| BPT4/rI |
PMID:17693511 |
1 |
GO:0020002(C,IDA) |
It was first thought (PubMed:17693511) that the antiholin possesses a SAR domain, but it undergoes normal processing of its N- terminal signal sequence. . |
| BPT4/rI |
PMID:34456892 |
1 |
GO:0044229(C,EXP) |
It was first thought (PubMed:17693511) that the antiholin possesses a SAR domain, but it undergoes normal processing of its N- terminal signal sequence. . |
| BPT4/uvsW |
PMID:17092935 |
1 |
GO:0016887(M,EXP) |
Originally thought to also encode the following gene uvsW1 (PubMed:17092935). . |
| DANRE/pcif1 |
PMID:30467178 |
3 |
GO:0006397(B,IDA); GO:0016422(M,IDA); GO:1904047(M,IDA) |
The role of N(6),2'-O-dimethyladenosine cap (m6A(m)) on transcripts is unclear and subject to discussion. According to a report, m6A(m) promotes the translation of capped mRNAs (PubMed:30467178). Howe |
| ECOLI/ftsI |
PMID:7030331 |
1 |
GO:0008955(M,IDA) |
Was originally thought to be a bifunctional enzyme with transglycosylase and transpeptidase activities. . |
| ECOLI/rbsD |
PMID:15060078 |
2 |
GO:0062193(M,IDA); GO:0019303(B,IMP) |
Was originally thought (PubMed:3011793) to be a high affinity ribose transport protein, but further analysis (PubMed:15060078) shows that it is a D-ribose pyranase. . |
| human/AGK |
PMID:28712724 |
4 |
GO:0005743(C,IDA); GO:0005758(C,IDA); GO:0042721(C,IDA); GO:0045039(B,IDA) |
According to a report, the N-terminal hydrophobic region forms a transmembrane region that crosses the mitochondrion inner membrane (PubMed:28712726). According to another report, the N-terminal hydro |
| human/AGK |
PMID:28712726 |
4 |
GO:0005743(C,IDA); GO:0005758(C,IDA); GO:0042721(C,IDA); GO:0045039(B,IDA) |
According to a report, the N-terminal hydrophobic region forms a transmembrane region that crosses the mitochondrion inner membrane (PubMed:28712726). According to another report, the N-terminal hydro |
| human/AIFM2 |
PMID:11980907 |
5 |
GO:0043065(B,IDA); GO:0008637(B,IDA); GO:0005739(C,IDA); GO:0005741(C,IDA); GO:0005829(C,IDA) |
Conflicting data exist on the pro-apoptotic function of the protein. It was initially claimed that overexpression of FSP1 induces caspase-independent apoptosis, but new evidence disputes this function |
| human/AIFM2 |
PMID:12135761 |
1 |
GO:0005737(C,IDA) |
Conflicting data exist on the pro-apoptotic function of the protein. It was initially claimed that overexpression of FSP1 induces caspase-independent apoptosis, but new evidence disputes this function |
| human/AIFM2 |
PMID:15958387 |
3 |
GO:0003677(M,IDA); GO:0004174(M,IDA); GO:0050660(M,IDA) |
Conflicting data exist on the pro-apoptotic function of the protein. It was initially claimed that overexpression of FSP1 induces caspase-independent apoptosis, but new evidence disputes this function |
| human/AIFM2 |
PMID:31634899 |
6 |
GO:0016655(M,IDA); GO:0016655(M,IDA); GO:0110076(B,IDA); GO:0016655(M,IDA); GO:0006743(B,IDA); GO:0110076(B,IMP) |
Conflicting data exist on the pro-apoptotic function of the protein. It was initially claimed that overexpression of FSP1 induces caspase-independent apoptosis, but new evidence disputes this function |
| human/AIFM2 |
PMID:31634900 |
5 |
GO:0005811(C,IDA); GO:0005886(C,IDA); GO:0006743(B,IDA); GO:0016655(M,IDA); GO:0110076(B,IMP) |
Conflicting data exist on the pro-apoptotic function of the protein. It was initially claimed that overexpression of FSP1 induces caspase-independent apoptosis, but new evidence disputes this function |
| human/ARIH1 |
PMID:15236971 |
3 |
GO:0004842(M,IDA); GO:0008270(M,IDA); GO:0016567(B,IDA) |
The RING-type 2 zinc finger was initially reported to only bind 1 zinc ion instead of 2 compared to classical RING-types (PubMed:15236971). But it was later shown that it is not the case and binds 2 z |
| human/ARIH1 |
PMID:23707686 |
5 |
GO:0005515(M,IPI); GO:0004842(M,IDA); GO:0008270(M,IDA); GO:0016567(B,IDA); GO:0031624(M,IPI) |
The RING-type 2 zinc finger was initially reported to only bind 1 zinc ion instead of 2 compared to classical RING-types (PubMed:15236971). But it was later shown that it is not the case and binds 2 z |
| human/ASAH2 |
PMID:10781606 |
4 |
GO:0005739(C,IDA); GO:0006670(B,IMP); GO:0017040(M,IMP); GO:0046514(B,IMP) |
Was proposed to be mitochondrial, based on experiments with an N-terminal GFP-tag (PubMed:10781606). The in vivo localization to the mitochondrion could not be confirmed (PubMed:15845354). However, it |
| human/ATF2 |
PMID:10821277 |
4 |
GO:0045815(B,IDA); GO:0010485(M,IDA); GO:0044013(M,IDA); GO:1902562(C,IDA) |
Appears to have histone acetyltransferase (HAT) activity, specifically towards histones H2B and H4 in vitro (PubMed:10821277). However, it is not clear if this activity is genuine or caused by contami |
| human/ATP13A1 |
PMID:24392018 |
1 |
GO:0005789(C,EXP) |
Was initially thought to mediate manganese transport (PubMed:24392018). However, it was later shown to specifically bind moderately hydrophobic transmembrane with short hydrophilic lumenal domains tha |
| human/ATP13A1 |
PMID:32973005 |
2 |
GO:0140567(M,IDA); GO:0140569(B,IDA) |
Was initially thought to mediate manganese transport (PubMed:24392018). However, it was later shown to specifically bind moderately hydrophobic transmembrane with short hydrophilic lumenal domains tha |
| human/BOLA3 |
PMID:22746225 |
2 |
GO:0005739(C,NAS); GO:0005739(C,IDA) |
Was initially reported to be secreted via a non-classical export pathway (PubMed:18548201). It was however later shown that it localizes to mitochondria, in agreement with other members of the family |
| human/C1QBP |
PMID:9305894 |
1 |
GO:0005759(C,IDA) |
The subcellular location has been matter of debate. After being reported to be exclusively localized to mitochondria, demonstrations of promiscuous associations and locations were considered as artifa |
| human/CHMP1A |
PMID:8863740 |
2 |
GO:0008237(M,TAS); GO:0008270(M,TAS) |
Was originally (PubMed:8863740) thought to be a metalloprotease (PRSM1). This was based on a wrong translation of the ORF which gave rise to a putative protein of 318 AA containing a pattern reminisce |
| human/CPT1C |
PMID:30135643 |
2 |
GO:0005783(C,IDA); GO:0008474(M,IDA) |
In contrast to its paralogs, CPT1A and CPT1B, does not have, or at very low levels, carnitine O-palmitoyltransferase activity (EC:2.3.1.21) in vivo, being unable to catalyze the transfer of the acyl g |
| human/CSNK1D |
PMID:20637175 |
2 |
GO:0106310(M,EXP); GO:0004674(M,IDA) |
Was shown to phosphorylate and activate DCK in vitro but probably not in vivo. . |
| human/DNAJC13 |
PMID:24643499 |
6 |
GO:0005515(M,IPI); GO:0005515(M,IPI); GO:0005515(M,IPI); GO:0007032(B,IMP); GO:0010008(C,IDA); GO:0071203(C,IDA) |
In human, WASHC2 has undergone evolutionary duplication giving rise to highly homologous family members. A WASHC2C construct with WASHC2A-specific sequence insertions (of 2 aa and 21 aa length resulti |
| human/EDEM2 |
PMID:25092655 |
3 |
GO:1904380(B,IMP); GO:0036503(B,IMP); GO:0004571(M,IMP) |
Has similarity to alpha 1,2-mannosidases, but the catalytic activity of this protein is controversial (PubMed:15537790, PubMed:25092655). One study shows that it is important for a specific oligosacch |
| human/EIF2D |
PMID:20566627 |
2 |
GO:0003743(M,IDA); GO:0005737(C,IDA) |
Was previously erroneously called ligatin, a trafficking receptor for phosphoglycoproteins, while ligatin is actually a distinct 10 kDa filamentous membrane protein encoded by a still unidentified gen |
| human/ENDOU |
PMID:2350438 |
5 |
GO:0005737(C,TAS); GO:0006508(B,IDA); GO:0007565(B,IEP); GO:0008236(M,IDA); GO:0005615(C,TAS) |
Was originally (PubMed:2350438) thought to be a serine protease. However, PubMed:18936097 showed it is not the case. . |
| human/HDAC6 |
PMID:10220385 |
1 |
GO:0004407(M,IDA) |
Was originally thought to be a histone deacetylase (PubMed:10220385). However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates (PubMed |
| human/HDAC6 |
PMID:12024216 |
5 |
GO:0005515(M,IPI); GO:0042903(M,EXP); GO:0010634(B,IMP); GO:0031252(C,IDA); GO:0048471(C,IDA) |
Was originally thought to be a histone deacetylase (PubMed:10220385). However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates (PubMed |
| human/HDAC6 |
PMID:18606987 |
3 |
GO:0010727(B,IMP); GO:0036479(M,IMP); GO:0070301(B,IMP) |
Was originally thought to be a histone deacetylase (PubMed:10220385). However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates (PubMed |
| human/HDAC6 |
PMID:20308065 |
3 |
GO:0005515(M,IPI); GO:0042903(M,IDA); GO:0090042(B,IDA) |
Was originally thought to be a histone deacetylase (PubMed:10220385). However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates (PubMed |
| human/HDAC6 |
PMID:26246421 |
4 |
GO:0005737(C,IDA); GO:0005813(C,IDA); GO:0036064(C,IDA); GO:0061523(B,IDA) |
Was originally thought to be a histone deacetylase (PubMed:10220385). However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates (PubMed |
| human/HDAC6 |
PMID:31857589 |
2 |
GO:0033558(M,IDA); GO:1905336(B,IDA) |
Was originally thought to be a histone deacetylase (PubMed:10220385). However, subsequent work has shown that it is predominantly cytoplasmic and deacetylates a range of non-histone substrates (PubMed |
| human/IL4I1 |
PMID:28891065 |
2 |
GO:0001772(C,IDA); GO:0050868(B,IDA) |
According to a report, acts as a negative regulator of T-cell activation independently of its enzymatic activity (PubMed:28891065). However, authors of this study only tested enzyme activity via pheny |
| human/IL4I1 |
PMID:32818467 |
5 |
GO:0001716(M,IDA); GO:0002841(B,IDA); GO:0005576(C,IDA); GO:0019440(B,IDA); GO:0045944(B,IDA) |
According to a report, acts as a negative regulator of T-cell activation independently of its enzymatic activity (PubMed:28891065). However, authors of this study only tested enzyme activity via pheny |
| human/IL4I1 |
PMID:32866000 |
3 |
GO:0001716(M,IDA); GO:0001716(M,IDA); GO:0019440(B,IDA) |
According to a report, acts as a negative regulator of T-cell activation independently of its enzymatic activity (PubMed:28891065). However, authors of this study only tested enzyme activity via pheny |
| human/ISCU |
PMID:16517407 |
1 |
GO:0006879(B,IDA) |
[Isoform 1]: Previous publications report that ISCU could provide the architecture on which both [2Fe-2S] and [4Fe-4S] clusters could be assembled (PubMed:16517407, PubMed:16527810, PubMed:23940031). |
| human/ISCU |
PMID:16527810 |
4 |
GO:0005515(M,IPI); GO:0005634(C,TAS); GO:0005829(C,IDA); GO:0060090(M,IDA) |
[Isoform 1]: Previous publications report that ISCU could provide the architecture on which both [2Fe-2S] and [4Fe-4S] clusters could be assembled (PubMed:16517407, PubMed:16527810, PubMed:23940031). |
| human/ISCU |
PMID:23940031 |
5 |
GO:0044572(B,IDA); GO:0005515(M,IPI); GO:0005515(M,IPI); GO:0005515(M,IPI); GO:0044571(B,IDA) |
[Isoform 1]: Previous publications report that ISCU could provide the architecture on which both [2Fe-2S] and [4Fe-4S] clusters could be assembled (PubMed:16517407, PubMed:16527810, PubMed:23940031). |
| human/ISCU |
PMID:34824239 |
1 |
GO:0042803(M,IDA) |
[Isoform 1]: Previous publications report that ISCU could provide the architecture on which both [2Fe-2S] and [4Fe-4S] clusters could be assembled (PubMed:16517407, PubMed:16527810, PubMed:23940031). |
| human/NME2 |
PMID:11121025 |
1 |
GO:0003677(M,IDA) |
Originnally, in addition to its DNA binding activity, some reports shown that exhibited an intrinsic nuclease activity (PubMed:11121025, PubMed:11694515). Bound DNA within the nuclease hypersensitive |
| human/PARK7 |
PMID:22523093 |
6 |
GO:1902176(B,IDA); GO:0009438(B,IDA); GO:0019249(B,IDA); GO:1903189(B,IDA); GO:0036471(B,IDA); GO:0046295(B,IDA) |
Glyoxalase activity has been reported (PubMed:22523093, PubMed:31653696). It may however reflect its deglycase activity (PubMed:25416785). . |
| human/PARK7 |
PMID:25416785 |
3 |
GO:0036524(M,IDA); GO:0030091(B,IDA); GO:0036524(M,IDA) |
Glyoxalase activity has been reported (PubMed:22523093, PubMed:31653696). It may however reflect its deglycase activity (PubMed:25416785). . |
| human/PARK7 |
PMID:25416785 |
3 |
GO:0036524(M,IDA); GO:0030091(B,IDA); GO:0036524(M,IDA) |
The protein deglycation activity is controversial. It has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648) and as a result of the removal of methylglyoxal by glyoxalase activ |
| human/PARK7 |
PMID:28596309 |
2 |
GO:0036524(M,IDA); GO:0006281(B,IDA) |
The protein deglycation activity is controversial. It has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648) and as a result of the removal of methylglyoxal by glyoxalase activ |
| human/PEX11B |
PMID:9792670 |
3 |
GO:0005778(C,IDA); GO:0007031(B,IDA); GO:0016559(B,IDA) |
PubMed:9792670 states that both the N- and the C-terminus are located in the cytoplasm. . |
| human/RHBDF1 |
PMID:15965977 |
2 |
GO:0000139(C,EXP); GO:0005789(C,EXP) |
Lacks serine protease activity as it lacks the catalytic Ser residue at position 720. . |
| human/SLC40A1 |
PMID:29792530 |
1 |
GO:0016323(C,IDA) |
Manganese Mn(2+) transport by SLC40A1 remains controversial. Some in vitro studies have suggested that SLC40A1 transports minimal amounts of Mn(2+) (PubMed:22178646, PubMed:30247984). Other groups hav |
| human/SLC40A1 |
PMID:30247984 |
1 |
GO:0005886(C,IDA) |
Manganese Mn(2+) transport by SLC40A1 remains controversial. Some in vitro studies have suggested that SLC40A1 transports minimal amounts of Mn(2+) (PubMed:22178646, PubMed:30247984). Other groups hav |
| human/SLC7A11 |
PMID:15151999 |
4 |
GO:0005886(C,IDA); GO:0015327(M,IDA); GO:0015811(B,IDA); GO:0015813(B,IDA) |
In the PMID:15151999, a typographical error has been introduced leading to L-cysteine spelling instead of L-cystine. . |
| human/STAT1 |
PMID:27796300 |
1 |
GO:0005737(C,IDA) |
Has been shown to be mono-ADP-ribosylated at Glu-657 and Glu- 705 by PARP14 which prevents phosphorylation at Tyr-701 (PubMed:27796300). However, the role of ADP-ribosylation in the prevention of phos |
| human/TCF25 |
PMID:16574069 |
1 |
GO:0005634(C,EXP) |
Was reported to have DNA-binding activity (PubMed:16574069). However, this is uncertain as it was shown with the protein fused to the yeast GAL4 DNA-binding domain. . |
| human/TP53 |
PMID:17170702 |
2 |
GO:0005515(M,IPI); GO:0005515(M,IPI) |
Interaction with BANP was reported to enhance phosphorylation on Ser-15 upon ultraviolet irradiation (PubMed:15701641). However, the publication has been retracted due to image duplication and manipul |
| human/TP53 |
PMID:17317671 |
1 |
GO:0005515(M,IPI) |
Interaction with BANP was reported to enhance phosphorylation on Ser-15 upon ultraviolet irradiation (PubMed:15701641). However, the publication has been retracted due to image duplication and manipul |
| human/TP53 |
PMID:19011621 |
4 |
GO:0042802(M,IPI); GO:0005515(M,IPI); GO:0005634(C,IDA); GO:0005737(C,IDA) |
Interaction with BANP was reported to enhance phosphorylation on Ser-15 upon ultraviolet irradiation (PubMed:15701641). However, the publication has been retracted due to image duplication and manipul |
| human/TP53 |
PMID:20959462 |
4 |
GO:0005515(M,IPI); GO:0005515(M,IPI); GO:0043065(B,IDA); GO:0045944(B,IDA) |
Interaction with BANP was reported to enhance phosphorylation on Ser-15 upon ultraviolet irradiation (PubMed:15701641). However, the publication has been retracted due to image duplication and manipul |
| human/TP53 |
PMID:21597459 |
3 |
GO:0005515(M,IPI); GO:0005634(C,IDA); GO:0005737(C,IDA) |
Interaction with BANP was reported to enhance phosphorylation on Ser-15 upon ultraviolet irradiation (PubMed:15701641). However, the publication has been retracted due to image duplication and manipul |
| human/TP53 |
PMID:22726440 |
2 |
GO:0005515(M,IPI); GO:0005515(M,IPI) |
Interaction with BANP was reported to enhance phosphorylation on Ser-15 upon ultraviolet irradiation (PubMed:15701641). However, the publication has been retracted due to image duplication and manipul |
| human/UBA5 |
PMID:18442052 |
2 |
GO:0005634(C,EXP); GO:0005737(C,EXP) |
Was initially reported to mediate activation of SUMO2 in addition to UFM1 (PubMed:18442052). However, it was later shown that it is specific for UFM1 (By similarity). . |
| human/UCHL1 |
PMID:12408865 |
1 |
GO:0004843(M,EXP) |
The homodimer may have ATP-independent ubiquitin ligase activity (PubMed:12408865). However, in another study, UCHL1 was shown to lack ubiquitin ligase activity (PubMed:23359680). . |
| human/UCHL1 |
PMID:23359680 |
1 |
GO:0004843(M,EXP) |
The homodimer may have ATP-independent ubiquitin ligase activity (PubMed:12408865). However, in another study, UCHL1 was shown to lack ubiquitin ligase activity (PubMed:23359680). . |
| human/UCHL1 |
PMID:9774100 |
1 |
GO:0004843(M,EXP) |
PubMed:9774100 reports the association of mutation Ile93Met with Parkinson disease. However, according to PubMed:16450370 this association is uncertain and UCHL1 is not a susceptibility gene for Parki |
| human/UFSP1 |
PMID:35525273 |
4 |
GO:0071569(B,IDA); GO:0008234(M,IDA); GO:0051604(B,IDA); GO:0071567(M,IDA) |
UFSP1 initiates at a non-canonical GUG codon (PubMed:35525273, PubMed:35926457). Was initially thought to initiate from Met-77 and constitute a inactive isopeptidase that lacks a functional protease d |
| human/UFSP1 |
PMID:35926457 |
5 |
GO:0071569(B,IDA); GO:0005829(C,IDA); GO:0008234(M,IDA); GO:0051604(B,IDA); GO:0071567(M,IDA) |
UFSP1 initiates at a non-canonical GUG codon (PubMed:35525273, PubMed:35926457). Was initially thought to initiate from Met-77 and constitute a inactive isopeptidase that lacks a functional protease d |
| human/VCP |
PMID:22120668 |
5 |
GO:0005515(M,IPI); GO:0006302(B,IDA); GO:0006974(B,IDA); GO:0016567(B,IDA); GO:0035861(C,IDA) |
It is unclear how it participates in the recruitment of TP53BP1 at DNA damage sites. According to a first report, participates in the recruitment of TP53BP1 by promoting ubiquitination and removal of |
| mouse/Dnajb11 |
PMID:11584023 |
5 |
GO:0005634(C,IDA); GO:0005737(C,IDA); GO:0051082(M,IDA); GO:0005515(M,IPI); GO:0016556(B,IDA) |
PubMed:11584023 reported a cytosolic, as well as nuclear subcellular location. This result was obtained using an N-terminally GFP-tagged construct which most probably affected signal peptide-driven ta |
| worm/P54811 |
PMID:18854144 |
1 |
GO:0016887(M,IDA) |
The role of cdc-48.1 in the regulation of kinase air-2, a component of the chromosomal passenger complex (CPC), is controversial. One study suggests that cdc-48.1 inactivates air-2 at the end of mitos |
| worm/cdc-48 |
PMID:18854144 |
1 |
GO:0016887(M,IDA) |
The role of cdc-48.1 in the regulation of kinase air-2, a component of the chromosomal passenger complex (CPC), is controversial. One study suggests that cdc-48.1 inactivates air-2 at the end of mitos |