CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011052
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein ECM5 
Protein Synonyms/Alias
 Extracellular matrix protein 5 
Gene Name
 ECM5 
Gene Synonyms/Alias
 YMR176W; YM8010.06 
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
215TRIPSIDKRTLDLYRubiquitination[1]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
 May be involved in cell wall organization and biogenesis. 
Sequence Annotation
 DOMAIN 118 159 JmjN.
 DOMAIN 185 279 ARID.
 DOMAIN 476 695 JmjC.
 ZN_FING 1238 1290 PHD-type.  
Keyword
 Cell wall biogenesis/degradation; Complete proteome; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1411 AA 
Protein Sequence
MSGHDSVTKI SHILNEPVNE KVMVQNGFHE SSKIADIELE IQERPSIKQW ESPRSAVIPT 60
SNHNFSPFLY TQFKSRGAAP FAPETIKSVD LVELPEGVPA RVFHEKTGLF YQISPHSIPT 120
FILAKKELPD PIKFYELVED LGSVYGCVKL KIIPDADKFT QLNVDVDRLW FKARKQFFNS 180
NEFQRTKIVD FYAKLYNFHN KIKKSTLTRI PSIDKRTLDL YRLRSCVKLR GGFNAVCEKK 240
LWAQIGRELG YSGRIMSSLS TSLRSAYAKI LLDFDIYEEE EQAARNNEKN EDMVESEIFR 300
HSNSRSRDEE EPLHKKAKIH RDVFRAGSIN HEFKRMRDIK HIKGFPTYFN SLTEFKLGYT 360
QSTETTLPGY DFTFWENGME IYDKSKYETK TSPVYNLRQY YEKSLAVFTA IVAKFGSSYP 420
DLFAKHTTLP QKEFERLYFH LLSEHFIDFE IDTGLGLPCS MRSPGNNSSN EKFAIKNILD 480
QWNLDNIPLN ELSLLQHLDL DMANFTRTTY DIGMLFSCQG WSVSDHFLPS IDFNHLGSTK 540
LVYSIAPKDM EKFEALIARG KSEWDTIQSR PRYSTSDDEL KSFIETDFYK SFLDAEQSAD 600
YSNTGDNSKN SFPEDKIAGN TLHDGSQSDF IFEPNFILAN GIKLYKTTQE QGSYIFKFPK 660
AFTCSIGSGF YLSQNAKFAP SSWLRFSSEA AKWTSKMGFL PGLDVNQLLI NALLNSNNPV 720
LRKKCRDLIS NYVVEEAENS KKLGELIGTV DVVYNKLNYI SDISLESTGL SKIVVTHGAL 780
QRNLSLKEFV VLLEKPENGA HSICGIPIRD QSGNLNVCLH SYFDSASLGI ALDGLDKPPT 840
SYLLVHNEDF EKKWDVLMTS TFRNRTVPLN IIQYLISHTD SNTEFNRMLR SNFDDSLLLI 900
EKCKKFIKTF VDVSCSVKDV DFGNGFNLRH LPLKFSDNMA DNLESLYESV RKCSIEFSEK 960
PTIIRLYHVS RQFPIDNRDI IDGNNLDLLK ELYQKSLTIP LKVSYWTKLT RKICRLEWLS 1020
VYEHIFIERC DIKNEDPAKY SLPLLYSYFE FGLKYCDSED IDKLGEVRKL ILKYQDMMQK 1080
VRVFLKKDPP SKISLSDLED VLLDIEEYRL PIQSSFFSEL DYVIREIENA KKMNDVNILY 1140
NTDNIDKIDE LIRKNDPKFV KFANQFNGSR LDKRPLASDN SGSVKAKQEL KVFKLWNQHL 1200
DQIMQKNKFI EILPSIFRCL DLKSDKYIPL ESCSKRQTKY CFCRRVEEGT AMVECEICKE 1260
WYHVDCISNG ELVPPDDPNV LFVCSICTPP CMAVDNIEGV TFELDDLKRI LVESLKLSLI 1320
PDPPILKNLF DVFAFALNFK NEMEKELFTN GYVNQLSSTH KIKYYLRKLK GSQCGFTNLT 1380
DPLRKHCQVK DAEAIKWLTD NGRIIITGIP N 1411 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0070211; C:Snt2C complex; IDA:SGD.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001606; ARID/BRIGHT_DNA-bd.
 IPR003347; JmjC_dom.
 IPR003349; TF_JmjN.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01388; ARID
 PF00628; PHD 
SMART
 SM00501; BRIGHT
 SM00558; JmjC
 SM00249; PHD 
PROSITE
 PS51011; ARID
 PS51184; JMJC
 PS51183; JMJN
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS