| Tag | Content |
|---|
| CPLM ID | CPLM-000432 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Midline-1 |
Protein Synonyms/Alias | Midin; Midline 1 RING finger protein; Putative transcription factor XPRF; RING finger protein 59; Tripartite motif-containing protein 18 |
Gene Name | MID1 |
Gene Synonyms/Alias | FXY; RNF59; TRIM18; XPRF |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 232 | SNLTNLIKRNTELET | ubiquitination | [1, 2] |
|
Reference | [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [ PMID: 21890473] [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Chen Z, Zhou Y, Song J, Zhang Z. Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [ PMID: 23603789] |
Functional Description | Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. |
Sequence Annotation | DOMAIN 320 379 COS.
DOMAIN 380 481 Fibronectin type-III.
DOMAIN 482 659 B30.2/SPRY.
ZN_FING 10 60 RING-type.
ZN_FING 116 165 B box-type 1.
ZN_FING 172 212 B box-type 2.
METAL 119 119 Zinc 1.
METAL 122 122 Zinc 1.
METAL 134 134 Zinc 2.
METAL 137 137 Zinc 2.
METAL 142 142 Zinc 1.
METAL 145 145 Zinc 1.
METAL 150 150 Zinc 2.
METAL 159 159 Zinc 2.
MOD_RES 92 92 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Ligase; Metal-binding; Microtubule; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 667 AA |
Protein Sequence | METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES ITAFQCPTCR 60
HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MTSAEKVLCQ 120
FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED 180
EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL 240
LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA 300
NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD 360
TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI 420
FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FMVKAINQAG SRSSEPGKLK 480
TNSQPFKLDP KSAHRKLKVS HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR 540
HYWEVVISGS TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH 600
LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VAFAQPVCPT FTVWNKCLTI ITGLPIPDHL 660
DCTEQLP 667 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005874; C:microtubule; IEA:UniProtKB-KW. GO:0005875; C:microtubule associated complex; TAS:ProtInc. GO:0005819; C:spindle; IEA:UniProtKB-SubCell. GO:0016874; F:ligase activity; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0000226; P:microtubule cytoskeleton organization; TAS:ProtInc. GO:0007389; P:pattern specification process; TAS:ProtInc. GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |