SPTN4_HUMAN - dbPTM
SPTN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPTN4_HUMAN
UniProt AC Q9H254
Protein Name Spectrin beta chain, non-erythrocytic 4
Gene Name SPTBN4
Organism Homo sapiens (Human).
Sequence Length 2564
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Protein Description
Protein Sequence MAQVPGEVDNMEGLPAPNNNPAARWESPDRGWEREQPAASTAAASLFECSRIKALADEREAVQKKTFTKWVNSHLARVGCHIGDLYVDLRDGFVLTRLLEVLSGEQLPRPTRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLVWTIILRFQIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLVDFSKLTKSNANYNLQRAFRTAEQHLGLARLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKALAVEGKRIGKVLDQVLEVGKIIERYEELAAELLAWIHRTVGLISNQKFANSLSGVQQQLQAFTAYCTLEKPVKFQEKGNLEVLLFSIQSKLRACNRRLFVPREGCGIWDIDKAWGELEKAEHEREAALRAELIRQEKLELLAQRFDHKVAMRESWLNENQRLVSQDNFGYELPAVEAAMKKHEAIEADIAAYEERVQGVAELAQALAAEGYYDIRRVAAQRDSVLRQWALLTGLVGARRTRLEQNLALQKVFQEMVYMVDWMEEMQAQLLSRECGQHLVEADDLLQKHGLLEGDIAAQSERVEALNAAALRFSQLQGYQPCDPQVICNRVNHVHGCLAELQEQAARRRAELEASRSLWALLQELEEAESWARDKERLLEAAGGGGAAGAAGAAGTAGGAHDLSSTARLLAQHKILQGELGGRRALLQQALRCGEELVAAGGAVGPGADTVHLVGLAERAASARRRWQRLEEAAARRERRLQEARALHQFGADLDGLLDWLRDAYRLAAAGDFGHDEASSRRLARQHRALTGEVEAHRGPVSGLRRQLATLGGASGAGPLVVALQVRVVEAEQLFAEVTEVAALRRQWLRDALAVYRMFGEVHACELWIGEKEQWLLSMRVPDSLDDVEVVQHRFESLDQEMNSLMGRVLDVNHTVQELVEGGHPSSDEVRSCQDHLNSRWNRIVELVEQRKEEMSAVLLVENHVLEVAEVRAQVREKRRAVESAPRAGGALQWRLSGLEAALQALEPRQAALLEEAALLAERFPAQAARLHQGAEELGAEWGALASAAQACGEAVAAAGRLQRFLHDLDAFLDWLVRAQEAAGGSEGPLPNSLEEADALLARHAALKEEVDQREEDYARIVAASEALLAADGAELGPGLALDEWLPHLELGWHKLLGLWEARREALVQAHIYQLFLRDLRQALVVLRNQEMALSGAELPGTVESVEEALKQHRDFLTTMELSQQKMQVAVQAAEGLLRQGNIYGEQAQEAVTRLLEKNQENQLRAQQWMQKLHDQLELQHFLRDCHELDGWIHEKMLMARDGTREDNHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFEASKADQLVQSFAELDKKLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWYREVGELQAQTAALPLEPASKELVGERQNAVGERLVRLLEPLQERRRLLLASKELHQVAHDLDDELAWVQERLPLAMQTERGNGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGALASLRSPEAEAVRRGLEQLQSAWAGLREAAERRQQVLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRRQSQVDRLYVALKELGEERRVALEQQYWLYQLSRQVSELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETGMAGRERLAAVNQMVDELIECGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSDARELQGQIEEKRRRLPRLTTPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVYAGEHAEAIASREQEVLQGWKELLSACEDARLHVSSTADALRFHSQVRDLLSWMDGIASQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELTTCQELGRSLLLNKSAMADEIQAQLDKLGTRKEEVSEKWDRHWEWLQQMLEVHQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEERFSSLRRLTTIEKIKAEQSKQPPTPLLGRKFFGDPTELAAKAAPLLRPGGYERGLEPLARRASDTLSAEVRTRVGYVRQELKPERLQPRIDRLPEIPGRVEPAALPAAPEDAAETPATPAAAEQVRPRPERQESADRAEELPRRRRPERQESVDQSEEAARRRRPERQESAEHEAAHSLTLGRYEQMERRRERRERRLERQESSEQEMPIRGDLVKGKATLADIVEQLQEKEAGPGLPAGPSLPQPRELPPGRLPNGLELPERTPRPDRPRARDRPKPRRRPRPREGGEGGGSRRSRSAPAQGGSAPAPPPPPTHTVQHEGFLLRKRELDANRKSSNRSWVSLYCVLSKGELGFYKDSKGPASGSTHGGEPLLSLHKATSEVASDYKKKKHVFKLQTQDGSEFLLQAKDEEEMNGWLEAVASSVAEHAEIARWGQTLPTTSSTDEGNPKREGGDRRASGRRK
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
41PhosphorylationREQPAASTAAASLFE
CCCCCHHHHHHHHHH		18.65-
64UbiquitinationDEREAVQKKTFTKWV
HHHHHHHHHHHHHHH		47.3723000965
65UbiquitinationEREAVQKKTFTKWVN
HHHHHHHHHHHHHHH		31.6023000965
69UbiquitinationVQKKTFTKWVNSHLA
HHHHHHHHHHHHHHH		44.9821890473
73PhosphorylationTFTKWVNSHLARVGC
HHHHHHHHHHHHCCC		15.4028857561
131UbiquitinationDKALQFLKEQRVHLE
HHHHHHHHHCCCCCC		53.76-
131AcetylationDKALQFLKEQRVHLE
HHHHHHHHHCCCCCC		53.7622634167
174UbiquitinationQVIKIETEDNRETRS
EEEEEECCCCCCCCC		40.2627667366
179O-linked_GlycosylationETEDNRETRSAKDAL
ECCCCCCCCCHHHHH		27.0429237092
208PhosphorylationNIQNFTTSWRDGLAF
CCCCCCCCCCCHHHH		19.63-
275PhosphorylationPDEKSIITYVVSFYH
CCHHHHHHHHHHHHH		14.4822468782
279PhosphorylationSIITYVVSFYHYFSK
HHHHHHHHHHHHHHH		15.2822468782
285PhosphorylationVSFYHYFSKMKALAV
HHHHHHHHHHHHHHC		25.3622468782
288UbiquitinationYHYFSKMKALAVEGK
HHHHHHHHHHHCCCH		43.9427667366
295UbiquitinationKALAVEGKRIGKVLD
HHHHCCCHHHHHHHH		27.60-
521PhosphorylationLRQWALLTGLVGARR
HHHHHHHHHHHHHHH		29.3523917254
702AcetylationARLLAQHKILQGELG
HHHHHHHHHHCCCCC		32.7919813571
1012PhosphorylationEKRRAVESAPRAGGA
HHHHHHHHCCCCCCH		36.6524719451
1025PhosphorylationGALQWRLSGLEAALQ
CHHHHHHHHHHHHHH		32.5327251275
1431PhosphorylationKKLLHMESQLQDVDP
HHHHHHHHHCCCCCC		28.72-
1454PhosphorylationSQLKKLQSMESQVEE
HHHHHHHHHHHHHHH		34.6528348404
1541PhosphorylationRLPLAMQTERGNGLQ
HHCCCCCCCCCCHHH		17.99-
1583PhosphorylationERAGALASLRSPEAE
HHHCHHHHCCCHHHH		25.7624719451
1673PhosphorylationLEQGVENYEESIAQL
HHHHHHCHHHHHHHH		13.9422210691
1676PhosphorylationGVENYEESIAQLSRQ
HHHCHHHHHHHHHHH		15.9822210691
1681PhosphorylationEESIAQLSRQCRALL
HHHHHHHHHHHHHHH		14.2822210691
1752PhosphorylationEKEVVAGSPELGQDF
HCCHHCCCCCCCCCC		12.8824076635
1861PhosphorylationRRRLPRLTTPPEPRP
HHCCCCCCCCCCCCC		38.24-
1862PhosphorylationRRLPRLTTPPEPRPS
HCCCCCCCCCCCCCC		41.2525332170
1916MethylationHAEAIASREQEVLQG
HHHHHHHHHHHHHHH		40.36115388639
1939PhosphorylationEDARLHVSSTADALR
HHHCCCCCCHHHHHH		15.95-
1941PhosphorylationARLHVSSTADALRFH
HCCCCCCHHHHHHHH		22.5024275569
2007PhosphorylationTCQELGRSLLLNKSA
HHHHHHHHHHCCHHH		22.90-
2012UbiquitinationGRSLLLNKSAMADEI
HHHHHCCHHHHHHHH		39.2930230243
2079PhosphorylationQSRELGSSVDEVEQL
CCHHHCCCHHHHHHH		31.6124076635
2106PhosphorylationAWEERFSSLRRLTTI
HHHHHHHHHHHHHHH		24.1524719451
2111PhosphorylationFSSLRRLTTIEKIKA
HHHHHHHHHHHHHHH		24.7420068231
2112PhosphorylationSSLRRLTTIEKIKAE
HHHHHHHHHHHHHHH		31.5620068231
2121PhosphorylationEKIKAEQSKQPPTPL
HHHHHHHHCCCCCCC		25.4320068231
2126PhosphorylationEQSKQPPTPLLGRKF
HHHCCCCCCCCCCCC		33.0024719451
2132UbiquitinationPTPLLGRKFFGDPTE
CCCCCCCCCCCCHHH		43.1530230243
2165PhosphorylationEPLARRASDTLSAEV
HHHHHHHHHCCCHHH		29.3529978859
2167PhosphorylationLARRASDTLSAEVRT
HHHHHHHCCCHHHHH		21.8129978859
2236PhosphorylationPRPERQESADRAEEL
CCHHHHHHHHHHHHC		27.4224719451
2254PhosphorylationRRPERQESVDQSEEA
CCHHHHHCHHHHHHH		23.7424719451
2272PhosphorylationRRPERQESAEHEAAH
HCHHHHHHHHHHHHH		30.5322985185
2280PhosphorylationAEHEAAHSLTLGRYE
HHHHHHHHHHHHHHH		20.5123312004
2282PhosphorylationHEAAHSLTLGRYEQM
HHHHHHHHHHHHHHH		30.1323312004
2286PhosphorylationHSLTLGRYEQMERRR
HHHHHHHHHHHHHHH		14.5526074081
2305PhosphorylationRRLERQESSEQEMPI
HHHHHHHCCCCCCCC		30.7326471730
2306PhosphorylationRLERQESSEQEMPIR
HHHHHHCCCCCCCCC		42.4126471730
2344PhosphorylationPGLPAGPSLPQPREL
CCCCCCCCCCCCCCC		52.33-
2400PhosphorylationGGSRRSRSAPAQGGS
CCCCCCCCCCCCCCC		39.5925849741
2437PhosphorylationELDANRKSSNRSWVS
HHCCCCCCCCCCCEE		29.6127251275
2438PhosphorylationLDANRKSSNRSWVSL
HCCCCCCCCCCCEEE		39.0227251275
2441PhosphorylationNRKSSNRSWVSLYCV
CCCCCCCCCEEEEEE		35.7627251275
2465PhosphorylationKDSKGPASGSTHGGE
CCCCCCCCCCCCCCC		36.0923879269
2481PhosphorylationLLSLHKATSEVASDY
CHHHHHHHHHHHHHH		30.1729083192
2482PhosphorylationLSLHKATSEVASDYK
HHHHHHHHHHHHHHH		34.6329083192
2486PhosphorylationKATSEVASDYKKKKH
HHHHHHHHHHHCCCC		46.8029083192
2488PhosphorylationTSEVASDYKKKKHVF
HHHHHHHHHCCCCEE		23.3929083192
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 SPTN4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPTN4_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 SPTN4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANK3_HUMANANK3physical
11807096
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 SPTN4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2111; THR-2112 ANDSER-2121, AND MASS SPECTROMETRY.

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