| Tag | Content |
|---|
| CPLM ID | CPLM-007516 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein BNI1 |
Protein Synonyms/Alias | Pointed projection formation protein 3; Sensitive to high expression protein 5; Synthetic lethal 39 |
Gene Name | BNI1 |
Gene Synonyms/Alias | PPF3; SHE5; YNL271C; N0646 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 123 | RSHSMQSKYSYSKRN | acetylation | [1] | | 228 | QDLQNELKKMRANTT | acetylation | [2] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] [2] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures. Xie H, Bandhakavi S, Roe MR, Griffin TJ. J Proteome Res. 2007 May;6(5):2019-26. [ PMID: 17397211] |
Functional Description | Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and acts as leaky capper, slowing both polymerization and depolymerization. Protects the growing actin fiber from tight capping proteins and so increases the time of elongation and the total amount of F-actin. May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members. |
Sequence Annotation | DOMAIN 174 696 GBD/FH3.
DOMAIN 1053 1337 FH1.
DOMAIN 1348 1766 FH2.
DOMAIN 1792 1826 DAD.
MOD_RES 311 311 Phosphoserine.
MOD_RES 325 325 Phosphoserine.
MOD_RES 1085 1085 Phosphoserine.
MOD_RES 1170 1170 Phosphoserine.
MOD_RES 1338 1338 Phosphoserine.
MOD_RES 1344 1344 Phosphoserine.
MOD_RES 1918 1918 Phosphothreonine. |
Keyword | 3D-structure; Actin-binding; Cell membrane; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1953 AA |
Protein Sequence | MLKNSGSKHS NSKESHSNSS SGIFQNLKRL ANSNATNSNT GSPTYASQQQ HSPVGNEVST 60
SPASSSSFRK LNAPSRSTST EARPLNKKST LNTQNLSQYM NGKLSGDVPV SSQHARSHSM 120
QSKYSYSKRN SSQASNKLTR QHTGQSHSAS SLLSQGSLTN LSKFTTPDGK IYLEMPSDPY 180
EVEVLFEDIM YKRNIFQSLS EDKQEALMGY SIEKKWLIVK QDLQNELKKM RANTTSSSTA 240
SRTSMASDHH PILTANSSLS SPKSVLMTSA SSPTSTVYSN SLNHSTTLSS VGTSTSKGKK 300
LVSGSLKKQP SLNNIYRGGA ENNTSASTLP GDRTNRPPIH YVQRILADKL TSDEMKDLWV 360
TLRTEQLDWV DAFIDHQGHI AMANVLMNSI YKTAPRENLT KELLEKENSF FKCFRVLSML 420
SQGLYEFSTH RLMTDTVAEG LFSTKLATRK MATEIFVCML EKKNKSRFEA VLTSLDKKFR 480
IGQNLHMIQN FKKMPQYFSH LTLESHLKII QAWLFAVEQT LDGRGKMGSL VGASDEFKNG 540
GGENAILEYC QWTMVFINHL CSCSDNINQR MLLRTKLENC GILRIMNKIK LLDYDKVIDQ 600
IELYDNNKLD DFNVKLEANN KAFNVDLHDP LSLLKNLWDI CKGTENEKLL VSLVQHLFLS 660
SSKLIEENQN SSKLTKQLKL MDSLVTNVSV ASTSDEETNM NMAIQRLYDA MQTDEVARRA 720
ILESRALTKK LEEIQAERDS LSEKLSKAEH GLVGQLEDEL HERDRILAKN QRVMQQLEAE 780
LEELKKKHLL EKHQQEVELR KMLTILNSRP EESFNKNEGT RGMNSSLNSS EKANIQKVLQ 840
DGLSRAKKDY KDDSKKFGMT LQPNKRLKML RMQMENIENE ARQLEMTNFA EFEKDRLEPP 900
IHIKKPKVKK MKNKDRKPLV KPQEADVNKL NDLRRALAEI QMESNDISKF NVEERVNELF 960
NEKKSLALKR LKELETKYKG FGIDFNVDEI MDSPKKNTGD VETEEDANYA SLDPKTYQKK 1020
LDEINRITDQ LLDIQTQTEH EIQVEEDGES DLSSSSSDDE SEEIYQDASP TQELRSEHSE 1080
LSSGSGPGSF LDALSQKYGT GQNVTASAAF GENNNGSGIG PLHSKVEKTF MNRLRKSTVS 1140
SAPYLEELTQ KVNKVEPYEQ NEDEGLDKKS LPENSTASAA SAFDKAEKDM RQHVENGKQG 1200
RVVNHEEDKT ADFSAVSKLN NTDGAEDLST QSSVLSSQPP PPPPPPPPVP AKLFGESLEK 1260
EKKSEDDTVK QETTGDSPAP PPPPPPPPPP PMALFGKPKG ETPPPPPLPS VLSSSTDGVI 1320
PPAPPMMPAS QIKSAVTSPL LPQSPSLFEK YPRPHKKLKQ LHWEKLDCTD NSIWGTGKAE 1380
KFADDLYEKG VLADLEKAFA AREIKSLASK RKEDLQKITF LSRDISQQFG INLHMYSSLS 1440
VADLVKKILN CDRDFLQTPS VVEFLSKSEI IEVSVNLARN YAPYSTDWEG VRNLEDAKPP 1500
EKDPNDLQRA DQIYLQLMVN LESYWGSRMR ALTVVTSYER EYNELLAKLR KVDKAVSALQ 1560
ESDNLRNVFN VILAVGNFMN DTSKQAQGFK LSTLQRLTFI KDTTNSMTFL NYVEKIVRLN 1620
YPSFNDFLSE LEPVLDVVKV SIEQLVNDCK DFSQSIVNVE RSVEIGNLSD SSKFHPLDKV 1680
LIKTLPVLPE ARKKGDLLED EVKLTIMEFE SLMHTYGEDS GDKFAKISFF KKFADFINEY 1740
KKAQAQNLAA EEEERLYIKH KKIVEEQQKR AQEKEKQKEN SNSPSSEGNE EDEAEDRRAV 1800
MDKLLEQLKN AGPAKSDPSS ARKRALVRKK YLSEKDNAPQ LLNDLDTEEG SILYSPEAMD 1860
PTADTVIHAE SPTPLATRGV MNTSEDLPSP SKTSALEDQE EISDRARMLL KELRGSDTPV 1920
KQNSILDEHL EKLRARKERS IGEASTGNRL SFK 1953 |
Gene Ontology | GO:0005884; C:actin filament; IDA:SGD. GO:0005935; C:cellular bud neck; IDA:SGD. GO:0005934; C:cellular bud tip; IDA:SGD. GO:0000131; C:incipient cellular bud site; IDA:SGD. GO:0043332; C:mating projection tip; IDA:SGD. GO:0005886; C:plasma membrane; IDA:SGD. GO:0000133; C:polarisome; IPI:SGD. GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. GO:0005522; F:profilin binding; IDA:SGD. GO:0071519; P:actin filament bundle assembly involved in cytokinetic actomyosin contractile ring assembly; IMP:SGD. GO:0045010; P:actin nucleation; IDA:SGD. GO:0051016; P:barbed-end actin filament capping; IDA:SGD. GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD. GO:0070649; P:formin-nucleated actin cable assembly; IDA:SGD. |
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