| Tag | Content |
|---|
| CPLM ID | CPLM-016120 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase LRSAM1 |
Protein Synonyms/Alias | Leucine-rich repeat and sterile alpha motif-containing protein 1; Tsg101-associated ligase |
Gene Name | Lrsam1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 135 | QLQTLNVKDNKLKEL | ubiquitination | [1] | | 491 | QLTQLELKRKSLDTE | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) cargos (By similarity). |
Sequence Annotation | REPEAT 30 51 LRR 1.
REPEAT 56 77 LRR 2.
REPEAT 82 103 LRR 3.
REPEAT 105 126 LRR 4.
REPEAT 128 150 LRR 5.
REPEAT 151 172 LRR 6.
DOMAIN 569 632 SAM.
ZN_FING 679 714 RING-type.
MOTIF 653 656 PTAP motif 1.
MOTIF 665 668 PTAP motif 2.
MOD_RES 234 234 Phosphoserine (By similarity).
MOD_RES 604 604 Phosphoserine (By similarity). |
Keyword | Coiled coil; Complete proteome; Cytoplasm; Leucine-rich repeat; Ligase; Metal-binding; Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 727 AA |
Protein Sequence | MPLFFRKRKP SEEARKRLEY QMCLAKEAGA DDILDISKCE LSEIPFGAFA TCKVLQKKVL 60
IVHTNHLTSL LPKSCSLLSL VTIKVLDLHE NQLTALPDDM GQLTVLQVLN VERNQLTHLP 120
RSIGNLLQLQ TLNVKDNKLK ELPDTLGELR SLRTLDISEN EIQRLPQMLA HVRTLETLSL 180
NALAMVYPPP EVCGAGTAAV QQFLCKESGL DYYPPSQYLL PVLEQDGAEN TQDSPDGPAS 240
RFSREEAEWQ NRFSDYEKRK EQKMLEKLEF ERRLDLGQRE HAELLQQSHS HKDEILQTVK 300
QEQTRLEQDL SERQRCLDAE RQQLQEQLKQ TEQSIASRIQ RLLQDNQRQK KSSEILKSLE 360
NERIRMEQLM SITQEETENL RQREIAAAMQ QMLTESCKSR LIQMAYESQR QSLAQQACSS 420
MAEMDKRFQQ ILSWQQMDQN KAISQILQES VMQKAAFEAL QVKKDLMHRQ IRNQIRLIET 480
ELLQLTQLEL KRKSLDTETL QEMVSEQRWA LSNLLQQLLK EKKQREEELH GILAELEAKS 540
ETKQENYWLI QYQRLLNQKP LSLKLQEEGM ERRLVALLVE LSAEHYLPLF AHHRISLDML 600
SRMSPGDLAK VGVSEAGLQH EILRRAQDLL AVPRVQPELK PLENEVLGAL EPPTAPRELQ 660
ESVRPSAPPA ELDMPTSECV VCLEREAQMV FLTCGHVCCC QQCCQPLRTC PLCRQEISQR 720
LRIYHSS 727 |
Gene Ontology | GO:0005737; C:cytoplasm; ISS:UniProtKB. GO:0044425; C:membrane part; ISS:UniProtKB. GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0045806; P:negative regulation of endocytosis; ISS:UniProtKB. GO:0046755; P:non-lytic virus budding; ISS:UniProtKB. GO:0051865; P:protein autoubiquitination; ISS:UniProtKB. GO:0030163; P:protein catabolic process; ISS:UniProtKB. GO:0000209; P:protein polyubiquitination; ISS:UniProtKB. GO:0015031; P:protein transport; IEA:UniProtKB-KW. GO:0070086; P:ubiquitin-dependent endocytosis; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |