MILK1_HUMAN - dbPTM
MILK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MILK1_HUMAN
UniProt AC Q8N3F8
Protein Name MICAL-like protein 1
Gene Name MICALL1
Organism Homo sapiens (Human).
Sequence Length 863
Subcellular Localization Recycling endosome membrane
Peripheral membrane protein. Late endosome membrane. Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6.
Protein Description Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth..
Protein Sequence MAGPRGALLAWCRRQCEGYRGVEIRDLSSSFRDGLAFCAILHRHRPDLLDFDSLSKDNVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFCSPGQAGVSPPRKGLAPCSPPSVAPTPVEPEDVAQGEELSSGSLSEQGTGQTPSSTCAACQQHVHLVQRYLADGRLYHRHCFRCRRCSSTLLPGAYENGPEEGTFVCAEHCARLGPGTRSGTRPGPFSQPKQQHQQQLAEDAKDVPGGGPSSSAPAGAEADGPKASPEARPQIPTKPRVPGKLQELASPPAGRPTPAPRKASESTTPAPPTPRPRSSLQQENLVEQAGSSSLVNGRLHELPVPKPRGTPKPSEGTPAPRKDPPWITLVQAEPKKKPAPLPPSSSPGPPSQDSRQVENGGTEEVAQPSPTASLESKPYNPFEEEEEDKEEEAPAAPSLATSPALGHPESTPKSLHPWYGITPTSSPKTKKRPAPRAPSASPLALHASRLSHSEPPSATPSPALSVESLSSESASQTAGAELLEPPAVPKSSSEPAVHAPGTPGNPVSLSTNSSLASSGELVEPRVEQMPQASPGLAPRTRGSSGPQPAKPCSGATPTPLLLVGDRSPVPSPGSSSPQLQVKSSCKENPFNRKPSPAASPATKKATKGSKPVRPPAPGHGFPLIKRKVQADQYIPEEDIHGEMDTIERRLDALEHRGVLLEEKLRGGLNEGREDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEYELRCLLNKPEKDWTEEDRAREKVLMQELVTLIEQRNAIINCLDEDRQREEEEDKMLEAMIKKKEFQREAEPEGKKKGKFKTMKMLKLLGNKRDAKSKSPRDKS
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
182MethylationQRYLADGRLYHRHCF
HHHHCCCCEECCCCC
32.40115483307
195PhosphorylationCFRCRRCSSTLLPGA
CCCCCCCCCCCCCCC
25.2523927012
196PhosphorylationFRCRRCSSTLLPGAY
CCCCCCCCCCCCCCH
27.0526657352
197PhosphorylationRCRRCSSTLLPGAYE
CCCCCCCCCCCCCHH
18.9328450419
203PhosphorylationSTLLPGAYENGPEEG
CCCCCCCHHCCCCCC
18.8223927012
227PhosphorylationRLGPGTRSGTRPGPF
HCCCCCCCCCCCCCC
44.3330576142
229PhosphorylationGPGTRSGTRPGPFSQ
CCCCCCCCCCCCCCC
34.6330576142
235PhosphorylationGTRPGPFSQPKQQHQ
CCCCCCCCCHHHHHH
49.0228555341
258PhosphorylationDVPGGGPSSSAPAGA
CCCCCCCCCCCCCCC
39.9523663014
259PhosphorylationVPGGGPSSSAPAGAE
CCCCCCCCCCCCCCC
33.3823663014
260PhosphorylationPGGGPSSSAPAGAEA
CCCCCCCCCCCCCCC
42.4823663014
273PhosphorylationEADGPKASPEARPQI
CCCCCCCCCCCCCCC
29.4230266825
282PhosphorylationEARPQIPTKPRVPGK
CCCCCCCCCCCCCCC
56.1430576142
289AcetylationTKPRVPGKLQELASP
CCCCCCCCHHHHCCC
40.7125953088
295PhosphorylationGKLQELASPPAGRPT
CCHHHHCCCCCCCCC
44.0019664994
302PhosphorylationSPPAGRPTPAPRKAS
CCCCCCCCCCCCCCC
30.6226055452
309PhosphorylationTPAPRKASESTTPAP
CCCCCCCCCCCCCCC
34.8130266825
311PhosphorylationAPRKASESTTPAPPT
CCCCCCCCCCCCCCC
34.7830266825
312PhosphorylationPRKASESTTPAPPTP
CCCCCCCCCCCCCCC
32.5230266825
313PhosphorylationRKASESTTPAPPTPR
CCCCCCCCCCCCCCC
27.0829255136
318PhosphorylationSTTPAPPTPRPRSSL
CCCCCCCCCCCCCHH
30.7629255136
323PhosphorylationPPTPRPRSSLQQENL
CCCCCCCCHHHHHCH
37.7822617229
324PhosphorylationPTPRPRSSLQQENLV
CCCCCCCHHHHHCHH
31.3221712546
338PhosphorylationVEQAGSSSLVNGRLH
HHHHCCCHHCCCEEC
37.7328555341
355PhosphorylationPVPKPRGTPKPSEGT
CCCCCCCCCCCCCCC
29.4422496350
359PhosphorylationPRGTPKPSEGTPAPR
CCCCCCCCCCCCCCC
55.5828857561
362PhosphorylationTPKPSEGTPAPRKDP
CCCCCCCCCCCCCCC
16.5422496350
367AcetylationEGTPAPRKDPPWITL
CCCCCCCCCCCCEEE
73.807670103
373PhosphorylationRKDPPWITLVQAEPK
CCCCCCEEEEECCCC
19.6026074081
389PhosphorylationKPAPLPPSSSPGPPS
CCCCCCCCCCCCCCC
41.3230266825
390PhosphorylationPAPLPPSSSPGPPSQ
CCCCCCCCCCCCCCC
46.4530266825
391PhosphorylationAPLPPSSSPGPPSQD
CCCCCCCCCCCCCCC
37.9130266825
396PhosphorylationSSSPGPPSQDSRQVE
CCCCCCCCCCCCCHH
50.1530266825
399PhosphorylationPGPPSQDSRQVENGG
CCCCCCCCCCHHCCC
19.5823403867
407PhosphorylationRQVENGGTEEVAQPS
CCHHCCCCCCCCCCC
30.3030266825
414PhosphorylationTEEVAQPSPTASLES
CCCCCCCCCCCCCCC
23.8530266825
416PhosphorylationEVAQPSPTASLESKP
CCCCCCCCCCCCCCC
32.9630266825
418PhosphorylationAQPSPTASLESKPYN
CCCCCCCCCCCCCCC
34.8430266825
421PhosphorylationSPTASLESKPYNPFE
CCCCCCCCCCCCCCC
44.2030266825
424PhosphorylationASLESKPYNPFEEEE
CCCCCCCCCCCCHHH
38.9225247763
443PhosphorylationEEAPAAPSLATSPAL
HCCCCCCCCCCCCCC
26.3823927012
446PhosphorylationPAAPSLATSPALGHP
CCCCCCCCCCCCCCC
40.3029978859
447PhosphorylationAAPSLATSPALGHPE
CCCCCCCCCCCCCCC
11.5421815630
455PhosphorylationPALGHPESTPKSLHP
CCCCCCCCCCCCCCC
55.2325627689
456PhosphorylationALGHPESTPKSLHPW
CCCCCCCCCCCCCCC
32.8321815630
459PhosphorylationHPESTPKSLHPWYGI
CCCCCCCCCCCCCCC
32.8722167270
464PhosphorylationPKSLHPWYGITPTSS
CCCCCCCCCCCCCCC
11.7822167270
467PhosphorylationLHPWYGITPTSSPKT
CCCCCCCCCCCCCCC
19.0222167270
469PhosphorylationPWYGITPTSSPKTKK
CCCCCCCCCCCCCCC
32.9422167270
470PhosphorylationWYGITPTSSPKTKKR
CCCCCCCCCCCCCCC
45.9322167270
471PhosphorylationYGITPTSSPKTKKRP
CCCCCCCCCCCCCCC
32.6622167270
474PhosphorylationTPTSSPKTKKRPAPR
CCCCCCCCCCCCCCC
45.2223403867
484PhosphorylationRPAPRAPSASPLALH
CCCCCCCCCCHHHHH
40.1529255136
486PhosphorylationAPRAPSASPLALHAS
CCCCCCCCHHHHHHH
25.4529255136
493PhosphorylationSPLALHASRLSHSEP
CHHHHHHHHCCCCCC
24.0123927012
496PhosphorylationALHASRLSHSEPPSA
HHHHHHCCCCCCCCC
24.6923927012
498PhosphorylationHASRLSHSEPPSATP
HHHHCCCCCCCCCCC
48.7119690332
502PhosphorylationLSHSEPPSATPSPAL
CCCCCCCCCCCCCCC
56.3323927012
504PhosphorylationHSEPPSATPSPALSV
CCCCCCCCCCCCCCH
28.7423927012
506PhosphorylationEPPSATPSPALSVES
CCCCCCCCCCCCHHH
20.6023927012
510PhosphorylationATPSPALSVESLSSE
CCCCCCCCHHHCCCC
26.4123927012
513PhosphorylationSPALSVESLSSESAS
CCCCCHHHCCCCCCC
31.2523927012
515PhosphorylationALSVESLSSESASQT
CCCHHHCCCCCCCCC
41.1423927012
516PhosphorylationLSVESLSSESASQTA
CCHHHCCCCCCCCCC
40.6423927012
518PhosphorylationVESLSSESASQTAGA
HHHCCCCCCCCCCCC
34.8625137130
520PhosphorylationSLSSESASQTAGAEL
HCCCCCCCCCCCCHH
37.0325137130
522PhosphorylationSSESASQTAGAELLE
CCCCCCCCCCCHHHC
25.2725137130
536PhosphorylationEPPAVPKSSSEPAVH
CCCCCCCCCCCCCCC
32.7830576142
537PhosphorylationPPAVPKSSSEPAVHA
CCCCCCCCCCCCCCC
44.8628450419
538PhosphorylationPAVPKSSSEPAVHAP
CCCCCCCCCCCCCCC
55.4828450419
547PhosphorylationPAVHAPGTPGNPVSL
CCCCCCCCCCCCCCC
27.2825159151
553PhosphorylationGTPGNPVSLSTNSSL
CCCCCCCCCCCCCCC
20.1928450419
555PhosphorylationPGNPVSLSTNSSLAS
CCCCCCCCCCCCCCC
20.3128450419
556PhosphorylationGNPVSLSTNSSLASS
CCCCCCCCCCCCCCC
44.4028450419
558PhosphorylationPVSLSTNSSLASSGE
CCCCCCCCCCCCCCC
27.1528450419
559PhosphorylationVSLSTNSSLASSGEL
CCCCCCCCCCCCCCC
29.9928450419
562PhosphorylationSTNSSLASSGELVEP
CCCCCCCCCCCCCCC
44.1428450419
563PhosphorylationTNSSLASSGELVEPR
CCCCCCCCCCCCCCH
30.5823927012
578PhosphorylationVEQMPQASPGLAPRT
HHHCCCCCCCCCCCC
17.7919664994
585PhosphorylationSPGLAPRTRGSSGPQ
CCCCCCCCCCCCCCC
38.0228102081
588PhosphorylationLAPRTRGSSGPQPAK
CCCCCCCCCCCCCCC
28.9122199227
589PhosphorylationAPRTRGSSGPQPAKP
CCCCCCCCCCCCCCC
58.2625394399
598PhosphorylationPQPAKPCSGATPTPL
CCCCCCCCCCCCCCE
39.7322199227
601PhosphorylationAKPCSGATPTPLLLV
CCCCCCCCCCCEEEE
31.0822199227
603PhosphorylationPCSGATPTPLLLVGD
CCCCCCCCCEEEECC
23.3930576142
612PhosphorylationLLLVGDRSPVPSPGS
EEEECCCCCCCCCCC
34.6823401153
616PhosphorylationGDRSPVPSPGSSSPQ
CCCCCCCCCCCCCCC
41.9723401153
616UbiquitinationGDRSPVPSPGSSSPQ
CCCCCCCCCCCCCCC
41.9723000965
619PhosphorylationSPVPSPGSSSPQLQV
CCCCCCCCCCCCEEC
30.9022167270
619UbiquitinationSPVPSPGSSSPQLQV
CCCCCCCCCCCCEEC
30.9023000965
620PhosphorylationPVPSPGSSSPQLQVK
CCCCCCCCCCCEECC
52.5322167270
621PhosphorylationVPSPGSSSPQLQVKS
CCCCCCCCCCEECCC
20.5419664994
622UbiquitinationPSPGSSSPQLQVKSS
CCCCCCCCCEECCCC
40.6323000965
627UbiquitinationSSPQLQVKSSCKENP
CCCCEECCCCCCCCC
24.5623000965
628PhosphorylationSPQLQVKSSCKENPF
CCCEECCCCCCCCCC
41.9523312004
629PhosphorylationPQLQVKSSCKENPFN
CCEECCCCCCCCCCC
24.4021712546
640PhosphorylationNPFNRKPSPAASPAT
CCCCCCCCCCCCCCC
30.1529255136
644PhosphorylationRKPSPAASPATKKAT
CCCCCCCCCCCCCCC
19.7122167270
647PhosphorylationSPAASPATKKATKGS
CCCCCCCCCCCCCCC
36.1423927012
655MalonylationKKATKGSKPVRPPAP
CCCCCCCCCCCCCCC
57.0932601280
670MethylationGHGFPLIKRKVQADQ
CCCCCCEEEECCCCC
54.58115973051
678PhosphorylationRKVQADQYIPEEDIH
EECCCCCCCCHHHCC
20.9927642862
708UbiquitinationRGVLLEEKLRGGLNE
CCHHHHHHHCCCCCC
33.8229967540
740PhosphorylationHLLVRRESELIYVFK
HHHHCCHHHHEEEEE
35.5728450419
744PhosphorylationRRESELIYVFKQQNL
CCHHHHEEEEEHHCH
16.6827642862
760PhosphorylationQRQADVEYELRCLLN
HHHCHHHHHHHHHHC
21.8028102081
768UbiquitinationELRCLLNKPEKDWTE
HHHHHHCCCCCCCCH
55.3029967540
771UbiquitinationCLLNKPEKDWTEEDR
HHHCCCCCCCCHHHH
68.0729967540
782UbiquitinationEEDRAREKVLMQELV
HHHHHHHHHHHHHHH
34.8129967540
822UbiquitinationMLEAMIKKKEFQREA
HHHHHHHHHHHHHHC
46.7623000965
825UbiquitinationAMIKKKEFQREAEPE
HHHHHHHHHHHCCCC
13.0923000965
828UbiquitinationKKKEFQREAEPEGKK
HHHHHHHHCCCCCCC
46.7523000965
833UbiquitinationQREAEPEGKKKGKFK
HHHCCCCCCCCCHHH
58.7723000965
840UbiquitinationGKKKGKFKTMKMLKL
CCCCCHHHHHHHHHH
51.7123000965
841PhosphorylationKKKGKFKTMKMLKLL
CCCCHHHHHHHHHHH
25.7526657352
843UbiquitinationKGKFKTMKMLKLLGN
CCHHHHHHHHHHHCC
46.4423000965
846UbiquitinationFKTMKMLKLLGNKRD
HHHHHHHHHHCCCCC
37.8623000965
847UbiquitinationKTMKMLKLLGNKRDA
HHHHHHHHHCCCCCC
6.9723000965
849UbiquitinationMKMLKLLGNKRDAKS
HHHHHHHCCCCCCCC
48.3123000965
850UbiquitinationKMLKLLGNKRDAKSK
HHHHHHCCCCCCCCC
35.8423000965
851UbiquitinationMLKLLGNKRDAKSKS
HHHHHCCCCCCCCCC
50.2723000965
852UbiquitinationLKLLGNKRDAKSKSP
HHHHCCCCCCCCCCC
53.7923000965
853UbiquitinationKLLGNKRDAKSKSPR
HHHCCCCCCCCCCCC
61.0223000965
855UbiquitinationLGNKRDAKSKSPRDK
HCCCCCCCCCCCCCC
63.8123000965
858UbiquitinationKRDAKSKSPRDKS--
CCCCCCCCCCCCC--
32.0523000965
860UbiquitinationDAKSKSPRDKS----
CCCCCCCCCCC----
71.7023000965
897Ubiquitination-----------------------------------------
-----------------------------------------
23000965
900Ubiquitination--------------------------------------------
--------------------------------------------
23000965
903Ubiquitination-----------------------------------------------
-----------------------------------------------
23000965
904Ubiquitination------------------------------------------------
------------------------------------------------
23000965
906Ubiquitination--------------------------------------------------
--------------------------------------------------
23000965
907Ubiquitination---------------------------------------------------
---------------------------------------------------
23000965
908Ubiquitination----------------------------------------------------
----------------------------------------------------
23000965
909Ubiquitination-----------------------------------------------------
-----------------------------------------------------
23000965
910Ubiquitination------------------------------------------------------
------------------------------------------------------
23000965
912Ubiquitination--------------------------------------------------------
--------------------------------------------------------
23000965
915Ubiquitination-----------------------------------------------------------
-----------------------------------------------------------
23000965
917Ubiquitination-------------------------------------------------------------
-------------------------------------------------------------
23000965

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 MILK1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MILK1_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 MILK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHD1_HUMANEHD1physical
22456504
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
CBY1_HUMANCBY1physical
27173435

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 MILK1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-467; SER-471; SER-484;SER-486 AND SER-578, AND MASS SPECTROMETRY.
"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-484; SER-486; SER-578AND SER-621, AND MASS SPECTROMETRY.
"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-295; SER-309; THR-313;THR-318; THR-467; SER-470; SER-471; SER-484; SER-486 AND SER-578, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND MASSSPECTROMETRY.

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