| Tag |
Content |
LipidDB ID |
LipidDB-9986-00832 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
5.79 |
Molecular Weight |
138413.39 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform |
Protein Synonyms/Alias |
Phosphorylase kinase alpha M subunit; |
Gene Name |
PHKA1 |
Gene Synonyms/Alias |
|
Created Date |
01-NOV-1990 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
1234 | Canonical | EFLPHSICAMQ**** | [1] | S-Farnesylation |
|
Organism |
Oryctolagus cuniculus (Rabbit) |
NCBI Taxa ID |
9986 |
Reference |
[1] Heilmeyer LM Jr, Serwe M, Weber C, Metzger J, Hoffmann-Posorske E, Meyer HE.Farnesylcysteine, a constituent of the alpha and beta subunits of rabbit skeletalmuscle phosphorylase kinase: localization by conversion to S-ethylcysteine and bytandem mass spectrometry. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9554-8.[ PMID:1409665]
|
Functional Description |
Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin. |
Sequence Annotation |
Region: 810 840 Calmodulin-binding.
Region: 1060 1100 Calmodulin-binding.
Functional site: 1234 1234 Not methylated.
Modified residue: 735 735 Phosphoserine.
Modified residue: 758 758 Phosphoserine.
Modified residue: 972 972 Phosphoserine; by autocatalysis.
Modified residue: 985 985 Phosphoserine; by autocatalysis.
Modified residue: 1007 1007 Phosphoserine; by autocatalysis.
Modified residue: 1018 1018 Phosphoserine; by PKA.
Modified residue: 1020 1020 Phosphoserine.
Modified residue: 1023 1023 Phosphoserine.
Modified residue: 1030 1030 Phosphoserine.
|
Protein Length |
1237 AA. |
Protein Sequence
(Canonical) |
MRSRSNSGVR LDSYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA 60
YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT 120
CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD 180
FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS 240
ILNSLLPRAS TSKEVDASLL SVISFPAFAV EDSKLVEITK QEIITKLQGR YGCCRFLRDG 300
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE YREALEAVLI 360
KGKNGVPLLP ELYSVPPDKV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP 420
GEIDPLNRRF STVPKPDVVV QVSILAETEE IKAILKDKGI NVETIAEVYP IRVQPARILS 480
HIYSSLGCNN RMKLSGRPYR HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV 540
EMLRTDLSYL CSRWRMTGQP TITFPISQTM LDEDGTSLNS SILAALRKMQ DGYFGGARIQ 600
TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDELE SGDWMDGYNS TSTARCGDEV 660
ARYLDHLLAH TAPHPKLAPA SQKGGLNRFR AAVQTTCDLM SLVTKAKELH VQNVHMYLPT 720
KLFQASRPSL NLLDSSHPSQ EDQVPTVRVE VHLPRDQSGE VDFQALVLQL KETSSLQEQA 780
DILYMLYTMK GPDWDTELYE EGSATVRELL TELYGKVGKI RHWGLIRYIS GILRKKVEAL 840
DEACTDLLSH QKHLTVGLPP EPREKTISAP LPYEALTRLI EEACEGDMNI SILTQEIMVY 900
LAMYMRTQPG LFAEMFRLRI GLIIQVMATE LAHSLRCSAE EATEGLMNLS PSAMKNLLHH 960
ILSGKEFGVE RSVRPTDSNV SPAISIHEIG AVGATKTERT GIMQLKSEIK QVEFRRLSIS 1020
TESQPNGGHS LGADLMSPSF LSPGTSVTPS SGSFPGHHTS KDSRQGQWQR RRRLDGALNR 1080
VPIGFYQKVW KVLQKCHGLS VEGFVLPSST TREMTPGEIK FSVHVESVLN RVPQPEYRQL 1140
LVEAILVLTM LADIEIHSIG SIIAVEKIVH IANDLFLQEQ KTLGADDIML AKDPASGICT 1200
LLYDSAPSGR FGTMTYLSKA AATYVQEFLP HSICAMQ 1237
|
FASTA
(Canonical) |
>LipidDB-9986-00832|P18688
MRSRSNSGVRLDSYARLVQQTILCHQNPVTGLLPASYDQKDAWVRDNVYSILAVWGLGLA
YRKNADRDEDKAKAYELEQSVVKLMRGLLHCMIRQVDKVESFKYSQSTKDSLHAKYNTKT
CATVVGDDQWGHLQLDATSVYLLFLAQMTASGLHIIHSLDEVNFIQNLVFYIEAAYKTAD
FGIWERGDKTNQGISELNASSVGMAKAALEALDELDLFGVKGGPQSVIHVLADEVQHCQS
ILNSLLPRASTSKEVDASLLSVISFPAFAVEDSKLVEITKQEIITKLQGRYGCCRFLRDG
YKTPKEDPNRLYYEPAELKLFENIECEWPLFWTYFILDGVFSGNAEQVQEYREALEAVLI
KGKNGVPLLPELYSVPPDKVDEEYQNPHTVDRVPMGKLPHMWGQSLYILGSLMAEGFLAP
GEIDPLNRRFSTVPKPDVVVQVSILAETEEIKAILKDKGINVETIAEVYPIRVQPARILS
HIYSSLGCNNRMKLSGRPYRHMGVLGTSKLYDIRKTIFTFTPQFIDQQQFYLALDNKMIV
EMLRTDLSYLCSRWRMTGQPTITFPISQTMLDEDGTSLNSSILAALRKMQDGYFGGARIQ
TGKLSEFLTTSCCTHLSFMDPGPEGKLYSEDYDDNYDELESGDWMDGYNSTSTARCGDEV
ARYLDHLLAHTAPHPKLAPASQKGGLNRFRAAVQTTCDLMSLVTKAKELHVQNVHMYLPT
KLFQASRPSLNLLDSSHPSQEDQVPTVRVEVHLPRDQSGEVDFQALVLQLKETSSLQEQA
DILYMLYTMKGPDWDTELYEEGSATVRELLTELYGKVGKIRHWGLIRYISGILRKKVEAL
DEACTDLLSHQKHLTVGLPPEPREKTISAPLPYEALTRLIEEACEGDMNISILTQEIMVY
LAMYMRTQPGLFAEMFRLRIGLIIQVMATELAHSLRCSAEEATEGLMNLSPSAMKNLLHH
ILSGKEFGVERSVRPTDSNVSPAISIHEIGAVGATKTERTGIMQLKSEIKQVEFRRLSIS
TESQPNGGHSLGADLMSPSFLSPGTSVTPSSGSFPGHHTSKDSRQGQWQRRRRLDGALNR
VPIGFYQKVWKVLQKCHGLSVEGFVLPSSTTREMTPGEIKFSVHVESVLNRVPQPEYRQL
LVEAILVLTMLADIEIHSIGSIIAVEKIVHIANDLFLQEQKTLGADDIMLAKDPASGICT
LLYDSAPSGRFGTMTYLSKAAATYVQEFLPHSICAMQ
|
Gene Ontology |
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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