LAMB4_HUMAN - dbPTM
LAMB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAMB4_HUMAN
UniProt AC A4D0S4
Protein Name Laminin subunit beta-4
Gene Name LAMB4
Organism Homo sapiens (Human).
Sequence Length 1761
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane.
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 MQFQLTLFLHLGWLSYSKAQDDCNRGACHPTTGDLLVGRNTQLMASSTCGLSRAQKYCILSYLEGEQKCFICDSRFPYDPYDQPNSHTIENVIVSFEPDREKKWWQSENGLDHVSIRLDLEALFRFSHLILTFKTFRPAAMLVERSTDYGHNWKVFKYFAKDCATSFPNITSGQAQGVGDIVCDSKYSDIEPSTGGEVVLKVLDPSFEIENPYSPYIQDLVTLTNLRINFTKLHTLGDALLGRRQNDSLDKYYYALYEMIVRGSCFCNGHASECRPMQKMRGDVFSPPGMVHGQCVCQHNTDGPNCERCKDFFQDAPWRPAADLQDNACRSCSCNSHSSRCHFDMTTYLASGGLSGGVCEDCQHNTEGQHCDRCRPLFYRDPLKTISDPYACIPCECDPDGTISGGICVSHSDPALGSVAGQCLCKENVEGAKCDQCKPNHYGLSATDPLGCQPCDCNPLGSLPFLTCDVDTGQCLCLSYVTGAHCEECTVGYWGLGNHLHGCSPCDCDIGGAYSNVCSPKNGQCECRPHVTGRSCSEPAPGYFFAPLNFYLYEAEEATTLQGLAPLGSETFGQSPAVHVVLGEPVPGNPVTWTGPGFARVLPGAGLRFAVNNIPFPVDFTIAIHYETQSAADWTVQIVVNPPGGSEHCIPKTLQSKPQSFALPAATRIMLLPTPICLEPDVQYSIDVYFSQPLQGESHAHSHVLVDSLGLIPQINSLENFCSKQDLDEYQLHNCVEIASAMGPQVLPGACERLIISMSAKLHDGAVACKCHPQGSVGSSCSRLGGQCQCKPLVVGRCCDRCSTGSYDLGHHGCHPCHCHPQGSKDTVCDQVTGQCPCHGEVSGRRCDRCLAGYFGFPSCHPCPCNRFAELCDPETGSCFNCGGFTTGRNCERCIDGYYGNPSSGQPCRPCLCPDDPSSNQYFAHSCYQNLWSSDVICNCLQGYTGTQCGECSTGFYGNPRISGAPCQPCACNNNIDVTDPESCSRVTGECLRCLHNTQGANCQLCKPGHYGSALNQTCRRCSCHASGVSPMECPPGGGACLCDPVTGACPCLPNVTGLACDRCADGYWNLVPGRGCQSCDCDPRTSQSSHCDQLTGQCPCKLGYGGKRCSECQENYYGDPPGRCIPCDCNRAGTQKPICDPDTGMCRCREGVSGQRCDRCARGHSQEFPTCLQCHLCFDQWDHTISSLSKAVQGLMRLAANMEDKRETLPVCEADFKDLRGNVSEIERILKHPVFPSGKFLKVKDYHDSVRRQIMQLNEQLKAVYEFQDLKDTIERAKNEADLLLEDLQEEIDLQSSVLNASIADSSENIKKYYHISSSAEKKINETSSTINTSANTRNDLLTILDTLTSKGNLSLERLKQIKIPDIQILNEKVCGDPGNVPCVPLPCGGALCTGRKGHRKCRGPGCHGSLTLSTNALQKAQEAKSIIRNLDKQVRGLKNQIESISEQAEVSKNNALQLREKLGNIRNQSDSEEENINLFIKKVKNFLLEENVPPEDIEKVANGVLDIHLPIPSQNLTDELVKIQKHMQLCEDYRTDENRLNEEADGAQKLLVKAKAAEKAANILLNLDKTLNQLQQAQITQGRANSTITQLTANITKIKKNVLQAENQTREMKSELELAKQRSGLEDGLSLLQTKLQRHQDHAVNAKVQAESAQHQAGSLEKEFVELKKQYAILQRKTSTTGLTKETLGKVKQLKDAAEKLAGDTEAKIRRITDLERKIQDLNLSRQAKADQLRILEDQVVAIKNEIVEQEKKYARCYS
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
41PhosphorylationDLLVGRNTQLMASST
CEECCCCCHHHHCCC
23.0121406692
46PhosphorylationRNTQLMASSTCGLSR
CCCHHHHCCCCCCHH
16.5321406692
47PhosphorylationNTQLMASSTCGLSRA
CCHHHHCCCCCCHHH
20.4121406692
48PhosphorylationTQLMASSTCGLSRAQ
CHHHHCCCCCCHHHH
14.2221406692
52PhosphorylationASSTCGLSRAQKYCI
HCCCCCCHHHHHHHH
15.7421406692
57PhosphorylationGLSRAQKYCILSYLE
CCHHHHHHHHHHHHC
3.4521406692
61PhosphorylationAQKYCILSYLEGEQK
HHHHHHHHHHCCCCE
14.0421406692
62PhosphorylationQKYCILSYLEGEQKC
HHHHHHHHHCCCCEE
12.8221406692
169N-linked_GlycosylationDCATSFPNITSGQAQ
HHHHCCCCCCCCCCC
48.43UniProtKB CARBOHYD
188PhosphorylationIVCDSKYSDIEPSTG
EEECCCCCCCCCCCC
35.5330631047
194PhosphorylationYSDIEPSTGGEVVLK
CCCCCCCCCCEEEEE
60.9830631047
229N-linked_GlycosylationTLTNLRINFTKLHTL
HHHCCCEEEEEECCH
31.91UniProtKB CARBOHYD
246N-linked_GlycosylationALLGRRQNDSLDKYY
HHCCCCCCCCHHHHH
38.74UniProtKB CARBOHYD
248PhosphorylationLGRRQNDSLDKYYYA
CCCCCCCCHHHHHHH
46.12-
252PhosphorylationQNDSLDKYYYALYEM
CCCCHHHHHHHHHHH
11.0222210691
253PhosphorylationNDSLDKYYYALYEMI
CCCHHHHHHHHHHHH
6.4922210691
254PhosphorylationDSLDKYYYALYEMIV
CCHHHHHHHHHHHHH
6.24-
257PhosphorylationDKYYYALYEMIVRGS
HHHHHHHHHHHHHCC
8.69-
272PhosphorylationCFCNGHASECRPMQK
CCCCCCHHHCCCCHH
31.3922210691
331PhosphorylationLQDNACRSCSCNSHS
HCCCCCHHCCCCCCC
15.40-
336PhosphorylationCRSCSCNSHSSRCHF
CHHCCCCCCCCCCCC
29.13-
338PhosphorylationSCSCNSHSSRCHFDM
HCCCCCCCCCCCCCH
21.21-
339PhosphorylationCSCNSHSSRCHFDMT
CCCCCCCCCCCCCHH
33.24-
667PhosphorylationSFALPAATRIMLLPT
CCCCCCHHEEEEECC
23.8824719451
674PhosphorylationTRIMLLPTPICLEPD
HEEEEECCCEECCCC
25.8426853621
843PhosphorylationCPCHGEVSGRRCDRC
CCCCCCCCCCCCCCC
23.45-
1016N-linked_GlycosylationGHYGSALNQTCRRCS
CCHHHHHHHHCCCCC
34.53UniProtKB CARBOHYD
1055N-linked_GlycosylationGACPCLPNVTGLACD
CCCCCCCCCCCCCCC
30.91UniProtKB CARBOHYD
1105PhosphorylationQCPCKLGYGGKRCSE
CCCCCCCCCCCCCHH
32.89-
1135PhosphorylationCDCNRAGTQKPICDP
CCCCCCCCCCCCCCC
32.22-
1154PhosphorylationCRCREGVSGQRCDRC
CCCCCCCCCCCCCCC
39.81-
1223N-linked_GlycosylationDFKDLRGNVSEIERI
HHHHHCCCHHHHHHH
27.92UniProtKB CARBOHYD
1301N-linked_GlycosylationDLQSSVLNASIADSS
HHHHHHHHHHHCCCC
29.50UniProtKB CARBOHYD
1314PhosphorylationSSENIKKYYHISSSA
CCCHHHHHHCCCHHH
8.6929083192
1315PhosphorylationSENIKKYYHISSSAE
CCHHHHHHCCCHHHH
11.1029083192
1318PhosphorylationIKKYYHISSSAEKKI
HHHHHCCCHHHHHHH
12.6229083192
1319PhosphorylationKKYYHISSSAEKKIN
HHHHCCCHHHHHHHC
32.7229083192
1320PhosphorylationKYYHISSSAEKKINE
HHHCCCHHHHHHHCC
33.3929083192
1326N-linked_GlycosylationSSAEKKINETSSTIN
HHHHHHHCCCCCCCC
56.21UniProtKB CARBOHYD
1329PhosphorylationEKKINETSSTINTSA
HHHHCCCCCCCCCCC
21.21-
1330PhosphorylationKKINETSSTINTSAN
HHHCCCCCCCCCCCC
40.5025332170
1333N-linked_GlycosylationNETSSTINTSANTRN
CCCCCCCCCCCCCHH
28.24UniProtKB CARBOHYD
1335PhosphorylationTSSTINTSANTRNDL
CCCCCCCCCCCHHHH
18.2925332170
1354N-linked_GlycosylationDTLTSKGNLSLERLK
HHHHCCCCCCHHHHH
30.14UniProtKB CARBOHYD
1469N-linked_GlycosylationEKLGNIRNQSDSEEE
HHHCCCCCCCCCHHH
41.74UniProtKB CARBOHYD
1517N-linked_GlycosylationHLPIPSQNLTDELVK
ECCCCCCCCHHHHHH
49.61UniProtKB CARBOHYD
1587N-linked_GlycosylationQITQGRANSTITQLT
HHHCCCCCHHHHHHH
38.02UniProtKB CARBOHYD
1596N-linked_GlycosylationTITQLTANITKIKKN
HHHHHHHHHHHHHHH
36.91UniProtKB CARBOHYD
1609N-linked_GlycosylationKNVLQAENQTREMKS
HHHHHHHHHHHHHHH
52.09UniProtKB CARBOHYD
1636PhosphorylationDGLSLLQTKLQRHQD
HHHHHHHHHHHHHHH
33.42-
1689PhosphorylationTTGLTKETLGKVKQL
CCCCCHHHHHHHHHH
42.22-
1707PhosphorylationAEKLAGDTEAKIRRI
HHHHCCCHHHHHHHH
36.6023403867
1725N-linked_GlycosylationERKIQDLNLSRQAKA
HHHHHHCCHHHHHHH
44.23UniProtKB CARBOHYD

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 LAMB4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMB4_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 LAMB4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LAMB4_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMB4_HUMAN

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Related Literatures of Post-Translational Modification

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