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TTLL12 TTLL12 UFM1 UFM1 UNK UNK UBE2V2 UBE2V2 UFC1 UFC1 UBE2D1 UBE2D1 UBE2V1 UBE2V1 UBXN1 UBXN1 UBXN7 UBXN7 USP9X USP9X SULT1A1 SULT1A1 ZFYVE19 ZFYVE19 USP34 USP34 UBE2C UBE2C UBE2L3 UBE2L3 ATP6V1B2 ATP6V1B2 UBC UBC VPS4B VPS4B SSSCA1 SSSCA1 ZRANB2 ZRANB2 UBE4B UBE4B UCHL3 UCHL3 UBQLN4 UBQLN4 UBQLN1 UBQLN1 UBQLN2 UBQLN2 UBL7 UBL7
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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small nodes:
protein of unknown 3D structure
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large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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Edges represent protein-protein associations
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from curated databases
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experimentally determined
Predicted Interactions
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fusion edge
gene fusions
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gene co-occurrence
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textmining
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co-expression
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Your Input:
TTLL12tubulin tyrosine ligase-like family, member 12 (644 aa)
VPS4Bvacuolar protein sorting 4 homolog B (S. cerevisiae); Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growt [...] (444 aa)
UFM1ubiquitin-fold modifier 1; Ubiquitin-like modifier protein which binds to a number of target proteins, such as DDRGK1 (85 aa)
ATP6V1B2ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2; Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (511 aa)
UNKunkempt homolog (Drosophila) (886 aa)
UBXN1UBX domain protein 1; Ubiquitin-binding protein that interacts with the BRCA1- BARD1 heterodimer, and regulates its activity. Specifically binds ’Lys-6’-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol (312 aa)
UBXN7UBX domain protein 7 (489 aa)
SSSCA1Sjogren syndrome/scleroderma autoantigen 1; Might play a role in mitosis. Antigenic molecule. Could be a centromere-associated protein. May induce anti-centromere antibodies (199 aa)
USP9Xubiquitin specific peptidase 9, X-linked; Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important role regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Essential component of TGF-beta/BMP signaling cascade. Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres. Specifically hydrolyzes both ’Lys-29’- and ’Lys-33’-linked polyubiquitins chains. Specificall [...] (2570 aa)
SULT1A1sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1; Sulfotransferase that utilizes 3’-phospho-5’-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N- hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk (295 aa)
UBE2V1ubiquitin-conjugating enzyme E2 variant 1 (170 aa)
UBE4Bubiquitination factor E4B; Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity) (1302 aa)
UBE2L3ubiquitin-conjugating enzyme E2L 3; Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine- in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys-11’-linked polyubiquitination. Involved in th [...] (154 aa)
UBCubiquitin C (685 aa)
UBQLN2ubiquilin 2; Increases the half-life of proteins destined to be degraded by the proteasome; may modulate proteasome-mediated protein degradation (624 aa)
ZFYVE19zinc finger, FYVE domain containing 19 (471 aa)
UBE2Cubiquitin-conjugating enzyme E2C; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating ’Lys-11’-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit (179 aa)
UBL7ubiquitin-like 7 (bone marrow stromal cell-derived) (380 aa)
UFC1ubiquitin-fold modifier conjugating enzyme 1; E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage (167 aa)
UBQLN4ubiquilin 4; Plays a role in the regulation of proteasomal protein degradation. Depending on the case, may promote or inhibit proteasomal protein degradation (601 aa)
ZRANB2zinc finger, RAN-binding domain containing 2; Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5’- splice site selection (330 aa)
UBE2D1ubiquitin-conjugating enzyme E2D 1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP- induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyu [...] (147 aa)
UBQLN1ubiquilin 1; Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors (By similarity). Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation (589 aa)
UCHL3ubiquitin carboxyl-terminal esterase L3 (ubiquitin thiolesterase); Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards ’Lys-48’-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGF [...] (230 aa)
USP34ubiquitin specific peptidase 34 (3546 aa)
UBE2V2ubiquitin-conjugating enzyme E2 variant 2; Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through ’Lys-63’. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage (145 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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