MILK2_HUMAN - dbPTM
MILK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MILK2_HUMAN
UniProt AC Q8IY33
Protein Name MICAL-like protein 2
Gene Name MICALL2
Organism Homo sapiens (Human).
Sequence Length 904
Subcellular Localization Cell membrane
Peripheral membrane protein. Cell junction, tight junction. Recycling endosome. Cell projection. Cytoplasm, cytoskeleton. Cytoplasm, cytosol.
Protein Description Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth (By similarity)..
Protein Sequence MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVALKVPDRLSILTYVSQYYNYFHGRSPIGGMAGVKRASEDSEEEPSGKKAPVQAAKLPSPAPARKPPLSPAQTNPVVQRRNEGAGGPPPKTDQALAGSLVSSTCGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSHLPAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQASALPPAGRRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQDMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEPRAGEAPRKVSGSFAGSVHITLTPVRPDRTPRPASPGPSLPARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEARVQSWKEEEKKPHLQGKPGRPLSPANVPALPGETVTSPVRLHPDYLSPEEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELRRLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKIWSPKSKSSPSQ
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
4 (in isoform 3)Phosphorylation-1.6027732954
5 (in isoform 3)Phosphorylation-25.2327732954
10 (in isoform 3)Phosphorylation-2.6427732954
11 (in isoform 3)Phosphorylation-2.1527732954
51PhosphorylationRPDLINFSALKKENI
CCCCCCHHHHCHHCC		28.3626307563
59PhosphorylationALKKENIYENNKLAF
HHCHHCCHHCCCHHH		24.9628152594
94PhosphorylationLKVPDRLSILTYVSQ
CCCCCHHHHHHHHHH		19.2224275569
97PhosphorylationPDRLSILTYVSQYYN
CCHHHHHHHHHHHHH		21.8724275569
98PhosphorylationDRLSILTYVSQYYNY
CHHHHHHHHHHHHHH		8.4824275569
100PhosphorylationLSILTYVSQYYNYFH
HHHHHHHHHHHHHHC		11.31-
102PhosphorylationILTYVSQYYNYFHGR
HHHHHHHHHHHHCCC		6.0324275569
105PhosphorylationYVSQYYNYFHGRSPI
HHHHHHHHHCCCCCC		4.8424275569
110PhosphorylationYNYFHGRSPIGGMAG
HHHHCCCCCCCCCCC		26.0130266825
122PhosphorylationMAGVKRASEDSEEEP
CCCCCCCCCCCCCCC		46.0725849741
125PhosphorylationVKRASEDSEEEPSGK
CCCCCCCCCCCCCCC		42.7425849741
130PhosphorylationEDSEEEPSGKKAPVQ
CCCCCCCCCCCCCCC		67.5327794612
143PhosphorylationVQAAKLPSPAPARKP
CCHHCCCCCCCCCCC		44.1030266825
153PhosphorylationPARKPPLSPAQTNPV
CCCCCCCCHHHCCCC		24.7830266825
157PhosphorylationPPLSPAQTNPVVQRR
CCCCHHHCCCCCCCC		43.5330266825
182PhosphorylationTDQALAGSLVSSTCG
CCHHHHHHHHHHHCC		21.7128857561
219PhosphorylationCFRCKQCSCTLHSGA
CCCCCCCEEEEECCC		13.9828060719
221PhosphorylationRCKQCSCTLHSGAYK
CCCCCEEEEECCCCC		15.9428060719
230PhosphorylationHSGAYKATGEPGTFV
ECCCCCCCCCCCEEE		37.6223403867
235PhosphorylationKATGEPGTFVCTSHL
CCCCCCCEEEEECCC		24.5023927012
239PhosphorylationEPGTFVCTSHLPAAA
CCCEEEEECCCCCCC		17.5523927012
240PhosphorylationPGTFVCTSHLPAAAS
CCEEEEECCCCCCCC		20.2123927012
247PhosphorylationSHLPAAASASPKLTG
CCCCCCCCCCCCCCC		25.2630266825
249PhosphorylationLPAAASASPKLTGLV
CCCCCCCCCCCCCCC		21.7730266825
253PhosphorylationASASPKLTGLVPRQP
CCCCCCCCCCCCCCC		34.3023312004
269PhosphorylationAMGVDSRTSCSPQKA
CCCCCCCCCCCHHHH		37.7325262027
270PhosphorylationMGVDSRTSCSPQKAQ
CCCCCCCCCCHHHHH		16.1025262027
272PhosphorylationVDSRTSCSPQKAQEA
CCCCCCCCHHHHHHH		30.0825849741
285PhosphorylationEANKARPSAWEPAAG
HHHHCCCCCCCCCCC		40.2230177828
294PhosphorylationWEPAAGNSPARASVP
CCCCCCCCCCCCCCC		21.0130266825
299PhosphorylationGNSPARASVPAAPNP
CCCCCCCCCCCCCCC		24.0723186163
309PhosphorylationAAPNPAATSATSVHV
CCCCCCCCCCCEEEE		22.4723186163
309O-linked_GlycosylationAAPNPAATSATSVHV
CCCCCCCCCCCEEEE		22.4728657654
310O-linked_GlycosylationAPNPAATSATSVHVR
CCCCCCCCCCEEEEC		25.4828657654
310PhosphorylationAPNPAATSATSVHVR
CCCCCCCCCCEEEEC		25.4823312004
312PhosphorylationNPAATSATSVHVRSP
CCCCCCCCEEEECCC		30.9223186163
313PhosphorylationPAATSATSVHVRSPA
CCCCCCCEEEECCCC		15.2223186163
318PhosphorylationATSVHVRSPARPSES
CCEEEECCCCCCCCC		23.0925849741
323PhosphorylationVRSPARPSESRLAPT
ECCCCCCCCCCCCCC		42.5223186163
325PhosphorylationSPARPSESRLAPTPT
CCCCCCCCCCCCCCC		36.6123186163
330PhosphorylationSESRLAPTPTEGKVR
CCCCCCCCCCCCCCC		36.9226657352
332PhosphorylationSRLAPTPTEGKVRPR
CCCCCCCCCCCCCCC		60.9027251275
375PhosphorylationAPDPRPATPQGGGAP
CCCCCCCCCCCCCCC		20.8729255136
407PhosphorylationTVDPPAWTPSASRTQ
CCCCCCCCCCCHHHH		14.9628555341
423PhosphorylationARNKFFQTSAVPPGT
HHHHHHCCCCCCCCC		17.3127307780
424PhosphorylationRNKFFQTSAVPPGTS
HHHHHCCCCCCCCCC		19.2424719451
433PhosphorylationVPPGTSLSGRGPTPS
CCCCCCCCCCCCCCC		26.6424719451
435MethylationPGTSLSGRGPTPSLV
CCCCCCCCCCCCCEE		44.5458854781
438PhosphorylationSLSGRGPTPSLVLSK
CCCCCCCCCCEEECC		28.4727307780
440PhosphorylationSGRGPTPSLVLSKDS
CCCCCCCCEEECCCC		33.3224425749
444PhosphorylationPTPSLVLSKDSSKEQ
CCCCEEECCCCCHHH		27.2624425749
448PhosphorylationLVLSKDSSKEQARNF
EEECCCCCHHHHHHH		50.8018669648
475PhosphorylationAPAPGRPSPATAAVP
CCCCCCCCCCCCCCC		26.3025159151
478PhosphorylationPGRPSPATAAVPSSQ
CCCCCCCCCCCCCCC		20.6622468782
488PhosphorylationVPSSQPKTEAPQASP
CCCCCCCCCCCCCCC		44.0223403867
488O-linked_GlycosylationVPSSQPKTEAPQASP
CCCCCCCCCCCCCCC		44.0228657654
494O-linked_GlycosylationKTEAPQASPLAKPLQ
CCCCCCCCCCCCCCC		18.3928657654
494PhosphorylationKTEAPQASPLAKPLQ
CCCCCCCCCCCCCCC		18.3925159151
502PhosphorylationPLAKPLQSSSPRVLG
CCCCCCCCCCCCCCC		40.2325849741
503PhosphorylationLAKPLQSSSPRVLGL
CCCCCCCCCCCCCCC		31.2529255136
504PhosphorylationAKPLQSSSPRVLGLP
CCCCCCCCCCCCCCC		23.2129255136
526PhosphorylationPLSTSSTSQASALPP
CCCCCCCHHHHCCCC		26.2019651622
573PhosphorylationTTLTQDMSTSLQEGQ
CCCCCHHHHHHHCCC		24.12-
598PhosphorylationLKPVDRRSPAERTLK
CCCCCCCCHHHHCCC		29.3823403867
625PhosphorylationGEAPRKVSGSFAGSV
CCCCCCCCCCCCCEE		31.5820639409
627PhosphorylationAPRKVSGSFAGSVHI
CCCCCCCCCCCEEEE		12.3820639409
631PhosphorylationVSGSFAGSVHITLTP
CCCCCCCEEEEEEEE		13.6920639409
635PhosphorylationFAGSVHITLTPVRPD
CCCEEEEEEEECCCC		15.0920639409
637PhosphorylationGSVHITLTPVRPDRT
CEEEEEEEECCCCCC		15.8720639409
644PhosphorylationTPVRPDRTPRPASPG
EECCCCCCCCCCCCC		30.9130266825
649PhosphorylationDRTPRPASPGPSLPA
CCCCCCCCCCCCCCC		32.8330266825
653PhosphorylationRPASPGPSLPARSPS
CCCCCCCCCCCCCCC		53.5530266825
658PhosphorylationGPSLPARSPSPPRRR
CCCCCCCCCCCCCHH		31.6623401153
660PhosphorylationSLPARSPSPPRRRRL
CCCCCCCCCCCHHHC		49.1023401153
693PhosphorylationGQEARVQSWKEEEKK
CHHHHHHCHHHHHCC		36.9427251275
712PhosphorylationGKPGRPLSPANVPAL
CCCCCCCCCCCCCCC		25.3429255136
723PhosphorylationVPALPGETVTSPVRL
CCCCCCCCCCCCCCC		34.6929255136
725PhosphorylationALPGETVTSPVRLHP
CCCCCCCCCCCCCCC		34.4329255136
726PhosphorylationLPGETVTSPVRLHPD
CCCCCCCCCCCCCCC		19.6429255136
734PhosphorylationPVRLHPDYLSPEEIQ
CCCCCCCCCCHHHHH		17.3322199227
736PhosphorylationRLHPDYLSPEEIQRQ
CCCCCCCCHHHHHHH		24.8422199227
844PhosphorylationEQELLEQYVSTVNDR
HHHHHHHHHHHCCCH		6.2326074081
846PhosphorylationELLEQYVSTVNDRSD
HHHHHHHHHCCCHHH		23.0026074081
847PhosphorylationLLEQYVSTVNDRSDI
HHHHHHHHCCCHHHH		17.1826074081
852PhosphorylationVSTVNDRSDIVDSLD
HHHCCCHHHHHHHCC		34.2526074081
857PhosphorylationDRSDIVDSLDEDRLR
CHHHHHHHCCHHHHH		27.1626074081
895PhosphorylationFRLSKIWSPKSKSSP
CCHHHCCCCCCCCCC		26.3924719451
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 MILK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MILK2_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 MILK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MILK2_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.
Regulatory Network of MILK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-494; SER-504;SER-649; SER-658 AND SER-660, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASSSPECTROMETRY.

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