AMOL2_HUMAN - dbPTM
AMOL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMOL2_HUMAN
UniProt AC Q9Y2J4
Protein Name Angiomotin-like protein 2
Gene Name AMOTL2
Organism Homo sapiens (Human).
Sequence Length 779
Subcellular Localization Recycling endosome.
Protein Description Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC..
Protein Sequence MRTLEDSSGTVLHRLIQEQLRYGNLTETRTLLAIQQQALRGGAGTGGTGSPQASLEILAPEDSQVLQQATRQEPQGQEHQGGENHLAENTLYRLCPQPSKGEELPTYEEAKAHSQYYAAQQAGTRPHAGDRDPRGAPGGSRRQDEALRELRHGHVRSLSERLLQLSLERNGARAPSHMSSSHSFPQLARNQQGPPLRGPPAEGPESRGPPPQYPHVVLAHETTTAVTDPRYRARGSPHFQHAEVRILQAQVPPVFLQQQQQYQYLQQSQEHPPPPHPAALGHGPLSSLSPPAVEGPVSAQASSATSGSAHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFAAAAAGTQGWQGLSSSERQTADAPARLTTDRAPTEEPVVTAPPAAHAKHGSRDGSTQTEGPPDSTSTCLPPEPDSLLGCSSSQRAASLDSVATSRVQDLSDMVEILI
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
7Phosphorylation-MRTLEDSSGTVLHR
-CCCCCCCCHHHHHH		22.6920860994
10PhosphorylationTLEDSSGTVLHRLIQ
CCCCCCHHHHHHHHH		23.1146163003
45PhosphorylationALRGGAGTGGTGSPQ
HHHCCCCCCCCCCCC		31.7222199227
48PhosphorylationGGAGTGGTGSPQASL
CCCCCCCCCCCCCEE		35.5122199227
50PhosphorylationAGTGGTGSPQASLEI
CCCCCCCCCCCEEEE		17.4230278072
54PhosphorylationGTGSPQASLEILAPE
CCCCCCCEEEEECCC		22.6830278072
63PhosphorylationEILAPEDSQVLQQAT
EEECCCCHHHHHHHH		22.1120068231
92PhosphorylationHLAENTLYRLCPQPS
CHHHCCHHHHCCCCC		10.254940353
99PhosphorylationYRLCPQPSKGEELPT
HHHCCCCCCCCCCCC		48.3128348404
100UbiquitinationRLCPQPSKGEELPTY
HHCCCCCCCCCCCCH		76.6227667366
106PhosphorylationSKGEELPTYEEAKAH
CCCCCCCCHHHHHHH		57.0725394399
107PhosphorylationKGEELPTYEEAKAHS
CCCCCCCHHHHHHHH		15.1631122319
108PhosphorylationGEELPTYEEAKAHSQ
CCCCCCHHHHHHHHH		54.6927251275
112PhosphorylationPTYEEAKAHSQYYAA
CCHHHHHHHHHHHHH		18.0120068231
157PhosphorylationLRHGHVRSLSERLLQ
HHHCHHHHHHHHHHH		34.8524670416
158UbiquitinationRHGHVRSLSERLLQL
HHCHHHHHHHHHHHH		4.2827667366
159PhosphorylationHGHVRSLSERLLQLS
HCHHHHHHHHHHHHH		23.1622199227
164PhosphorylationSLSERLLQLSLERNG
HHHHHHHHHHHHHCC		33.3327251275
165PhosphorylationLSERLLQLSLERNGA
HHHHHHHHHHHHCCC		6.7827642862
166PhosphorylationSERLLQLSLERNGAR
HHHHHHHHHHHCCCC		18.4122617229
176PhosphorylationRNGARAPSHMSSSHS
HCCCCCCCCCCCCCC		30.7323403867
179PhosphorylationARAPSHMSSSHSFPQ
CCCCCCCCCCCCHHH		24.2223403867
180PhosphorylationRAPSHMSSSHSFPQL
CCCCCCCCCCCHHHH		25.2123403867
181PhosphorylationAPSHMSSSHSFPQLA
CCCCCCCCCCHHHHH		18.8223403867
183PhosphorylationSHMSSSHSFPQLARN
CCCCCCCCHHHHHHH		40.3430278072
197MethylationNQQGPPLRGPPAEGP
HCCCCCCCCCCCCCC		62.44-
217PhosphorylationPPQYPHVVLAHETTT
CCCCCEEEEEEECCC		3.3927251275
224PhosphorylationVLAHETTTAVTDPRY
EEEEECCCCCCCHHH		26.9227251275
236PhosphorylationPRYRARGSPHFQHAE
HHHHCCCCCCCCHHH		15.0630266825
239PhosphorylationRARGSPHFQHAEVRI
HCCCCCCCCHHHHHH		6.9027251275
241PhosphorylationRGSPHFQHAEVRILQ
CCCCCCCHHHHHHHH		23.9419651622
294PhosphorylationSLSPPAVEGPVSAQA
HCCCCCCCCCCCCCC		60.9419691289
341UbiquitinationELESSAEKAGRIEKL
HHHHHHHHHHHHHHH		56.7227667366
341 (in isoform 2)Ubiquitination-56.72-
347UbiquitinationEKAGRIEKLESEIQR
HHHHHHHHHHHHHHH		56.0033845483
375O-linked_GlycosylationKREALEKTMRNKMDS
HHHHHHHHHHHHHHH		16.4030379171
399UbiquitinationRDLRERLESANRRLA
HHHHHHHHHHHHHHH		54.7727667366
405UbiquitinationLESANRRLASKTQEA
HHHHHHHHHHHHHHH		5.9533845483
408 (in isoform 1)Ubiquitination-48.9321906983
408 (in isoform 2)Ubiquitination-48.93-
408UbiquitinationANRRLASKTQEAQAG
HHHHHHHHHHHHHHC		48.932190698
422UbiquitinationGSQDMVAKLLAQSYE
CCHHHHHHHHHHHHH		32.4029967540
436UbiquitinationEQQQEQEKLEREMAL
HHHHHHHHHHHHHHH		56.1729967540
466UbiquitinationEQALGNAQGRAARAE
HHHHHHHHHHHHHHH		46.0023503661
466 (in isoform 2)Ubiquitination-46.0021906983
480UbiquitinationEEELRKKQAYVEKVE
HHHHHHHHHHHHHHH		40.7529967540
494UbiquitinationERLQQALGQLQAACE
HHHHHHHHHHHHHHH		29.2129967540
502UbiquitinationQLQAACEKREQLELR
HHHHHHHHHHHHHHH		62.2129967540
512PhosphorylationQLELRLRTRLEQELK
HHHHHHHHHHHHHHH		44.1727470641
519SumoylationTRLEQELKALRAQQR
HHHHHHHHHHHHHHH		44.62-
534PhosphorylationQAGAPGGSSGSGGSP
HHCCCCCCCCCCCCH		37.1230183078
535PhosphorylationAGAPGGSSGSGGSPE
HCCCCCCCCCCCCHH		40.0130183078
537PhosphorylationAPGGSSGSGGSPELS
CCCCCCCCCCCHHHH		41.7629255136
540PhosphorylationGSSGSGGSPELSALR
CCCCCCCCHHHHHHH		20.8019664994
544PhosphorylationSGGSPELSALRLSEQ
CCCCHHHHHHHHHHH		24.4829255136
560UbiquitinationREKEEQILALEADMT
HHHHHHHHHHHCCCH		4.4329967540
566UbiquitinationILALEADMTKWEQKY
HHHHHCCCHHHHHHH		5.5332015554
567PhosphorylationLALEADMTKWEQKYL
HHHHCCCHHHHHHHH		33.2929052541
568UbiquitinationALEADMTKWEQKYLE
HHHCCCHHHHHHHHH		41.9432015554
573PhosphorylationMTKWEQKYLEERAMR
CHHHHHHHHHHHHHH		21.027343357
592PhosphorylationDAAATAAAQRDTTLI
HHHHHHHHHCCCCEE		11.5020068231
596PhosphorylationTAAAQRDTTLIRHSP
HHHHHCCCCEEECCC		26.2023927012
597PhosphorylationAAAQRDTTLIRHSPQ
HHHHCCCCEEECCCC		25.2023927012
598PhosphorylationAAQRDTTLIRHSPQP
HHHCCCCEEECCCCC		3.3419664994
602PhosphorylationDTTLIRHSPQPSPSS
CCCEEECCCCCCCCC		18.5123927012
606PhosphorylationIRHSPQPSPSSSFNE
EECCCCCCCCCCCCC		31.9723927012
608PhosphorylationHSPQPSPSSSFNEGL
CCCCCCCCCCCCCCC		42.8423927012
609PhosphorylationSPQPSPSSSFNEGLL
CCCCCCCCCCCCCCC		42.1923927012
610PhosphorylationPQPSPSSSFNEGLLT
CCCCCCCCCCCCCCC		36.1123927012
617PhosphorylationSFNEGLLTGGHRHQE
CCCCCCCCCCHHHHH		46.2724732914
626UbiquitinationGHRHQEMESRLKVLH
CHHHHHHHHHHHHHH		31.7732015554
628UbiquitinationRHQEMESRLKVLHAQ
HHHHHHHHHHHHHHH		25.8129967540
630UbiquitinationQEMESRLKVLHAQIL
HHHHHHHHHHHHHHH		41.4629967540
655PhosphorylationQRSRRDPGKAIQGSL
HHHCCCCCCCCCCCC		35.9920068231
660PhosphorylationDPGKAIQGSLRPAKS
CCCCCCCCCCCCCCC		23.6427251275
661PhosphorylationPGKAIQGSLRPAKSV
CCCCCCCCCCCCCCC		12.5819691289
664PhosphorylationAIQGSLRPAKSVPSV
CCCCCCCCCCCCCCH		49.7020068231
665PhosphorylationIQGSLRPAKSVPSVF
CCCCCCCCCCCCCHH		15.4332142685
666PhosphorylationQGSLRPAKSVPSVFA
CCCCCCCCCCCCHHH		55.4527251275
667PhosphorylationGSLRPAKSVPSVFAA
CCCCCCCCCCCHHHH		41.1722617229
670PhosphorylationRPAKSVPSVFAAAAA
CCCCCCCCHHHHHHH		27.9329507054
679PhosphorylationFAAAAAGTQGWQGLS
HHHHHHCCCCCCCCC		21.1227542207
688UbiquitinationGWQGLSSSERQTADA
CCCCCCHHHCCCCCC		33.1629967540
719PhosphorylationTAPPAAHAKHGSRDG
CCCCHHHCCCCCCCC		10.7919691289
723PhosphorylationAAHAKHGSRDGSTQT
HHHCCCCCCCCCCCC		27.2427050516
725PhosphorylationHAKHGSRDGSTQTEG
HCCCCCCCCCCCCCC		58.0332142685
753PhosphorylationDSLLGCSSSQRAASL
CCCCCCCHHHHCCCC		34.2710952955
759PhosphorylationSSSQRAASLDSVATS
CHHHHCCCCCHHHHH		31.5530266825
760PhosphorylationSSQRAASLDSVATSR
HHHHCCCCCHHHHHH		4.9524719451
762PhosphorylationQRAASLDSVATSRVQ
HHCCCCCHHHHHHHC		20.9530266825
765PhosphorylationASLDSVATSRVQDLS
CCCCHHHHHHHCCHH		18.2123403867
766PhosphorylationSLDSVATSRVQDLSD
CCCHHHHHHHCCHHH		22.2523403867
817Phosphorylation---------------------------------------------
---------------------------------------------		19691289
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
107YPhosphorylationKinaseFGFR1P11362
Uniprot
159SPhosphorylationKinaseLATS2Q9NRM7
PSP
759SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMOL2_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 AMOL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCC1_HUMANGCC1physical
16189514
K1C20_HUMANKRT20physical
16189514
MGN2_HUMANMAGOHBphysical
16189514
AMOL2_HUMANAMOTL2physical
16189514
LATS2_HUMANLATS2physical
21832154
YAP1_HUMANYAP1physical
21832154
CG043_HUMANC7orf43physical
24255178
DYL1_HUMANDYNLL1physical
24255178
INADL_HUMANINADLphysical
24255178
LIN7C_HUMANLIN7Cphysical
24255178
MPDZ_HUMANMPDZphysical
24255178
MPP5_HUMANMPP5physical
24255178
MERL_HUMANNF2physical
24255178
PARD3_HUMANPARD3physical
24255178
PRS6A_HUMANPSMC3physical
24255178
PSMD9_HUMANPSMD9physical
24255178
SMD2_HUMANSNRPD2physical
24255178
ASPP2_HUMANTP53BP2physical
24255178
TPC10_HUMANTRAPPC10physical
24255178
TPPC3_HUMANTRAPPC3physical
24255178
TPPC9_HUMANTRAPPC9physical
24255178
AMOL2_HUMANAMOTL2physical
25416956
K1C20_HUMANKRT20physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
BRE1A_HUMANRNF20physical
25416956
CARD9_HUMANCARD9physical
25416956
F184A_HUMANFAM184Aphysical
25416956
RASF5_HUMANRASSF5physical
25416956
BRM1L_HUMANBRMS1Lphysical
25416956
ZGPAT_HUMANZGPATphysical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
SH3R2_HUMANSH3RF2physical
25416956
MIC19_HUMANCHCHD3physical
21516116
RA51D_HUMANRAD51Dphysical
21516116
YAP1_HUMANYAP1physical
26598551
USP9X_HUMANUSP9Xphysical
26598551
LATS2_HUMANLATS2physical
26598551
USP9X_HUMANUSP9Xphysical
28720576
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 AMOL2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND MASSSPECTROMETRY.

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