dbPTM

MYLK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MYLK_HUMAN
UniProt AC	Q15746
Protein Name	Myosin light chain kinase, smooth muscle
Gene Name	MYLK
Organism	Homo sapiens (Human).
Sequence Length	1914
Subcellular Localization	Cytoplasm. Cell projection, lamellipodium. Cleavage furrow. Cytoplasm, cytoskeleton. Localized to stress fibers during interphase and to the cleavage furrow during mitosis.
Protein Description	Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis..
Protein Sequence	MGDVKLVASSHISKTSLSVDPSRVDSMPLTEAPAFILPPRNLCIKEGATAKFEGRVRGYPEPQVTWHRNGQPITSGGRFLLDCGIRGTFSLVIHAVHEEDRGKYTCEATNGSGARQVTVELTVEGSFAKQLGQPVVSKTLGDRFSAPAVETRPSIWGECPPKFATKLGRVVVKEGQMGRFSCKITGRPQPQVTWLKGNVPLQPSARVSVSEKNGMQVLEIHGVNQDDVGVYTCLVVNGSGKASMSAELSIQGLDSANRSFVRETKATNSDVRKEVTNVISKESKLDSLEAAAKSKNCSSPQRGGSPPWAANSQPQPPRESKLESCKDSPRTAPQTPVLQKTSSSITLQAARVQPEPRAPGLGVLSPSGEERKRPAPPRPATFPTRQPGLGSQDVVSKAANRRIPMEGQRDSAFPKFESKPQSQEVKENQTVKFRCEVSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVERLAVMEVAPSFSSVLKDCAVIEGQDFVLQCSVRGTPVPRITWLLNGQPIQYARSTCEAGVAELHIQDALPEDHGTYTCLAENALGQVSCSAWVTVHEKKSSRKSEYLLPVAPSKPTAPIFLQGLSDLKVMDGSQVTMTVQVSGNPPPEVIWLHNGNEIQESEDFHFEQRGTQHSLCIQEVFPEDTGTYTCEAWNSAGEVRTQAVLTVQEPHDGTQPWFISKPRSVTASLGQSVLISCAIAGDPFPTVHWLRDGKALCKDTGHFEVLQNEDVFTLVLKKVQPWHAGQYEILLKNRVGECSCQVSLMLQNSSARALPRGREPASCEDLCGGGVGADGGGSDRYGSLRPGWPARGQGWLEEEDGEDVRGVLKRRVETRQHTEEAIRQQEVEQLDFRDLLGKKVSTKTLSEDDLKEIPAEQMDFRANLQRQVKPKTVSEEERKVHSPQQVDFRSVLAKKGTSKTPVPEKVPPPKPATPDFRSVLGGKKKLPAENGSSSAETLNAKAVESSKPLSNAQPSGPLKPVGNAKPAETLKPMGNAKPAETLKPMGNAKPDENLKSASKEELKKDVKNDVNCKRGHAGTTDNEKRSESQGTAPAFKQKLQDVHVAEGKKLLLQCQVSSDPPATIIWTLNGKTLKTTKFIILSQEGSLCSVSIEKALPEDRGLYKCVAKNDAGQAECSCQVTVDDAPASENTKAPEMKSRRPKSSLPPVLGTESDATVKKKPAPKTPPKAAMPPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQAQVNLTVVDKPDPPAGTPCASDIRSSSLTLSWYGSSYDGGSAVQSYSIEIWDSANKTWKELATCRSTSFNVQDLLPDHEYKFRVRAINVYGTSEPSQESELTTVGEKPEEPKDEVEVSDDDEKEPEVDYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLEAVAEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEGEEEEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 10)	Acetylation	-	60.77	22814378
2 (in isoform 8)	Acetylation	-	60.77	22814378
5 (in isoform 8)	Phosphorylation	-	41.82	27251275
9	Phosphorylation	GDVKLVASSHISKTS CCCEEEEECCCCCCE	18.25	28857561
10	Phosphorylation	DVKLVASSHISKTSL CCEEEEECCCCCCEE	18.33	27251275
12 (in isoform 10)	Phosphorylation	-	4.96	26657352
13	Phosphorylation	LVASSHISKTSLSVD EEEECCCCCCEECCC	25.18	19651622
13 (in isoform 10)	Phosphorylation	-	25.18	28348404
13 (in isoform 8)	Phosphorylation	-	25.18	27251275
14 (in isoform 10)	Phosphorylation	-	41.34	26657352
15	Phosphorylation	ASSHISKTSLSVDPS EECCCCCCEECCCHH	28.27	24702127
16	Phosphorylation	SSHISKTSLSVDPSR ECCCCCCEECCCHHH	23.53	19651622
16 (in isoform 10)	Phosphorylation	-	23.53	26657352
18	Phosphorylation	HISKTSLSVDPSRVD CCCCCEECCCHHHCC	25.00	10092231
18 (in isoform 10)	Phosphorylation	-	25.00	26657352
19 (in isoform 10)	Phosphorylation	-	17.78	29507054
19 (in isoform 8)	Phosphorylation	-	17.78	27251275
28 (in isoform 10)	Phosphorylation	-	39.83	28348404
88	Phosphorylation	LDCGIRGTFSLVIHA EECCCCCEEEEEEEE	10.53	-
104	Phosphorylation	HEEDRGKYTCEATNG CHHHCCCEEEEEECC	21.32	22817900
109	Phosphorylation	GKYTCEATNGSGARQ CCEEEEEECCCCCEE	20.16	-
118	Phosphorylation	GSGARQVTVELTVEG CCCCEEEEEEEEEEC	10.42	-
145	Phosphorylation	KTLGDRFSAPAVETR CCCCCCCCCCCCCCC	33.95	-
193	Phosphorylation	GRPQPQVTWLKGNVP CCCCCCEEEEECCCC	21.60	23403867
231	Phosphorylation	NQDDVGVYTCLVVNG CCCCCEEEEEEEECC	5.94	22817900
244	Sulfoxidation	NGSGKASMSAELSIQ CCCCCEEECEEEEEC	5.41	30846556
249	Phosphorylation	ASMSAELSIQGLDSA EEECEEEEECCHHHC	12.36	27251275
255	Phosphorylation	LSIQGLDSANRSFVR EEECCHHHCCHHHHH	32.27	27251275
259	Phosphorylation	GLDSANRSFVRETKA CHHHCCHHHHHHHCC	28.09	27251275
283	Phosphorylation	TNVISKESKLDSLEA HHHHCHHHHHHHHHH	42.10	30140170
287	Phosphorylation	SKESKLDSLEAAAKS CHHHHHHHHHHHHHC	38.25	27251275
298	Phosphorylation	AAKSKNCSSPQRGGS HHHCCCCCCCCCCCC	55.22	29514088
299	Phosphorylation	AKSKNCSSPQRGGSP HHCCCCCCCCCCCCC	27.53	22199227
305	Phosphorylation	SSPQRGGSPPWAANS CCCCCCCCCCCHHCC	30.52	30266825
312	Phosphorylation	SPPWAANSQPQPPRE CCCCHHCCCCCCCCH	38.21	29514088
320	Phosphorylation	QPQPPRESKLESCKD CCCCCCHHHHHHCCC	43.77	22199227
324	Phosphorylation	PRESKLESCKDSPRT CCHHHHHHCCCCCCC	36.58	22199227
328	Phosphorylation	KLESCKDSPRTAPQT HHHHCCCCCCCCCCC	11.19	22199227
331	Phosphorylation	SCKDSPRTAPQTPVL HCCCCCCCCCCCCCC	46.18	30266825
335	Phosphorylation	SPRTAPQTPVLQKTS CCCCCCCCCCCCCCC	17.82	30266825
341	Phosphorylation	QTPVLQKTSSSITLQ CCCCCCCCCCCEEEE	22.38	24719451
342	Phosphorylation	TPVLQKTSSSITLQA CCCCCCCCCCEEEEE	29.17	25072903
343	Phosphorylation	PVLQKTSSSITLQAA CCCCCCCCCEEEEEE	30.87	28258704
344	Phosphorylation	VLQKTSSSITLQAAR CCCCCCCCEEEEEEE	21.25	22199227
365	Phosphorylation	APGLGVLSPSGEERK CCCCCCCCCCCCCCC	18.02	30266825
367	Phosphorylation	GLGVLSPSGEERKRP CCCCCCCCCCCCCCC	56.30	30266825
391	Phosphorylation	TRQPGLGSQDVVSKA CCCCCCCCHHHHHHH	28.40	24505115
422	Phosphorylation	KFESKPQSQEVKENQ CCCCCCCCHHCCCCC	36.51	23312004
460	Phosphorylation	PVRRQEGSIEVYEDA CCCCCCCCEEEEECC	18.15	24719451
464	Phosphorylation	QEGSIEVYEDAGSHY CCCCEEEEECCCCEE	8.70	22817900
469	Phosphorylation	EVYEDAGSHYLCLLK EEEECCCCEEEEEEE	15.64	24719451
471	Phosphorylation	YEDAGSHYLCLLKAR EECCCCEEEEEEEEE	10.78	22817900
488	Phosphorylation	DSGTYSCTASNAQGQ CCCEEEEEECCCCCE	27.46	-
510	Sulfoxidation	QVERLAVMEVAPSFS EEEEEEEHHHCCCHH	2.59	30846556
515	Phosphorylation	AVMEVAPSFSSVLKD EEHHHCCCHHHHHHC	28.20	-
556	Phosphorylation	LNGQPIQYARSTCEA ECCCCCCHHHHHCCC	12.52	22817900
603	Methylation	AWVTVHEKKSSRKSE EEEEEEECCCCCCCE	42.98	-
608	Acetylation	HEKKSSRKSEYLLPV EECCCCCCCEEEEEC	49.97	19826488
609	Phosphorylation	EKKSSRKSEYLLPVA ECCCCCCCEEEEECC	30.29	28857561
611	Phosphorylation	KSSRKSEYLLPVAPS CCCCCCEEEEECCCC	22.19	25884760
792	Phosphorylation	QPWHAGQYEILLKNR CCCCCCEEEEEECCC	12.20	22817900
827	Phosphorylation	PRGREPASCEDLCGG CCCCCCCCHHHHCCC	28.84	28857561
846	Phosphorylation	DGGGSDRYGSLRPGW CCCCCCCCCCCCCCC	18.96	22817900
848	Phosphorylation	GGSDRYGSLRPGWPA CCCCCCCCCCCCCCC	16.57	27251275
850 (in isoform 11)	Phosphorylation	-	29.40	26657352
851 (in isoform 11)	Phosphorylation	-	55.27	28348404
852 (in isoform 11)	Phosphorylation	-	36.24	26657352
854 (in isoform 11)	Phosphorylation	-	20.28	26657352
856 (in isoform 11)	Phosphorylation	-	33.61	26657352
857 (in isoform 11)	Phosphorylation	-	32.24	29507054
866 (in isoform 11)	Phosphorylation	-	35.96	28348404
883	Phosphorylation	RVETRQHTEEAIRQQ HHHHHHHHHHHHHHH	27.47	24719451
903	Ubiquitination	DFRDLLGKKVSTKTL CHHHHCCCCCCCCCC	50.39	-
909	Phosphorylation	GKKVSTKTLSEDDLK CCCCCCCCCCHHHHH	35.29	28857561
911	Phosphorylation	KVSTKTLSEDDLKEI CCCCCCCCHHHHHHC	44.18	28355574
923	Sulfoxidation	KEIPAEQMDFRANLQ HHCCHHHHCHHHHHH	3.86	30846556
947	Phosphorylation	EEERKVHSPQQVDFR HHHHCCCCCCCCCHH	27.65	30266825
978	Phosphorylation	VPPPKPATPDFRSVL CCCCCCCCCCHHHHH	31.73	26657352
1011	Phosphorylation	NAKAVESSKPLSNAQ CHHHHHCCCCCCCCC	25.45	24719451
1042	Acetylation	LKPMGNAKPAETLKP CCCCCCCCCHHHCCC	49.08	7925315
1061	Phosphorylation	KPDENLKSASKEELK CCCCCHHHCCHHHHH	40.72	26437602
1063	Phosphorylation	DENLKSASKEELKKD CCCHHHCCHHHHHHH	47.92	26657352
1091	Phosphorylation	TTDNEKRSESQGTAP CCCCHHHCCCCCCCH	53.30	26657352
1093	Phosphorylation	DNEKRSESQGTAPAF CCHHHCCCCCCCHHH	34.85	28857561
1096	Phosphorylation	KRSESQGTAPAFKQK HHCCCCCCCHHHHHH	23.10	30576142
1101	Methylation	QGTAPAFKQKLQDVH CCCCHHHHHHHCCEE	48.94	115980853
1103	Methylation	TAPAFKQKLQDVHVA CCHHHHHHHCCEEEC	49.02	115980865
1113	2-Hydroxyisobutyrylation	DVHVAEGKKLLLQCQ CEEECCCCEEEEEEE	31.58	-
1113	Acetylation	DVHVAEGKKLLLQCQ CEEECCCCEEEEEEE	31.58	19813259
1122	Phosphorylation	LLLQCQVSSDPPATI EEEEEEECCCCCCEE	11.80	26657352
1123	Phosphorylation	LLQCQVSSDPPATII EEEEEECCCCCCEEE	56.11	27251275
1147	Phosphorylation	TTKFIILSQEGSLCS EEEEEEECCCCCEEE	18.77	22210691
1151	Phosphorylation	IILSQEGSLCSVSIE EEECCCCCEEEEEHH	26.00	26657352
1154	Phosphorylation	SQEGSLCSVSIEKAL CCCCCEEEEEHHHHC	24.96	22210691
1156	Phosphorylation	EGSLCSVSIEKALPE CCCEEEEEHHHHCCC	14.56	22210691
1208	Phosphorylation	MKSRRPKSSLPPVLG HHCCCCCCCCCCCCC	39.53	22199227
1209	Phosphorylation	KSRRPKSSLPPVLGT HCCCCCCCCCCCCCC	51.53	26657352
1230	Phosphorylation	KKKPAPKTPPKAAMP CCCCCCCCCCCCCCC	43.71	29457462
1236	Sulfoxidation	KTPPKAAMPPQIIQF CCCCCCCCCCCEEEC	6.26	30846556
1254	Phosphorylation	QKVRAGESVELFGKV CCCCCCCCEEEECEE	21.70	27499020
1337	Phosphorylation	KPDPPAGTPCASDIR CCCCCCCCCCCHHCC	19.80	26657352
1410	Phosphorylation	RVRAINVYGTSEPSQ EEEEEEEECCCCCCC	15.36	-
1416	Phosphorylation	VYGTSEPSQESELTT EECCCCCCCCCCEEE	42.39	28348404
1419	Phosphorylation	TSEPSQESELTTVGE CCCCCCCCCEEECCC	30.21	28348404
1422	Phosphorylation	PSQESELTTVGEKPE CCCCCCEEECCCCCC	18.51	28348404
1423	Phosphorylation	SQESELTTVGEKPEE CCCCCEEECCCCCCC	38.85	26657352
1438	Phosphorylation	PKDEVEVSDDDEKEP CCCCCCCCCCCCCCC	23.09	20058876
1449	Phosphorylation	EKEPEVDYRTVTINT CCCCCCEEEEEEECC	17.23	22817900
1474	Malonylation	EERLGSGKFGQVFRL HHHHCCCCCHHHEEE	48.28	26320211
1496	Acetylation	VWAGKFFKAYSAKEK HHHHHHHHHCCHHHH	49.93	7479999
1570	Phosphorylation	IKYMRQISEGVEYIH HHHHHHHHCCCHHHH	21.69	26657352
1575	Phosphorylation	QISEGVEYIHKQGIV HHHCCCHHHHHCCCE	13.11	22817900
1617	Phosphorylation	RRLENAGSLKVLFGT HHHHHCCCCEEEECC	23.70	29514088
1624	Phosphorylation	SLKVLFGTPEFVAPE CCEEEECCCCCCCCC	16.59	26657352
1635	Phosphorylation	VAPEVINYEPIGYAT CCCCEECCCCCCCCH	16.38	22817900
1656	Phosphorylation	VICYILVSGLSPFMG HHHHHHHHCCCCCCC	30.48	19651622
1659	Phosphorylation	YILVSGLSPFMGDND HHHHHCCCCCCCCCC	21.44	19651622
1723	Phosphorylation	HPWLMKDTKNMEAKK CHHHHHCCCCCCHHH	20.85	19651622
1744	Acetylation	KKYMARRKWQKTGNA HHHHHHHHHHHHCHH	48.72	69223
1747	Acetylation	MARRKWQKTGNAVRA HHHHHHHHHCHHHHH	58.23	69227
1759	Phosphorylation	VRAIGRLSSMAMISG HHHHHHHHHHHHHHC	19.39	21082442
1760	Phosphorylation	RAIGRLSSMAMISGL HHHHHHHHHHHHHCC	18.36	21082442
1765	Phosphorylation	LSSMAMISGLSGRKS HHHHHHHHCCCCCCC	22.16	22210691
1768	Phosphorylation	MAMISGLSGRKSSTG HHHHHCCCCCCCCCC	39.83	28060719
1772	Phosphorylation	SGLSGRKSSTGSPTS HCCCCCCCCCCCCCC	31.60	30266825
1772 (in isoform 6)	Phosphorylation	-	31.60	26657352
1773	Phosphorylation	GLSGRKSSTGSPTSP CCCCCCCCCCCCCCC	39.56	23911959
1773 (in isoform 6)	Phosphorylation	-	39.56	28348404
1774	Phosphorylation	LSGRKSSTGSPTSPL CCCCCCCCCCCCCCC	49.09	30266825
1774 (in isoform 6)	Phosphorylation	-	49.09	26657352
1776	Phosphorylation	GRKSSTGSPTSPLNA CCCCCCCCCCCCCCH	25.70	30266825
1776 (in isoform 6)	Phosphorylation	-	25.70	26657352
1778	Phosphorylation	KSSTGSPTSPLNAEK CCCCCCCCCCCCHHH	44.68	30266825
1778 (in isoform 6)	Phosphorylation	-	44.68	26657352
1779	Phosphorylation	SSTGSPTSPLNAEKL CCCCCCCCCCCHHHH	30.67	30266825
1779 (in isoform 6)	Phosphorylation	-	30.67	29507054
1788	Phosphorylation	LNAEKLESEEDVSQA CCHHHHCCHHHHHHH	57.64	26657352
1788 (in isoform 6)	Phosphorylation	-	57.64	28348404
1793	Phosphorylation	LESEEDVSQAFLEAV HCCHHHHHHHHHHHH	28.28	26657352
1812	O-linked_Glycosylation	PHVKPYFSKTIRDLE CCCCCCCCCEECCEE	24.05	30620550
1824	Phosphorylation	DLEVVEGSAARFDCK CEEEEECCCEEECEE	12.78	27499020
1835	Phosphorylation	FDCKIEGYPDPEVVW ECEEECCCCCCCEEE	7.53	-
1848	Phosphorylation	VWFKDDQSIRESRHF EEECCCCCHHHHCEE	30.52	26657352
1852	Phosphorylation	DDQSIRESRHFQIDY CCCCHHHHCEEEEEE	22.62	30242111

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
13	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
13	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
16	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
16	S	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
16	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
16	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
231	Y	Phosphorylation	Kinase	ABL	P00519	PSP
464	Y	Phosphorylation	Kinase	ABL	P00519	PSP
464	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
471	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
556	Y	Phosphorylation	Kinase	ABL	P00519	PSP
611	Y	Phosphorylation	Kinase	ABL	P00519	PSP
792	Y	Phosphorylation	Kinase	ABL	P00519	PSP
846	Y	Phosphorylation	Kinase	ABL	P00519	PSP
1449	Y	Phosphorylation	Kinase	ABL	P00519	PSP
1575	Y	Phosphorylation	Kinase	ABL	P00519	PSP
1635	Y	Phosphorylation	Kinase	ABL	P00519	PSP
1772	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
1773	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
1776	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
1779	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
1779	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
608	K	Acetylation		19826488
Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration.

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 MYLK_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MLC1_HUMAN	MLC1	physical	10092231
SRC_HUMAN	SRC	physical	10362724
GOPC_HUMAN	GOPC	physical	25416956
SRC8_HUMAN	CTTN	physical	25241761

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613780	Aortic aneurysm, familial thoracic 7 (AAT7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MYLK_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Arrest defective-1 controls tumor cell behavior by acetylating myosinlight chain kinase."; Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.; PLoS ONE 4:E7451-E7451(2009). Cited for: FUNCTION IN TUMOR CELL MIGRATION, ACETYLATION AT LYS-608 BYNAA10/ARD1, INTERACTION WITH NAA10/ARD1, AND MUTAGENESIS OF LYS-608.	19826488 [Abstract]
Phosphorylation
Reference	PubMed
"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-1779, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1438, AND MASSSPECTROMETRY.	18318008 [Abstract]
"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-1438; SER-1760;SER-1772; THR-1774; SER-1776; THR-1778 AND SER-1779, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chainkinase to regulate endothelial barrier function."; Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E.,Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E.,Imam S.Z., Garcia J.G.N.; Mol. Biol. Cell 21:4042-4056(2010). Cited for: PHOSPHORYLATION AT TYR-231; TYR-464; TYR-556; TYR-611; TYR-792;TYR-846; TYR-1449; TYR-1575 AND TYR-1635 BY ABL1, AND INTERACTION WITHCTTN AND ABL1.	20861316 [Abstract]
"Novel interaction of cortactin with endothelial cell myosin lightchain kinase."; Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N.; Biochem. Biophys. Res. Commun. 298:511-519(2002). Cited for: INTERACTION WITH CTTN, AND PHOSPHORYLATION AT TYR-464 AND TYR-471 BYSRC.	12408982 [Abstract]
"Differential regulation of alternatively spliced endothelial cellmyosin light chain kinase isoforms by p60(Src)."; Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F.,Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.; J. Biol. Chem. 276:8567-8573(2001). Cited for: SEQUENCE REVISION (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 457-476 AND968-985, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION ATTYR-464 AND TYR-471, CALMODULIN-BINDING, AND ENZYME REGULATION.	11113114 [Abstract]

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