CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022774
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tripartite motif-containing protein 3 
Protein Synonyms/Alias
 RING finger protein 22; RING finger protein HAC1 
Gene Name
 Trim3 
Gene Synonyms/Alias
 Hac1; Rnf22 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
565SIFSPEGKFKTKIGAubiquitination[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
 Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). 
Sequence Annotation
 REPEAT 317 418 Filamin.
 REPEAT 473 516 NHL 1.
 REPEAT 520 563 NHL 2.
 REPEAT 564 605 NHL 3.
 REPEAT 609 652 NHL 4.
 REPEAT 656 699 NHL 5.
 REPEAT 700 743 NHL 6.
 ZN_FING 22 63 RING-type.
 ZN_FING 110 151 B box-type.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 7 7 Phosphoserine.  
Keyword
 Acetylation; Coiled coil; Complete proteome; Cytoplasm; Endosome; Metal-binding; Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 744 AA 
Protein Sequence
MAKREDSPGP EVQPMDKQFL VCSICLDRYR CPKVLPCLHT FCERCLQNYI PPQSLTLSCP 60
VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPEGAHDPE DPHPLSAVAG RPLSCPNHEG 120
KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI 180
ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLESICGAK QKVLQTQLDT 240
LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL 300
EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA 360
ELCAEITGPD GVRLAVPVVD HKNGTYELVY TARTEGDLLL SVLLYGQPVR GSPFRVRALR 420
PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIED ELVFRVGSRG 480
REKGEFTNLQ GVSAASSGRI VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA 540
VDTNGDIIVA DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF 600
TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG 660
SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA 720
LTSDGHVVVA DAGNHCFKAY RYLQ 744 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR003649; Bbox_C.
 IPR001298; Filamin.
 IPR017868; Filamin/ABP280_repeat-like.
 IPR013783; Ig-like_fold.
 IPR014756; Ig_E-set.
 IPR001258; NHL_repeat.
 IPR013017; NHL_repeat_subgr.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00630; Filamin
 PF01436; NHL
 PF00643; zf-B_box 
SMART
 SM00502; BBC
 SM00336; BBOX
 SM00557; IG_FLMN
 SM00184; RING 
PROSITE
 PS50194; FILAMIN_REPEAT
 PS51125; NHL
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS