wanglab/gogpt-training-data huggingface dataset:
Protein: TELO2-interacting protein 1 homolog (Protein SMG10) (O43156)
Organism: Homo sapiens (Human)
Function: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23263282}.
Interaction partners:
- Proline-rich protein 5
- Target of rapamycin complex subunit LST8
- Rapamycin-insensitive companion of mTOR
- Serine/threonine-protein kinase mTOR
- Telomere length regulation protein TEL2 homolog
- TELO2-interacting protein 2
- Regulatory-associated protein of mTOR
- Target of rapamycin complex 2 subunit MAPKAP1
- DEP domain-containing mTOR-interacting protein
- Proline-rich AKT1 substrate 1
Sequence:
MAVFDTPEEAFGVLRPVCVQLTKTQTVENVEHLQTRLQAVSDSALQELQQYILFPLRFTLKTPGPKRERLIQSVVECLTFVLSSTCVKEQELLQELFSELSACLYSPSSQKPAAVSEELKLAVIQGLSTLMHSAYGDIILTFYEPSILPRLGFAVSLLLGLAEQEKSKQIKIAALKCLQVLLLQCDCQDHPRSLDELEQKQLGDLFASFLPGISTALTRLITGDFKQGHSIVVSSLKIFYKTVSFIMADEQLKRISKVQAKPAVEHRVAELMVYREADWVKKTGDKLTILIKKIIECVSVHPHWKVRLELVELVEDLLLKCSQSLVECAGPLLKALVGLVNDESPEIQAQCNKVLRHFADQKVVVGNKALADILSESLHSLATSLPRLMNSQDDQGKFSTLSLLLGYLKLLGPKINFVLNSVAHLQRLSKALIQVLELDVADIKIVEERRWNSDDLNASPKTSATQPWNRIQRRYFRFFTDERIFMLLRQVCQLLGYYGNLYLLVDHFMELYHQSVVYRKQAAMILNELVTGAAGLEVEDLHEKHIKTNPEELREIVTSILEEYTSQENWYLVTCLETEEMGEELMMEHPGLQAITSGEHTCQVTSFLAFSKPSPTICSMNSNIWQICIQLEGIGQFAYALGKDFCLLLMSALYPVLEKAGDQTLLISQVATSTMMDVCRACGYDSLQHLINQNSDYLVNGISLNLRHLALHPHTPKVLEVMLRNSDANLLPLVADVVQDVLATLDQFYDKRAASFVSVLHALMAALAQWFPDTGNLGHLQEQSLGEEGSHLNQRPAALEKSTTTAEDIEQFLLNYLKEKDVADGNVSDFDNEEEEQSVPPKVDENDTRPDVEPPLPLQIQIAMDVMERCIHLLSDKNLQIRLKVLDVLDLCVVVLQSHKNQLLPLAHQAWPSLVHRLTRDAPLAVLRAFKVLRTLGSKCGDFLRSRFCKDVLPKLAGSLVTQAPISARAGPVYSHTLAFKLQLAVLQGLGPLCERLDLGEGDLNKVADACLIYLSVKQPVKLQEAARSVFLHLMKVDPDSTWFLLNELYCPVQFTPPHPSLHPVQLHGASGQQNPYTTNVLQLLKELQ
Protein: 1,3-beta-glucanosyltransferase gas2 (EC 2.4.1.-) (Q9USU5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16823372}. Secreted {ECO:0000305|PubMed:16823372}.
Interaction partners:
Sequence:
MVSFTKFTLQLLSASAAFAYFEPLTIKGRKFFKNDTQFYIKGVAYQPAVDAEETSTIVDPLAEVNYKNCTEDAKIISNLGANVIRVYAVNASLNHDKCMEAFRNESIYVFLDLANPKTGIDRDTPTWNTDQFSSYQSVIDTFQKYNNTGAFFAGNEVVNNASNAPAVAYVRAAVRDSKNYIKSKKYRTIPVGYAGADIPVVRTELAAYLSCNATKLNNDTNSETDFLGYNMYEWCGHSDFYTSGYAARTQELENFTIPIFLSEFGCNKVTPRVFTEVQAIYSDNMTNVWSGGIVYEYSQEVNDYGLVNVSSTGERVLTTDYNNLKKQWASISPNITYKHSYNPNGTIPECPSRNKTSWAVSANAFPVTPNTTICSNAVKNLKCSANGTPSGSKISQVLSELCYYDNKACSSISSDPYEGTYGNYTGCTGVQQLSIALNAYTQDHGADSCSWGGVGELKA
Protein: Uncharacterized protein (Q54FB1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MGNLLSHTYGVPSIISIIIIVSSSIFLIILKKDKQKYINNQINNQINNQIVPEISNNNSYNNSDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDDSSVNLGNNLKTTDYDIVIDLQSVDTFVIKDACWTVYVNKDLLKNVKEDSPNPLDCLLEGSNKFRTATIIGYFKRGKTFTANLINNINLPSGSKTKTKGLSIYISHTNDTLFIDTQGSNTPLPFFVDENENEELKKAYNINQADGSIKLNNLHLARKKATESFIQETAISLSNVVIFVVNEMTWHDQQNIMAIQKKIKTQNPIEKQKIRELYVFHNYMNISNMVDLMAMIKTYVTTPFKGYFHTEFSLHSDNEYIIYYTDAENFTTHFFLCNHGSEFGKKWNELVGKFVKTKIKNVTNQNYAFDTILLETLKEKMKTNIKNPTDLKIVPYYNSQTQVVEIENKSSSTRSNTFVYKRQTGIPLKDQKTLEDLEEMFNQVKAHTIDINQVPMYSIVPAIKNNEYEQWKYALNNKDIIFIDNLLIVTGSFNPTYDSLECENRTLIFTFDLPDIPESHFSHSIYYDPSDKVRYLKVSGNRKLSYRALTGTRGGESTINEYPSAGVKIGNSLNLRKDGEFDLRIPIEANYSKNYSNHFENGVLTLTFKEEIEGLPDESCK
Protein: X-ray repair cross-complementing protein 6 (X-ray repair-complementing defective repair in Chinese hamster cells 6) (F1QZ60)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- WRN RecQ-like helicase.
- X-ray repair cross-complementing protein 5
- DNA ligase
- DNA-dependent protein kinase catalytic subunit
- Non-homologous end-joining factor 1
- Double-strand break repair protein
- DNA repair protein RAD52 homolog
- non-specific serine/threonine protein kinase
- DNA ligase
- Protein artemis
Sequence:
MANWGNYFPNEDDVDEQDEEESGGDYKSSGRDSLVFLVDASKEMFIKGENGEPSNFDMTMQCVRSVYTSKIISSDRDLVALVFYGTEQSKNPRNSFKHVYVYHDLESPGAKRVQDIDKLKGDKGGQFAEKTMGSGETSLGEALWCCSNLYSDIKLRLSHKRLMIFTCRDEPHGGDSAKDRQARTKAADLKETGVAIDLMHLSKPGGFDVSLFFCDIVSPPEDESDLGLQIEPCRKLEDLQKRVRAKELKKRAQCRLTFSLGEGVDLAVGVYVLARTAMKPSAVKLYRDNNEPVRTKSRLFHTQTGGILLPNDTKRAQVYGQKQIVMEKDEVDEIKKFDDPGLVLIGFKPIDRLKLHHHLRPALFIYPEEEQISGSSCMFTALLLKCCEKNVFALCKYIPRRNTPPRFVALVPQREELDQSQTQATPPGFHVIYLPFADDIRTVDPHVGPTASDEQVDKMKEIVHKLRFKYRSDAFENPVLQQHYSNLEALALDMLSPEPIEDLTMPKVKMMDDRLGPLVQEFKDLVYPPDYNPEGKPAAKRKPAESGGGAAEKKAKVEISEEELKIHVAKGTLGKLTVPVLKDACKQFNIRTTGTKKQELIDALTMQLSK
Protein: Probable cytochrome P450 6t3 (EC 1.14.-.-) (CYPVIT3) (Q9V676)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Spookier
- Cholesterol 7-desaturase nvd
- Ecdysone 20-monooxygenase
- Short-chain dehydrogenase/reductase)
- Cytochrome P450 315a1, mitochondrial
Sequence:
MLLIWLLLLTIVTLNFWLRHKYDYFRSRGIPHLPPSSWSPMGNLGQLLFLRISFGDLFRQLYADPRNGQAKIVGFFIFQTPALMVRDPELIRQVLIKNFNNFLNRFESADAGDPMGALTLPLAKYHHWKESRQCMSQLFTSGRMRDVMYSQMLDVASDLEQYLNRKLGDRLERVLPLGRMCQLYTTDVTGNLFYSLNVGGLRRGRSELITKTKELFNTNPRKVLDFMSVFFLPKWTGVLKPKVFTEDYARYMRHLVDDHHEPTKGDLINQLQHFQLSRSSNHYSQHPDFVASQAGIILLAGFETSSALMGFTLYELAKAPDIQERLRSELREAFISTATLSYDTLMTLPYLKMVCLEALRLYPAAAFVNRECTSSASEGFSLQPHVDFIVPPGMPAYISILGLHRDERFWPEPCVFDPERFGPERSRHIHPMTYIPFGAGPHGCIGSRLGVLQLKLGIVHILKQYWVETCERTVSEIRFNPKSFMLESENEIYLRFCRSSL
Protein: Protein Wnt (Wnt homolog) (G5EG05)
Organism: Caenorhabditis elegans
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Frizzled-4
- Frizzled-2
- Frizzled-4
- Protein mom-5
- Secreted frizzled-related protein 1
- Protein-serine O-palmitoleoyltransferase porcupine
- Protein wntless homolog
- Tyrosine-protein kinase receptor cam-1
- Inactive tyrosine-protein kinase RYK
- Protein Wnt-1
Sequence:
MQFFICLIFLFVLLVYGQYSPPSATYSTQQVPYNWLTLAFVGSNDYLPRPHYHSTDREHFKELCRRLDGLNPNQQALCAENPFSIPFVARGVREAIRECENKFKFERWNCSSRDEVTETRHGKFQDILGKTLRSANKEAAFLNAIMAASIVHSITKGCNTGNLTECGCDSKPGMQRYQAESDPSMSRDQFSWGGCSDNVPHGIRYAKKFLDDWETAQFDKTKNVAHLVRRHNNFVGREAIAQNIRRQCRCHGVSGSCEFKTCWLQMQKFSQVSDLLKKRYDHFAVQVTRKATKRLRRKERTERKIPLRGNEMAYVHRSPSYCEKNLTAGILGTSGRECIHNSYSSESCDLLCCGRGYNTRLEIRQTQCECKFVWCCEVKCKTCTEEVAVHTCK
Protein: Dipeptide transport ATP-binding protein DppF (EC 7.4.2.9) (P37313)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter DppABCDF involved in dipeptide transport. Responsible for energy coupling to the transport system (Probable).
Subcellular location: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Dipeptide transport ATP-binding protein DppD
- Dipeptide transport system permease protein DppB
- Dipeptide transport system permease protein DppC
- Dipeptide-binding protein
- Oligopeptide transport system permease protein OppC
- Probable D,D-dipeptide transport system permease protein DdpC
- Glutathione transport system permease protein GsiD
- Nickel transport system permease protein NikC
- Putrescine export system permease protein SapC
- Oligopeptide transport system permease protein OppB
Sequence:
MSTQEATLQQPLLQAIDLKKHYPVKKGMFAPERLVKALDGVSFNLERGKTLAVVGESGCGKSTLGRLLTMIEMPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSKEQRREKALSMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKDQIFNNPRHPYTQALLSATPRLNPDDRRERIKLSGELPSPLNPPPGCAFNARCRRRFGPCTQLQPQLKDYGGQLVACFAVDQDENPQR
Protein: Amphoterin-induced protein 2 (AMIGO-2) (Alivin-1) (Q80ZD9)
Organism: Mus musculus (Mouse)
Function: Required for depolarization-dependent survival of cultured cerebellar granule neurons. May mediate homophilic as well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3. May contribute to signal transduction through its intracellular domain (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated with nucleus as well as plasma membrane. Restricted to somata of cerebellar as well as hippocampal neurons (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSLRFHTLPTLPRAVKPGCRELLCLLVIAVMVSPSASGMCPTACICATDIVSCTNKNLSKVPGNLFRLIKRLDLSYNRIGLLDADWIPVSFVKLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRLKSVKSATFQELKALEVLLLYNNHISYLDPAAFGGLSHLQKLYLSGNFLTQFPMDLYTGRFKLADLTFLDVSYNRIPSIPMHHINLVPGRQLRGIYLHGNPFVCDCSLYSLLIFWYRRHFSSVMDFKNDYTCRLWSDSRHSHQLQLLQESFLNCSYSVINGSFHALGFIHEAQVGERAIVHCDSKTGNGNTDFIWVGPDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMNRQRLLNETVDIMINVSNFTINRSHAHEAFNTAFTTLAACVASIVLVLLYLYLTPCPCKCKAKRQKNTLSQSSAHSSILSPGPTGDASADDRKAGKRVVFLEPLKDTAAGQNGKVKLFPSETVIAEGILKSTRAKSDSDSVNSVFSDTPFVAST
Protein: Protein unc-45 homolog B (Unc-45B) (UNC45-related protein) (Q6DGE9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain (By similarity). Plays a role in sarcomere formation during muscle cell development. Required for myoseptal integrity, myofiber attachment, motility and craniofacial development. Is necessary for normal early lens development.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}.
Interaction partners:
- Heat shock protein HSP 90-alpha 1
- [histone H3]-lysine
- Heat shock protein 90, alpha
- SET and MYND domain-containing 1a.
- Heat shock protein HSP 90-beta
- Ubiquitin conjugation factor E4 B
- Titin, tandem duplicate 1.
Sequence:
MTMGEIGDSVQLKEEGNKHFQAGEIDQAIDCYTKAIKTCKKEDKKALAVIYRNRSACFLKKENYSNAASDATKAIDVDAADIKALYRRCQAFEKLGKLDMAFKDVQRCATIEPKNKTFLETLRRLGAEIQQKLKTTFSTDSRVQNMFDILFSDEPDKEKREKAANNLIVLAREDAGAERIFQNNGVPLLMQLIDTGKPEMILAAIRTLSGMCTGHRARATAIIHSVGISKLCSIMAVDNEEIALATANLFQCVNDSLSGGDKRNYGKEEALVLDSSKDLKDILLALLEMIASKNVSGHGRDQALNLLTKNVPRQNKKSTDNSKCLFTIDHGLKKILKVCGQVPDLPDQLPMTENTQLIASVLLSKLYDDLRCDPERDQFRDICDDYIKSKFDPNDMDKNIHAINTLSGILQGPFDLGNVLAGRQGVMEMMVALCGSEREVDQLVAVEALIHASTKTSKASFFISNGVSLLKEMYKKTKNEKIKIRALVGLCKLGSAGGDDYSMRQFAEGSTEKLAKQCRKWLCNPTLDVRTRKWAIEGLAYLTNDADVKDDFAEDEPAMRAMFELTKSNDKTILYAVACTLVNCTNSYDKKEIIPEMVQLAKFSKQHVPEQHPKDKKDFIVRRVKRLLKAGVTSALAVMVKADNSILTDQTKEMLARVFLALTEDVKDRGIIVAQGGGKALIPLALEGTDKGKIKASHALAKIAAVSNPEIAFPGERIYEVVRPLVSLLGTDRDGMENFEALRGLTNLAGLNDKLRVKILKEKALPEIENYMFEDHEQIRQAATECMCNLVCCKEVQDRYLEDGNDKLKLLVLLCGEDEEKLQRAAAGALAMLTAAQKKLAVKMTKVTEQWLEILQRLCIHDNPEIQHRGLVTVFNMLDADDQLAKKLVESDMLEILTYVAKLEDNPKKQNAIDAARACLSKAMDNGLIKPFSN
Protein: Probable nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (QAPRTase) (P77938)
Organism: Rhodospirillum rubrum
Function: Involved in the catabolism of quinolinic acid (QA).
Interaction partners:
Sequence:
MRPNHPVAALSPFAIDEAVRRALAEDLGRAGDITSTATIPAATRAHARFVARQPGILAGLGCARSAFALLDDTVTFTTPLEDGAEIAAGQTVAEVAGAARTILAAERTALNFLGHLSGIATRTRRFGDAIAHTRARLTCTRKTTPGLRGLEKYAVRCGGGSNHRFGLDDAVLIKDNHIAVAGGVSAALSRARAGVGHMVRIEIEVDTLEQLAEVLAVGGAEVVLLDNMDAPTLTRAVDMVAGRLVTEASGGVSLDTIAALAESGVDYISVGALTHSVTTLDIGLDIVVAPPKAERA
Protein: Sorting nexin-6 (TRAF4-associated factor 2) [Cleaved into: Sorting nexin-6, N-terminally processed] (Q9UNH7)
Organism: Homo sapiens (Human)
Function: Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R. May function as link between transport vesicles and dynactin (Probable). Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation. In association with GIT1 involved in EGFR degradation. Promotes lysosomal degradation of CDKN1B (By similarity). May contribute to transcription regulation (Probable).
Subcellular location: Early endosome {ECO:0000269|PubMed:11485546, ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:19935774}. Early endosome membrane {ECO:0000269|PubMed:19935774, ECO:0000303|PubMed:11485546}; Peripheral membrane protein {ECO:0000269|PubMed:11485546}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:20354142}. Cytoplasm {ECO:0000269|PubMed:20830743}. Nucleus {ECO:0000269|PubMed:11591366, ECO:0000269|PubMed:20830743}. Note=Interaction with SNX1 or SNX2 promotes location at endosome membranes (PubMed:19935774). Only a minor proportion is seen in the nucleus. {ECO:0000269|PubMed:19935774}.
Interaction partners:
- Sorting nexin-2
- Sorting nexin-1
- Sorting nexin-5
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26A
- Sorting nexin-32
- Sorting nexin-3
- Sorting nexin-4
- TBC1 domain family member 5
Sequence:
MMEGLDDGPDFLSEEDRGLKAINVDLQSDAALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRRDLNFHVFLEYNQDLSVRGKNKKEKLEDFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICKFFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNGDT
Protein: Kelch-like protein 12 (CUL3-interacting protein 1) (DKIR homolog) (hDKIR) (Q53G59)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport. The BCR(KLHL12) complex is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). The BCR(KLHL12) complex is also involved in neural crest specification: in response to cytosolic calcium increase, interacts with the heterodimer formed with PEF1 and PDCD6/ALG-2, leading to bridge together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export. As part of the BCR(KLHL12) complex, also acts as a negative regulator of the Wnt signaling pathway by mediating ubiquitination and subsequent proteolysis of DVL3. The BCR(KLHL12) complex also mediates polyubiquitination of DRD4 and PEF1, without leading to degradation of these proteins.
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle {ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27716508}.
Interaction partners:
- Cullin-3
- Peflin
- Segment polarity protein dishevelled homolog DVL-1
- Protein transport protein Sec31A
- Protein SEC13 homolog
- Kelch-like protein 3
- Programmed cell death protein 6
- Protein transport protein Sec24B
- Protein transport protein Sec23A
- Protein transport protein Sec24C
Sequence:
MGGIMAPKDIMTNTHAKSILNSMNSLRKSNTLCDVTLRVEQKDFPAHRIVLAACSDYFCAMFTSELSEKGKPYVDIQGLTASTMEILLDFVYTETVHVTVENVQELLPAACLLQLKGVKQACCEFLESQLDPSNCLGIRDFAETHNCVDLMQAAEVFSQKHFPEVVQHEEFILLSQGEVEKLIKCDEIQVDSEEPVFEAVINWVKHAKKEREESLPNLLQYVRMPLLTPRYITDVIDAEPFIRCSLQCRDLVDEAKKFHLRPELRSQMQGPRTRARLGANEVLLVVGGFGSQQSPIDVVEKYDPKTQEWSFLPSITRKRRYVASVSLHDRIYVIGGYDGRSRLSSVECLDYTADEDGVWYSVAPMNVRRGLAGATTLGDMIYVSGGFDGSRRHTSMERYDPNIDQWSMLGDMQTAREGAGLVVASGVIYCLGGYDGLNILNSVEKYDPHTGHWTNVTPMATKRSGAGVALLNDHIYVVGGFDGTAHLSSVEAYNIRTDSWTTVTSMTTPRCYVGATVLRGRLYAIAGYDGNSLLSSIECYDPIIDSWEVVTSMGTQRCDAGVCVLREK
Protein: Protein arginine methyltransferase NDUFAF7 homolog, mitochondrial (EC 2.1.1.320) (NADH dehydrogenase [ubiquinone] complex I, assembly factor 7 homolog) (Protein midA homolog) (O14138)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable octanoyltransferase
- mRNA export factor elf1
- Elongation factor 3
- Putative uncharacterized oxidoreductase C1773.04
- Nucleoporin nup184
- Probable nudix hydrolase C6G9.05
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS15
- tRNA
- Small ribosomal subunit protein uS5
Sequence:
MLNLYMWKLSRSQVYQASLLFGSRVISALAFTNTGLVLHGPRRWYTTDNGFLLHRDSKVSLADYIHESTFDPSKGYYSRLWTGSTNNLSHSVHVLRKEGHKCSKEFDPFLHGIPIPQKALNIYEKQRSLFSESISNYLVLQYKLRYFPVFDLKIYDFHSGTGIIALDILDYLYKNHLEVYGRTTYNIVLHNSWQASWFKSMLTSVRYAKHGDHIDIYVSDPLTWNHTDTNPCFVLALQVISSFGHDLFRQSNGAMMMERCWLGPEHFLNEFFTLNTHQKVSSLNYHLAFQQARINVQQGFSDSRAKRYFSGVKQVFWSFFSTQKLTYYPTKAIRFFERLSKQFPHHSLLLMDVCHVDKSLPGINAPSVLSMENDFSTKKMSSNIGHVFQNETVKYVFPTPLYLVSDILQLATHNRSFICSLPHFLRRWSNEHGRKFFVPVEPSSKNLKVPYSFNNYYVVSSMPTYYY
Protein: Putative TGFB1-induced anti-apoptotic factor 1 (12 kDa TGF-beta-1-induced antiapoptotic factor) (O95411)
Organism: Homo sapiens (Human)
Function: Inhibits the cytotoxic effects of TNF-alpha and overexpressed TNF receptor adapters TRADD, FADD, and RIPK1. Involved in TGF-beta1 inhibition of IkappaB-alpha expression and suppression of TNF-mediated IkappaB-alpha degradation.
Subcellular location: [Isoform TIAF1]: Nucleus {ECO:0000269|PubMed:9918798}.
Interaction partners:
- Unconventional myosin-XVIIIa
Sequence:
MSSPSSPFREQSFLCAAGDAGEESRVQVLKNEVRRGSPVLLGWVEQAYADKCVCGPSAPPAPTPPSLSQRVMCNDLFKVNPFQLQQFRADPSTASLLLCPGGLDHKLNLRGKAWG
Protein: Ubiquitin-specific protease 15 (F4I642)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLEPRGADIPILFLVLVVLPVVAYILLGKWSNISEKRVRANLLAQMAAEEALRAETVVNADRGVRFESVATENRAQRTRTKTVSAGGGAVRAEFDAGARETVAEQRSDSVTATCGVTVVAPVNNNELHVCARCFGPAKTRCSRCKSVRYCSGKCQIIHWRVAHKDECVPVESCSSSSERVSFEKDSVLYDHGMDSTMYSNNTTQAAKGKTSKSSVDFASLGISQNDITPQINTQGRKSVGKQHSSKANRESCRRDSATVFDSSDEAASAGGDNKTSHIKHKSRGNSYAAETNPRRHSVDSSAVQMNGQSFVSGMQESHKHENNLGVRSSFGCPNTQYPSNGTRTATLPRTGINKSGEQSCTETSKKGQVAAVSKTVRSKDTGISEESNGISSTMGIMKMMGLRNSTKHDDRYKNLKVSSLMLFPYEEFLKFFQCEVFDLSPRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRILSHMRSINCQIGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYGWVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMTRTGDVPPLYMLYAVIVHLDTLNASFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYMRSYPRPQRGEHNGKAPVHHSQPRNEMKEQRKPVNRFKPRADHKNTESSSSEWSLFTSSDEASFTTESTRDSFSTIDYTDVCHVVDSSSPFAIFNNVYHNVEPSPHNTVACRMFSGTKPETRYFVEQETNHNNTVVLDATPSLYPIPAPYPPHDYYDQSMYVNYETNPEFNNGQDQDRTYSYW
Protein: C3H1-type domain-containing protein (Q57Z17)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein
- Cleavage and polyadenylation specificity factor subunit, putative
- Cleavage and polyadenylation specificity factor-like protein, putative
- Suppressor of forked domain-containing protein
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Cleavage and polyadenylation specificity factor subunit 2
- Uncharacterized protein
- Nucleic acid binding protein, putative
- Cleavage and polyadenylation specificity factor subunit 5
- RNA-binding protein, putative
Sequence:
MEEGGEGPFVITHADGVENPTFVTVQATDGQEMERQPQGFEPENVKDDVVGLIPLCVRHAEGPQINTAVFGYDIAQMQKRPWDEPTANLRDYFNYGFNESSWRLYCSMQAEGESSLLAKANTFLRKLNTSAMKGGADEAMGGEPTPYYMPPTHPQGSSHTYYGGQRDGFHNSRGVCQRFLEGRCGKGDQCNYSHVYGGMCAPPAMHHHHHHHHHHHHHHHHRQPPYVLPNFGGDPGVLPHVGTPVTGVLDPNTPAPPYGAVPPPPPPQQQQQQQQHSEDT
Protein: Matrix protein 2 (Proton channel protein M2) (Q6DPW5)
Organism: Influenza A virus (strain A/Vietnam/1203/2004 H5N1)
Subcellular location: Virion membrane {ECO:0000256|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000256|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000256|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000256|HAMAP-Rule:MF_04069}.
Interaction partners:
Sequence:
MSLLTEVETPTRNEWECRCSDSSDPIVVAANIIGILHLILWILDRLFFKCIYRRLKYGLKRGPATAGVPESMREEYRQEQQSAVDVDDGHFVNIELE
Protein: Sphingolipid delta(4)-desaturase DES1 (EC 1.14.19.17) (Degenerative spermatocyte homolog 1) (Dihydroceramide desaturase-1) (Retinol isomerase) (EC 5.2.1.-) (O09005)
Organism: Mus musculus (Mouse)
Function: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). Catalyzes the equilibrium isomerization of retinols (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:O15121}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15121}.
Interaction partners:
- Ceramide synthase 2
- Ceramide glucosyltransferase
- 3-ketodihydrosphingosine reductase
- Ceramide synthase 5
- Ceramide synthase 4
- Ceramide synthase 3
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
- Acid ceramidase
- Sphingomyelin phosphodiesterase 2
Sequence:
MGSRVSREEFEWVYTDQPHAARRKEILAKYPEIKSLMKPDHNLIWIVAMMLLVQLASFYLVKDLDWKWVIFWSYVFGSCLNHSMTLAIHEISHNFPFGHHKALWNRWFGMFANLSLGVPYSISFKRYHMDHHRYLGADKIDVDIPTDFEGWFFCTTFRKFVWVILQPLFYAFRPLFINPKPITYLEIINTVIQITFDIIIYYVFGVKSLVYMLAATLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPMVRKIASEYYDDLPHYNSWIKVLYDFVTDDTISPYSRMKRPPKGNEILE
Protein: Protein singed (Q24524)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as an actin bundling protein. May have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Forked, isoform F
Sequence:
MNGQGCELGHSNGDIISQNQQKGWWTIGLINGQHKYMTAETFGFKLNANGASLKKKQLWTLEPSNTGESIIYLRSHLNKYLSVDQFGNVLCESDERDAGSRFQISISEDGSGRWALKNESRGYFLGGTPDKLVCTAKTPGASEFWTVHLAARPQVNLRSIGRKRFAHLSESQDEIHVDANIPWGEDTLFTLEFRAEEGGRYALHTCNNKYLNANGKLQVVCNEDCLFSAEYHGGHLALRDRQGQYLSPIGSKAVLKSRSSSVTRDELFSLEDSLPQASFIAGLNLRYVSVKQGVDVTANQDEVGENETFQLEYDWSAHRWALRTTQDRYWCLSAGGGIQATGNRRCADALFELIWHGDGSLSFRANNGKFLATKRSGHLFATSESIEEIAKFYFYLINRPILVLKCEQGFVGYRTPGNLKLECNKATYETILVERAQKGLVHLKAHSGKYWRIEGESISVDADAPSDGFFLELREPTRICIRSQQGKYLGATKNGAFKLLDDGTDSATQWEF