK
HHHCCCCCHHHCHHH
39.257619062
95PhosphorylationSSSSEEMSLSKCAEQ
CCCCHHHCHHHHHHH
32.5428450419
97PhosphorylationSSEEMSLSKCAEQFC
CCHHHCHHHHHHHHH
20.5528450419
130PhosphorylationIRRMNENSHVQVPFQ
HHHHHCCCCCCCCHH
20.8926330541
145PhosphorylationQLNQLAAYPYAVWYY
HHHHHHHHCHHHHHC
7.3826330541
147PhosphorylationNQLAAYPYAVWYYPQ
HHHHHHCHHHHHCCH
10.9126330541
151PhosphorylationAYPYAVWYYPQIMQY
HHCHHHHHCCHHHHH
9.9226330541
152PhosphorylationYPYAVWYYPQIMQYV
HCHHHHHCCHHHHHC
3.4926330541
158PhosphorylationYYPQIMQYVPFPPFS
HCCHHHHHCCCCCCC
7.8426330541
165PhosphorylationYVPFPPFSDISNPTA
HCCCCCCCCCCCCCC
39.5526330541
168PhosphorylationFPPFSDISNPTAHEN
CCCCCCCCCCCCCCC
41.5726330541
171PhosphorylationFSDISNPTAHENYEK
CCCCCCCCCCCCHHH
44.9226330541
176PhosphorylationNPTAHENYEKNNVML
CCCCCCCHHHCCCCC
25.8726330541

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

Oops, there are no upstream regulatory protein records of CASA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASA1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CASA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE10_HUMANPDE10Aphysical
28514442
B4GN4_HUMANB4GALNT4physical
28514442
LTBP1_HUMANLTBP1physical
28514442
EMIL3_HUMANEMILIN3physical
28514442
KLH15_HUMANKLHL15physical
28514442
GRP78_HUMANHSPA5physical
28514442
TIMP3_HUMANTIMP3physical
28514442
ERF_HUMANERFphysical
28514442
BCOR_HUMANBCORphysical
28514442
CARF_HUMANCDKN2AIPphysical
28514442
F120A_HUMANFAM120Aphysical
28514442
ETV3_HUMANETV3physical
28514442

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.
Regulatory Network of CASA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phosphorylation pattern of human alphas1-casein is markedlydifferent from the ruminant species.";
Sorensen E.S., Moller L., Vinther M., Petersen T.E., Rasmussen L.K.;
Eur. J. Biochem. 270:3651-3655(2003).
Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-33 AND SER-41, LACKOF GLYCOSYLATION, AND MASS SPECTROMETRY.
"Analysis of the human casein phosphoproteome by 2-D electrophoresisand MALDI-TOF/TOF MS reveals new phosphoforms.";
Poth A.G., Deeth H.C., Alewood P.F., Holland J.W.;
J. Proteome Res. 7:5017-5027(2008).
Cited for: PROTEIN SEQUENCE OF 28-48, PHOSPHORYLATION AT SER-31; SER-33; SER-41;SER-86; SER-88; SER-89; SER-90 AND SER-91, AND MASS SPECTROMETRY.
"On studying protein phosphorylation patterns using bottom-up LC-MS/MS: the case of human alpha-casein.";
Kjeldsen F., Savitski M.M., Nielsen M.L., Shi L., Zubarev R.A.;
Analyst 132:768-776(2007).
Cited for: PROTEIN SEQUENCE OF 27-42 AND 83-98, PHOSPHORYLATION AT SER-33;SER-41; SER-88 AND SER-90, AND MASS SPECTROMETRY.

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