LAMA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LAMA2_HUMAN
• UniProt AC: P24043
• Protein Name: Laminin subunit alpha-2
• Gene Name: LAMA2
• Organism: Homo sapiens (Human).
• Sequence Length: 3122
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane. Major component.
• Protein Description: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components..
• Protein Sequence: MPGAAGVLLLLLLSGGLGGVQAQRPQQQRQSQAHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQPVRNPQCRICNQNSSNPNQRHPITNAIDGKNTWWQSPSIKNGIEYHYVTITLDLQQVFQIAYVIVKAANSPRPGNWILERSLDDVEYKPWQYHAVTDTECLTLYNIYPRTGPPSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDPSPELLEFTSARYIRLRFQRIRTLNADLMMFAHKDPREIDPIVTRRYYYSVKDISVGGMCICYGHARACPLDPATNKSRCECEHNTCGDSCDQCCPGFHQKPWRAGTFLTKTECEACNCHGKAEECYYDENVARRNLSLNIRGKYIGGGVCINCTQNTAGINCETCTDGFFRPKGVSPNYPRPCQPCHCDPIGSLNEVCVKDEKHARRGLAPGSCHCKTGFGGVSCDRCARGYTGYPDCKACNCSGLGSKNEDPCFGPCICKENVEGGDCSRCKSGFFNLQEDNWKGCDECFCSGVSNRCQSSYWTYGKIQDMSGWYLTDLPGRIRVAPQQDDLDSPQQISISNAEARQALPHSYYWSAPAPYLGNKLPAVGGQLTFTISYDLEEEEEDTERVLQLMIILEGNDLSISTAQDEVYLHPSEEHTNVLLLKEESFTIHGTHFPVRRKEFMTVLANLKRVLLQITYSFGMDAIFRLSSVNLESAVSYPTDGSIAAAVEVCQCPPGYTGSSCESCWPRHRRVNGTIFGGICEPCQCFGHAESCDDVTGECLNCKDHTGGPYCDKCLPGFYGEPTKGTSEDCQPCACPLNIPSNNFSPTCHLDRSLGLICDGCPVGYTGPRCERCAEGYFGQPSVPGGSCQPCQCNDNLDFSIPGSCDSLSGSCLICKPGTTGRYCELCADGYFGDAVDAKNCQPCRCNAGGSFSEVCHSQTGQCECRANVQGQRCDKCKAGTFGLQSARGCVPCNCNSFGSKSFDCEESGQCWCQPGVTGKKCDRCAHGYFNFQEGGCTACECSHLGNNCDPKTGRCICPPNTIGEKCSKCAPNTWGHSITTGCKACNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYPRCNLCDCFLPGTDATTCDSETKKCSCSDQTGQCTCKVNVEGIHCDRCRPGKFGLDAKNPLGCSSCYCFGTTTQCSEAKGLIRTWVTLKAEQTILPLVDEALQHTTTKGIVFQHPEIVAHMDLMREDLHLEPFYWKLPEQFEGKKLMAYGGKLKYAIYFEAREETGFSTYNPQVIIRGGTPTHARIIVRHMAAPLIGQLTRHEIEMTEKEWKYYGDDPRVHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQGRGTTMTPPADLIEKCDCPLGYSGLSCEACLPGFYRLRSQPGGRTPGPTLGTCVPCQCNGHSSLCDPETSICQNCQHHTAGDFCERCALGYYGIVKGLPNDCQQCACPLISSSNNFSPSCVAEGLDDYRCTACPRGYEGQYCERCAPGYTGSPGNPGGSCQECECDPYGSLPVPCDPVTGFCTCRPGATGRKCDGCKHWHAREGWECVFCGDECTGLLLGDLARLEQMVMSINLTGPLPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIVASRTGRNGTISVRALDGPKASIVPSTHHSTSPPGYTILDVDANAMLFVGGLTGKLKKADAVRVITFTGCMGETYFDNKPIGLWNFREKEGDCKGCTVSPQVEDSEGTIQFDGEGYALVSRPIRWYPNISTVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRIQKQANISIVDIDTNQEENIATSSSGNNFGLDLKADDKIYFGGLPTLRNLSMKARPEVNLKKYSGCLKDIEISRTPYNILSSPDYVGVTKGCSLENVYTVSFPKPGFVELSPVPIDVGTEINLSFSTKNESGIILLGSGGTPAPPRRKRRQTGQAYYAILLNRGRLEVHLSTGARTMRKIVIRPEPNLFHDGREHSVHVERTRGIFTVQVDENRRYMQNLTVEQPIEVKKLFVGGAPPEFQPSPLRNIPPFEGCIWNLVINSVPMDFARPVSFKNADIGRCAHQKLREDEDGAAPAEIVIQPEPVPTPAFPTPTPVLTHGPCAAESEPALLIGSKQFGLSRNSHIAIAFDDTKVKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTHTMIPTKINDGQWHKIKIMRSKQEGILYVDGASNRTISPKKADILDVVGMLYVGGLPINYTTRRIGPVTYSIDGCVRNLHMAEAPADLEQPTSSFHVGTCFANAQRGTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTTTTGVLLGISSQKMDGMGIEMIDEKLMFHVDNGAGRFTAVYDAGVPGHLCDGQWHKVTANKIKHRIELTVDGNQVEAQSPNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCIRSLKLTKGTGKPLEVNFAKALELRGVQPVSCPAN

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
48	Phosphorylation	PAVLNLASNALITTN HHHHHHHHCCEEECC	26.29	22210691
55	N-linked_Glycosylation	SNALITTNATCGEKG HCCEEECCCCCCCCC	25.30	UniProtKB CARBOHYD
89	N-linked_Glycosylation	QCRICNQNSSNPNQR CCCCCCCCCCCCCCC	33.15	UniProtKB CARBOHYD
236	Phosphorylation	SPELLEFTSARYIRL CHHHHHHHCHHHHHH	16.47	23403867
237	Phosphorylation	PELLEFTSARYIRLR HHHHHHHCHHHHHHH	18.97	23403867
240	Phosphorylation	LEFTSARYIRLRFQR HHHHCHHHHHHHHHH	7.07	23403867
274	Phosphorylation	DPIVTRRYYYSVKDI CCCCCCEEEEECEEE	11.94	-
275	Phosphorylation	PIVTRRYYYSVKDIS CCCCCEEEEECEEEE	6.35	-
303	N-linked_Glycosylation	CPLDPATNKSRCECE CCCCCCCCHHHCCCC	42.27	UniProtKB CARBOHYD
363	N-linked_Glycosylation	DENVARRNLSLNIRG CHHHHCCCEEEEECC	28.55	16335952
365	Phosphorylation	NVARRNLSLNIRGKY HHHCCCEEEEECCEE	23.95	29978859
380	N-linked_Glycosylation	IGGGVCINCTQNTAG ECCCEEEECCCCCCC	20.04	UniProtKB CARBOHYD
428	Ubiquitination	SLNEVCVKDEKHARR CCCEEEECCHHHHCC	55.85	-
441	Phosphorylation	RRGLAPGSCHCKTGF CCCCCCCCCCCCCCC	10.30	30576142
446	Phosphorylation	PGSCHCKTGFGGVSC CCCCCCCCCCCCCCC	43.04	25367160
452	Phosphorylation	KTGFGGVSCDRCARG CCCCCCCCCCCCCCC	17.36	25367160
470	N-linked_Glycosylation	YPDCKACNCSGLGSK CCCCCCCCCCCCCCC	28.05	UniProtKB CARBOHYD
746	N-linked_Glycosylation	WPRHRRVNGTIFGGI CCCCCCCCCEEECCC	39.83	UniProtKB CARBOHYD
897	Phosphorylation	KPGTTGRYCELCADG CCCCCCCCCCCCCCC	7.51	-
905	Phosphorylation	CELCADGYFGDAVDA CCCCCCCCCCCCCCC	12.63	-
1061	N-linked_Glycosylation	TTGCKACNCSTVGSL CCCCCCCCCCCCCEE	27.86	UniProtKB CARBOHYD
1249	Phosphorylation	EGKKLMAYGGKLKYA CCEEEEEECCEEEEE	16.67	30576142
1255	Phosphorylation	AYGGKLKYAIYFEAR EECCEEEEEEEEEEC	14.52	18083107
1258	Phosphorylation	GKLKYAIYFEAREET CEEEEEEEEEECHHC	6.28	-
1270	Phosphorylation	EETGFSTYNPQVIIR HHCCCCCCCCEEEEE	24.52	-
1358	Phosphorylation	QSRISEISMEVAEQG HHHHEEHHHHHHHCC	12.58	19664995
1368	Phosphorylation	VAEQGRGTTMTPPAD HHHCCCCCCCCCCHH	16.42	21406692
1369	Phosphorylation	AEQGRGTTMTPPADL HHCCCCCCCCCCHHH	23.13	19664995
1371	Phosphorylation	QGRGTTMTPPADLIE CCCCCCCCCCHHHHH	24.83	21406692
1595	Phosphorylation	RLEQMVMSINLTGPL HHHHHHHHCCCCCCC	9.27	23663014
1597	N-linked_Glycosylation	EQMVMSINLTGPLPA HHHHHHCCCCCCCCC	25.01	UniProtKB CARBOHYD
1599	Phosphorylation	MVMSINLTGPLPAPY HHHHCCCCCCCCCCH	32.06	23663014
1606	Phosphorylation	TGPLPAPYKMLYGLE CCCCCCCHHHHHCHH	15.90	23663014
1610	Phosphorylation	PAPYKMLYGLENMTQ CCCHHHHHCHHHHHH	19.03	23663014
1614	N-linked_Glycosylation	KMLYGLENMTQELKH HHHHCHHHHHHHHHH	43.79	UniProtKB CARBOHYD
1616	Phosphorylation	LYGLENMTQELKHLL HHCHHHHHHHHHHHH	30.39	23663014
1624	Phosphorylation	QELKHLLSPQRAPER HHHHHHHCCCCCCHH	25.91	24719451
1676	Acetylation	ERTNTRAKSLGEFIK HHHHHHHHHHHHHHH	42.81	19816775
1683	Acetylation	KSLGEFIKELARDAE HHHHHHHHHHHHCHH	52.58	7367691
1700	N-linked_Glycosylation	NEKAIKLNETLGTRD HHHHHHHHHCCCCHH	34.89	UniProtKB CARBOHYD
1756	Acetylation	ALLKKVKKLFGESRG HHHHHHHHHHCCCCC	52.62	19413330
1810	N-linked_Glycosylation	LFAVNQKNMTALEKK HHEECCCCCHHHHHH	24.23	UniProtKB CARBOHYD
1878	Phosphorylation	NDKIDDLSQEIKDRK HHHHHHHHHHHHHHH	32.53	27499020
1901	N-linked_Glycosylation	ESHAAQLNDSSAVLD HHHHHHCCCHHHHHH	34.73	19159218
1916	N-linked_Glycosylation	GILDEAKNISFNATA HHHHHHHHCCCCHHH	42.03	19159218
1920	N-linked_Glycosylation	EAKNISFNATAAFKA HHHHCCCCHHHHHHH	29.59	19159218
1943	Methylation	DEAEKVAKEAKDLAH HHHHHHHHHHHHHHH	62.28	23644510
2017	N-linked_Glycosylation	GDLLRTLNDTLGKLS CCHHHHHHHHHHHHH	39.34	19159218
2028	N-linked_Glycosylation	GKLSAIPNDTAAKLQ HHHHCCCCCHHHHHH	53.83	UniProtKB CARBOHYD
2038	Ubiquitination	AAKLQAVKDKARQAN HHHHHHHHHHHHHCH	57.43	-
2040	Ubiquitination	KLQAVKDKARQANDT HHHHHHHHHHHCHHH	39.49	-
2045	N-linked_Glycosylation	KDKARQANDTAKDVL HHHHHHCHHHHHHHH	38.54	UniProtKB CARBOHYD
2126	N-linked_Glycosylation	LEDNLKKNISEIKEL HHHHHHHCHHHHHHH	41.24	UniProtKB CARBOHYD
2205	Phosphorylation	EMRKGKVSFLWDVGS CCCCCCEEEEEECCC	20.36	-
2212	Phosphorylation	SFLWDVGSGVGRVEY EEEEECCCCCCEEEC	30.10	-
2237	Phosphorylation	YRIVASRTGRNGTIS EEEEEECCCCCCEEE	37.69	30622161
2240	N-linked_Glycosylation	VASRTGRNGTISVRA EEECCCCCCEEEEEE	53.99	UniProtKB CARBOHYD
2360	N-linked_Glycosylation	RPIRWYPNISTVMFK CCEEECCCCCEEEEE	25.75	UniProtKB CARBOHYD
2435	N-linked_Glycosylation	SRIQKQANISIVDID HHHHHHCCEEEEECC	26.50	UniProtKB CARBOHYD
2478	N-linked_Glycosylation	GGLPTLRNLSMKARP CCHHHHCCCCCCCCC	39.31	UniProtKB CARBOHYD
2504	Phosphorylation	KDIEISRTPYNILSS CEEEECCCCCCCCCC	24.27	24043423
2506	Phosphorylation	IEISRTPYNILSSPD EEECCCCCCCCCCCC	17.77	24043423
2510	Phosphorylation	RTPYNILSSPDYVGV CCCCCCCCCCCEECC	35.71	24043423
2511	Phosphorylation	TPYNILSSPDYVGVT CCCCCCCCCCEECCC	20.53	24043423
2514	Phosphorylation	NILSSPDYVGVTKGC CCCCCCCEECCCCCC	11.50	24043423
2518	Phosphorylation	SPDYVGVTKGCSLEN CCCEECCCCCCCCCC	18.78	24043423
2551	N-linked_Glycosylation	IDVGTEINLSFSTKN EECCCEEEEEEECCC	24.33	UniProtKB CARBOHYD
2558	N-linked_Glycosylation	NLSFSTKNESGIILL EEEEECCCCCCEEEE	49.07	UniProtKB CARBOHYD
2567	Phosphorylation	SGIILLGSGGTPAPP CCEEEECCCCCCCCC	33.74	-
2581	Phosphorylation	PRRKRRQTGQAYYAI CCHHHCCCCCEEHHH	29.47	21712546
2600	Phosphorylation	GRLEVHLSTGARTMR CCEEEEECCCCCEEE	15.21	23403867
2601	Phosphorylation	RLEVHLSTGARTMRK CEEEEECCCCCEEEE	41.02	23403867
2648	N-linked_Glycosylation	ENRRYMQNLTVEQPI CCCCEECCCEECCCE	22.58	19159218
2658	Ubiquitination	VEQPIEVKKLFVGGA ECCCEEEEEEECCCC	30.85	21906983
2691	Phosphorylation	IWNLVINSVPMDFAR CHHHHCCCCCCCCCC	19.24	22496350
2741	O-linked_Glycosylation	VPTPAFPTPTPVLTH CCCCCCCCCCCCCCC	33.08	OGP
2743	O-linked_Glycosylation	TPAFPTPTPVLTHGP CCCCCCCCCCCCCCC	28.62	OGP
2747	O-linked_Glycosylation	PTPTPVLTHGPCAAE CCCCCCCCCCCCCCC	25.64	OGP
2772	Phosphorylation	QFGLSRNSHIAIAFD ECCCCCCCEEEEEEC	18.37	20044836
2781	Phosphorylation	IAIAFDDTKVKNRLT EEEEECCCCCCCCEE	39.31	20044836
2856	Ubiquitination	KIKIMRSKQEGILYV EEEEEECCCCCEEEE	41.84	2190698
2868	N-linked_Glycosylation	LYVDGASNRTISPKK EEECCCCCCCCCCCC	44.58	UniProtKB CARBOHYD
2872	Phosphorylation	GASNRTISPKKADIL CCCCCCCCCCCCCHH	30.01	24719451
2886	Phosphorylation	LDVVGMLYVGGLPIN HHHCCHHEECCCCCC	6.53	-
2893	N-linked_Glycosylation	YVGGLPINYTTRRIG EECCCCCCCCCCCCC	26.59	UniProtKB CARBOHYD
2894	Phosphorylation	VGGLPINYTTRRIGP ECCCCCCCCCCCCCC	15.37	-
2951	Ubiquitination	FDGTGFAKAVGGFKV CCCCCCHHHCCCEEE	41.15	-
2974	Phosphorylation	EFRTTTTTGVLLGIS EEEECCCCCCEEEEE	24.17	-
3107	Ubiquitination	PLEVNFAKALELRGV CEEEEEHHHHEECCC	49.74	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LAMA2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LAMA2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LAMA2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of LAMA2_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 607855: Merosin-deficient congenital muscular dystrophy 1A (MDC1A)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1901; ASN-1916; ASN-1920;ASN-2017 AND ASN-2648, AND MASS SPECTROMETRY.
PubMed: 19159218

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363, AND MASSSPECTROMETRY.
PubMed: 16335952