wanglab/gogpt-training-data huggingface dataset:
Protein: Sphingolipid C9-methyltransferase (C-9-MT) (EC 2.1.1.317) (Cyclopropane fatty acyl phospholipid synthase homolog 1) (Methyltransferase for sphingolipid 1) (Q5APD4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes methylation of the sphingoid base component of glucosylceramides (GluCers) at the C9-position. Sphingolipid C9-methylation requires 4,8-desaturated ceramides as substrates. Glucosylceramides play important roles in growth, differentiation and pathogenicity. The methyl group at the C9-position distinguishes fungal glucosylceramides from those of plants and animals, and may thus play a role in host-pathogen interactions enabling the host to recognize the fungal attack and initiate specific defense responses. Not necessary for vegetative growth at low temperatures, but plays a role in hyphal formation on solid medium.
Subcellular location: Membrane {ECO:0000250|UniProtKB:C4R7Z3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- serine C-palmitoyltransferase
- Serine C-palmitoyltransferase
Sequence:
MLDDVAFIKTPAAKKQPPASNECGVWTTDSPAIHNAPLPADGPGSTSFSNTILFSILALVPGYITYKLGLGFKTWVFFFLILAIPILMAYWSIMSTFSPRINEKVKYPNRPISYYLEFHTPELKAKYETSNGGKGSKIPIETFQELYFDGKVSFKGDCLDVLEYKHDWASFRFTLGLFRFFLLGMIPEVIFHSQSQDEEQVRDHYDRGDDFYTWFLGPRMIYTSGVISDITREETLEELQDNKLTVMADKIDLKKGDHVLDIGCGWGTWTTFASSKYGANVTGITLGRNQTKWGNTLLKEYGIPSDQSRIVCCDYRDAPKSSKPSGKYDKITSVEMAEHVGIRRLTAYLEQCRDALEDDGLLFLQYSGLRKNWQYEDLEWGLFMNKYIFPGADASTPLSFFASCMESVGFEIVSVDNIGVHYSATLWRWYRNWIGNKDKVVNKYGVKWYRIWEFFLGSSVVASRNGTATCYQFICRKNINSYRRIDYVPQQKGLQGPVQEGTKWAKEFTNFYD
Protein: Cyanocobalamin reductase / alkylcobalamin dealkylase (Alkylcobalamin:glutathione S-alkyltransferase) (EC 2.5.1.151) (CblC) (Cyanocobalamin reductase (cyanide-eliminating)) (EC 1.16.1.6) (Methylmalonic aciduria and homocystinuria type C protein) (MMACHC) (Q9Y4U1)
Organism: Homo sapiens (Human)
Function: Cobalamin (vitamin B12) cytosolic chaperone that catalyzes the reductive decyanation of cyanocob(III)alamin (cyanocobalamin, CNCbl) to yield cob(II)alamin and cyanide, using FAD or FMN as cofactors and NADPH as cosubstrate. Cyanocobalamin constitutes the inactive form of vitamin B12 introduced from the diet, and is converted into the active cofactors methylcobalamin (MeCbl) involved in methionine biosynthesis, and 5'-deoxyadenosylcobalamin (AdoCbl) involved in the TCA cycle. Forms a complex with the lysosomal transporter ABCD4 and its chaperone LMBRD1, to transport cobalamin across the lysosomal membrane into the cytosol. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR (methionine synthase) which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine. Also acts as a glutathione transferase by catalyzing the dealkylation of the alkylcob(III)alamins MeCbl and AdoCbl, using the thiolate of glutathione for nucleophilic displacement to generate cob(I)alamin and the corresponding glutathione thioether. The conversion of incoming MeCbl or AdoCbl into a common intermediate cob(I)alamin is necessary to meet the cellular needs for both cofactors. Cysteine and homocysteine cannot substitute for glutathione in this reaction.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23270877}.
Interaction partners:
- Cobalamin trafficking protein CblD
- Lysosomal cobalamin transport escort protein LMBD1
- Methionine synthase
- Corrinoid adenosyltransferase MMAB
- Methylmalonic aciduria type A protein, mitochondrial
- Methylmalonyl-CoA mutase, mitochondrial
- Methionine synthase reductase
- Diacylglycerol kinase epsilon
- Lysosomal cobalamin transporter ABCD4
Sequence:
MEPKVAELKQKIEDTLCPFGFEVYPFQVAWYNELLPPAFHLPLPGPTLAFLVLSTPAMFDRALKPFLQSCHLRMLTDPVDQCVAYHLGRVRESLPELQIEIIADYEVHPNRRPKILAQTAAHVAGAAYYYQRQDVEADPWGNQRISGVCIHPRFGGWFAIRGVVLLPGIEVPDLPPRKPHDCVPTRADRIALLEGFNFHWRDWTYRDAVTPQERYSEEQKAYFSTPPAQRLALLGLAQPSEKPSSPSPDLPFTTPAPKKPGNPSRARSWLSPRVSPPASPGP
Protein: TMEM276-ZFTRAF1 readthrough (E9PQ42)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPKPGAEWSTALSHLVLGVVSLHAAVSTAECTNGHLMCAGCFIHLLADARLKEEQATCPNCRCEISKSLCCRNLAVEKAVSELPSECGFCLRQFPRSLLERHQKEECQDRVTQCKYKRIGCPWHGPFHELTVHEAACAHPTKTGSELMEILDGMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLSCKRTLSFQLLLKSKVTAPL
Protein: Serine/threonine-protein phosphatase 2A activator 2 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase PTPA-2) (PPIase PTPA-2) (Rotamase PTPA-2) (Phosphotyrosyl phosphatase activator 2) (Q12461)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein phosphatase PP2A regulatory subunit A
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP1-1
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Protein phosphatase PP2A regulatory subunit B
- Leucine carboxyl methyltransferase 1
- Type 2A phosphatase-associated protein 42
Sequence:
MLPEKRLLTPDDMKLWEESPTRAHFTKFIIDLAESVKGHENSQYKEPISESINSMMNLLSQIKDITQKHPVIKDADSSRFGKVEFRDFYDEVSRNSRKILRSEFPSLTDEQLEQLSIYLDESWGNKRRIDYGSGHELNFMCLLYGLYSYGIFNLSNDSTNLVLKVFIEYLKIMRILETKYWLEPAGSHGVWGLDDYHFLPFLFGAFQLTTHKHLKPISIHNNELVEMFAHRYLYFGCIAFINKVKSSASLRWHSPMLDDISGVKTWSKVAEGMIKMYKAEVLSKLPIMQHFYFSEFLPCPDGVSPPRGHIHDGTDKDDECNFEGHVHTTWGDCCGIKLPSAIAATEMNKKHHKPIPFD
Protein: Interleukin-17C (Il-17c) (Cytokine CX2) (Q8K4C5)
Organism: Mus musculus (Mouse)
Function: Cytokine that plays a crucial role in innate immunity of the epithelium, including to intestinal bacterial pathogens, in an autocrine manner. Stimulates the production of antibacterial peptides and pro-inflammatory molecules for host defense by signaling through the NFKB and MAPK pathways. Acts synergically with IL22, TNF and IL1B in inducing antibacterial peptides. May have protective function by maintaining epithelial homeostasis after an inflammatory challenge, such as that caused in the intestine by dextran sulfate sodium in a colitis model. May also promote an inflammatory phenotype, such as skin in a psoriasis model. Enhanced IL17C/IL17RE signaling may also lead to greater susceptibility to autoimmune diseases, such as autoimmune encephalitis.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Interleukin-17 receptor E
- Interleukin-17 receptor A
- Interleukin-17 receptor B
- Interleukin-17 receptor C
- Interleukin-17 receptor D
- Interleukin-22
Sequence:
MSLLLLGWLPTGMTHQDPPSWGKPRSHRTLRCYSAEELSHGQAPPHLLTRSARWEQALPVALVASLEATGHRRQHEGPLAGTQCPVLRPEEVLEADTHERSISPWRYRIDTDENRYPQKLAVAECLCRGCINAKTGRETAALNSVQLLQSLLVLRRQPCSRDGTADPTPGSFAFHTEFIRVPVGCTCVLPRSTQ
Protein: Splicing factor ESS-2 homolog (ES2 protein) (Expressed sequence 2 embryonic lethal) (O70279)
Organism: Mus musculus (Mouse)
Function: May be involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P34420}.
Interaction partners:
- Integral membrane protein DGCR2/IDD
- Estrogen receptor
- Polycomb protein Suz12
- Pre-mRNA-splicing factor SYF1
Sequence:
MGTPGTSAGALFLSSASAPSRKRAAGEAGEAGVARSRQRVLDEEEYIEGLQTVIQRDFFPDVEKLQAQKEYLEAEENGDLERMRQIAIKFGSALGKISREPPPPYVTPATFETPEVHPGSAVLGNKPRPQGRDLDDGEAGEEEEKEPLPSLDVFLSQYTSEDNASFQEIMEVAKEKSHARHAWLYQAEEEFEKRQKDNLELPSAEHQAIESSQAGVETWKYKAKNSLMYYPEGVPDEEQLFKKPRQIVHKNTRFLRDPFSQALSRSQLQQAAALNAQHKQGKVGPDGKELIPQESPRVGGFGFVATPSPAPGVNESPLMTWGEVENTPLRVEGSESPYVDRTPGPTFKILEPGRRERLGLKMANEAAAKNRAKKQEALRRVTENLASLTPKGLSPAMSPALQRLVSRTASKYTDRALRASYTPSPARSSHLKTPAGGPQTPTSTPAPGSATRTPLTQDPASITDNLLQLPARRKASDFF
Protein: Ribosomal RNA-processing protein 7 (O94683)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays an important role in the synthesis of 18S rRNA but is not required for the 5.8S and 25S pathway. Is necessary for the cleavage at site A2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 22
- rRNA biogenesis protein rrp5
- U3 small nucleolar RNA-associated protein 10
- Ribosome biogenesis protein enp2 homolog
- U3 small nucleolar RNA-associated protein 21 homolog
- Probable U3 small nucleolar RNA-associated protein 18
- RNA cytidine acetyltransferase
- Ribosome biogenesis protein bms1
- KRR1 small subunit processome component homolog
- Periodic tryptophan protein 2 homolog
Sequence:
MDKLKEKGFVKLEIYLENKKRLHSIFLKEDTEDVEKKSLYLINVPITTTEKILKRAISQLGGRIVNIYPNISGLLKSGTHLRVKLVEPAEVKQVIKAASKKTTSLPWKFTQHTGLKRYVESYDRQFVNPRVLAESVDSYMKRVTKKEIAEKRRLFAMKNQPDEDGFVTVVRSGRAPVGRPQDAERQLEKKKDTGIHKDFYRFQLREKKKKALLDLAHKFEFDKQRIQQLKEKRQFKPY
Protein: RNA-binding protein 27 (RNA-binding motif protein 27) (Q9P2N5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm. Nucleus speckle. Note=Incorporated into the nuclear speckles and to speckles proximal to the nuclear periphery. Also localizes to punctate structures in the cytoplasm termed cytospeckles (By similarity). {ECO:0000250}.
Interaction partners:
- Zinc finger C3H1 domain-containing protein
Sequence:
MLIEDVDALKSWLAKLLEPICDADPSALANYVVALVKKDKPEKELKAFCADQLDVFLQKETSGFVDKLFESLYTKNYLPLLEPVKPEPKPLVQEKEEIKEEVFQEPAEEERDGRKKKYPSPQKTRSESSERRTREKKREDGKWRDYDRYYERNELYREKYDWRRGRSKSRSKSRGLSRSRSRSRGRSKDRDPNRNVEHRERSKFKSERNDLESSYVPVSAPPPNSSEQYSSGAQSIPSTVTVIAPAHHSENTTESWSNYYNNHSSSNSFGRNLPPKRRCRDYDERGFCVLGDLCQFDHGNDPLVVDEVALPSMIPFPPPPPGLPPPPPPGMLMPPMPGPGPGPGPGPGPGPGPGPGPGHSMRLPVPQGHGQPPPSVVLPIPRPPITQSSLINSRDQPGTSAVPNLASVGTRLPPPLPQNLLYTVSERQPMYSREHGAAASERLQLGTPPPLLAARLVPPRNLMGSSIGYHTSVSSPTPLVPDTYEPDGYNPEAPSITSSGRSQYRQFFSRTQTQRPNLIGLTSGDMDVNPRAANIVIQTEPPVPVSINSNITRVVLEPDSRKRAMSGLEGPLTKKPWLGKQGNNNQNKPGFLRKNQYTNTKLEVKKIPQELNNITKLNEHFSKFGTIVNIQVAFKGDPEAALIQYLTNEEARKAISSTEAVLNNRFIRVLWHRENNEQPTLQSSAQLLLQQQQTLSHLSQQHHHLPQHLHQQQVLVAQSAPSTVHGGIQKMMSKPQTSGAYVLNKVPVKHRLGHAGGNQSDASHLLNQSGGAGEDCQIFSTPGHPKMIYSSSNLKTPSKLCSGSKSHDVQEVLKKKQEAMKLQQDMRKKRQEVLEKQIECQKMLISKLEKNKNMKPEERANIMKTLKELGEKISQLKDELKTSSAVSTPSKVKTKTEAQKELLDTELDLHKRLSSGEDTTELRKKLSQLQVEAARLGILPVGRGKTMSSQGRGRGRGRGGRGRGSLNHMVVDHRPKALTVGGFIEEEKEDLLQHFSTANQGPKFKDRRLQISWHKPKVPSISTETEEEEVKEEETETSDLFLPDDDDEDEDEYESRSWRR
Protein: Putative ankyrin repeat domain-containing protein 26-like 1 (Ankyrin repeat domain-containing protein 36B pseudogene 1) (Q96IX9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGTRTLQFEISDSHEKEEDLLHKNHLMQDEIARLRLEIHTIKNQILEKKYLKDIEIIKRKHEDLQKALKQNGEKSTKTIAHYSGQLTALTDENTMLRSKLEKEKQSRQRLTKWNHTIVD
Protein: Pericentrin-like protein, isoform H (M9PFA3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MSRLKLEFEKQLNRKNKRHLTFDAARDLEQVICERDGLRELSKSFRSVLCRLAKCVAHCEEDLNATLSEEVQRLLFHSRSQDGGDDLEATISSSLNNTKHMLRVPDVHSLLEVVEDPSLVQFIDSKSNEEPSEDFDLNDCLERLKSEASYLLHLSEDLHKQRTHDESSEHLDEPEKQEHELCCEAEDGLKTTGAVNQQVLSKFLRTNSLNDQQMGVANQRKNSNPEAGKTHSSLPPDLQEHAGNASELSFQLVQLKNRLIKSEADRQNLQQQLSRTIDRNAELGQELQALRDQLSQLNSLNHTDYNEGYGLGTMKSLQEQGLDQSSASFLALQERARHLLSSSPVKEQPSRDHGNSTVILLQMIEDFCREGDKVVEFSKKDREDLQSQIDTADKQLKDTRRFLEDQAAEREQERDEFQREIERLKAQLRDKEKEHSSYANASEEYAQLESQFREVNQQLCESNAKRDKFEVELKASIDKIFVLREIISELETQVQTKALNEEVLAEKAQQLEEYVSLQMRDNDILQQEVHSLKTDIGEGYQSRIRVLEEKLKQSGPTAEQGVVLSQVAEKLRDIETTLDQKTKALESLHNSNATSNSASLSVTEDVSIHGSKEPTAVGSPSHPSLTVEGVQRVTEKLDRHTRVEEAAIKRIRDLEMQVHQMRAGCVELQHERDTLQGRMEEQTQRISTLQNRLEEQRQRAEQLHRTGTSDLNTRVHELQGEVQNLYEQLAARDKQMANMRQQLQRSKEEITRLETEVEVRTQPDRSLVNKLQAEVQQKGAEIVKLKDKIRTEMINRLAIPDLMETMLADKNDEIDHLRDQLEAKEKELQASQQEASQISSPSGAAGKQEGSGGKLSARTLSDIGSITEFPEPDVERRAAMRSLTALQMSEGAGGFLHQTMETSKEAVANLTHKRTDDLSGFIVPYPVNTFEHPHYFQALGVTAQSTDGLTPGLVPRQINFSNLTEDSKLKTTSLLMHTPELPRPTTPPEIHQLRVKLSDLQTEKQRQQSELEKKLQDLQKELEQEKEKLSRQAQTLQSYEESEAKYRLRIENLESKVLETAAQAASDRENLRKELNCVSAAHEQCENAAAARKRELEKLNSEVKVKADQLHAALRRCADLELQVLTLERDLERLKNSDNSSKQYSVDEIAQQVEKELNYSAQLDSNILKAIESEEENNLDKKLQKGVQTEEETLPGTGNGTDDENFTGERELLNQLEALRAQLAVEREQCEAMSKELLGEKQHSQDIQEQDVIIIEAMRKRLETALDAEDELHKQLDQERERCERLQTQLTSLQRAESRRNSSLLLKSPGDSPRKSPRADFESELGDRLRSEIKLLVAQNERERERSADAQRSSERERQRYEKELQERVAYCERLKQEMEKLSRDKESAETELEHFNERLTLQASEIESLEARLVTLQEAETRRANTRTRQHQENVKLQAEIHELKSKLLAAEAARDCLDQKVTQLRFDVSRSGQREAKLAEALAQANDRLAHSTDDNVPAQFMQKMKEINALLAENTQENRQMAETVQFLVGERIALQKKCEELGGAGNTNVTELEERCRQLIGRYLRVESHRKALVYQKRYLKLTLEGYQASEQLALQNLRGGAEQPPQRNIKKKFKTVALAIIAIQRIKYIGRIWHTGKRIVSKSVFTITQQRSPGLNLNVAPPQSPLPGPNSNLPTNNNNLMGRLSYAPLSPPMVNFSTVQPIMLPSDFTLQAPTTSLQTTIANNNSENTLPSLARLDWPTMQKPKRAHARHH
Protein: NADH-ubiquinone oxidoreductase chain 6 (EC 7.1.1.2) (NADH dehydrogenase subunit 6) (P03924)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:25209663, ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 1
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 subunit C2
Sequence:
MMLYIVFILSVIFVMGFVGFSSKPSPIYGGLGLIVSGGVGCGIVLNFGGSFLGLMVFLIYLGGMMVVFGYTTAMATEQYPEIWLSNKAVLGAFVTGLLMEFFMVYYVLKDKEVEVVFEFNGLGDWVIYDTGDSGFFSEEAMGIAALYSYGTWLVIVTGWSLLIGVVVIMEITRGN
Protein: FCS-Like Zinc finger 11 (Q9SL94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29945970}. Nucleus {ECO:0000269|PubMed:29945970}.
Interaction partners:
- FCS-Like Zinc finger 15
- FCS-Like Zinc finger 12
- FCS-Like Zinc finger 16
- FCS-Like Zinc finger 17
- Protein INCREASED RESISTANCE TO MYZUS PERSICAE 1
- FCS-Like Zinc finger 3
- FCS-Like Zinc finger 1
- FCS-Like Zinc finger 2
Sequence:
MLKTRAMFPHKDQAMSLSLDPQSDLVVGHTNNRPITNPLALSLLIGLNNKNKCISDSDFVRSPKSPLEFRVLSTMADSFFLRSPRSSLTAHLNCCCGPAAKVGLSIVDSLGDDRCLLPDIVFGPALRIKCSEVMDKHPKLLFPVANKSKKIENERSGVVFEIGDNSSETEPVGLRNRSFSANDCLRKTRVLSRSKLGQEGDFPGSGSDNAFSSEDDMEDYTCIIAHGPNPKTTHIYGDRVLECHKNELKGDEDNKEKFGSVFPSDNFLGICNFCNKKLGGGDDIYMYREKSFCSEECRSEEMMIDEEDLEEPCIDMHESLKKLF
Protein: F-box only protein 6 (F-box only protein 6b) (F-box protein that recognizes sugar chains 2) (F-box/G-domain protein 2) (Q9QZN4)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to insure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication (By similarity). Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- F-box only protein 2
- S-phase kinase-associated protein 1
- Cullin-1
Sequence:
MVHINELPENILLELFIHIPAPQLLRNCRLVCRLWRDLIDVVSLWKRKSLREGFFTKDRCEPVEDWKVFYILCSLQRNLLRNPCAEENLSSWRIDSNGGDRWKVETLPGSCGTSFPDNKVKKYFVTSFEMCLKSQMVDLKAEGYCEELMDTFRPDIVVKDWVAPRADCGCTYQLRVQLASADYIVLASFEPPPVTFQQWNDAKWQEISHTFSDYPPGVRHILFQHGGQDTQFWKGWYGPRVTNSSIIISHRTAKNPPPARTLPEETVVIGRRRRASDSNTHEGFFWQGLWQRLRR
Protein: NADH kinase POS5, mitochondrial (EC 2.7.1.86) (Q06892)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphorylates both NADH and NAD(+), with a twofold preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:12727869, ECO:0000269|PubMed:12912900, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- Isocitrate dehydrogenase, mitochondrial
- NAD
- ATP-NADH kinase YEF1
- Potassium-activated aldehyde dehydrogenase, mitochondrial
- NAD-dependent malic enzyme, mitochondrial
Sequence:
MFVRVKLNKPVKWYRFYSTLDSHSLKLQSGSKFVKIKPVNNLRSSSSADFVSPPNSKLQSLIWQNPLQNVYITKKPWTPSTREAMVEFITHLHESYPEVNVIVQPDVAEEISQDFKSPLENDPNRPHILYTGPEQDIVNRTDLLVTLGGDGTILHGVSMFGNTQVPPVLAFALGTLGFLSPFDFKEHKKVFQEVISSRAKCLHRTRLECHLKKKDSNSSIVTHAMNDIFLHRGNSPHLTNLDIFIDGEFLTRTTADGVALATPTGSTAYSLSAGGSIVSPLVPAILMTPICPRSLSFRPLILPHSSHIRIKIGSKLNQKPVNSVVKLSVDGIPQQDLDVGDEIYVINEVGTIYIDGTQLPTTRKTENDFNNSKKPKRSGIYCVAKTENDWIRGINELLGFNSSFRLTKRQTDND
Protein: Uncharacterized protein UNK4,15 (O14080)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized transcriptional regulatory protein C139.03
- Uncharacterized membrane protein C3H7.05c
- Uncharacterized transporter C11D3.06
- Protein rds1
- Putative uracil phosphoribosyltransferase urg2
- Uncharacterized transcriptional regulatory protein C1399.05c
- Uncharacterized transcriptional regulatory protein PB24D3.01
- Uracil phosphoribosyltransferase 2
Sequence:
MPQFFRTQPLTDRTTSHGFAEVSSEDHCYCVWLVPAISSDIELRYRTFVDWAVCHKVDFEEMQLPTAPHITLARGIKLKPNQSFKSVLQYIASKRKSPLNIKFGKVAIGDSFYKRVYIQVEKTPGLEELQNAAYDLADTSDPFNVIEHPYMPVIYAKSICSDYSTSDPIETISSIGQASWGKACFLELIQLNKANHQGYVCDRIEFTV
Protein: Decapping protein 2, isoform E (LP11827p) (Q5U127)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Decapping protein 1, isoform A
- Enhancer of mRNA-decapping protein 3
- Protein associated with topo II related - 1, isoform A
- Enhancer of mRNA-decapping protein 4 homolog
- ATP-dependent RNA helicase me31b
- 5'-3' exoribonuclease 1
- U6 snRNA-associated Sm-like protein LSm1
- poly
- Trailer hitch, isoform H
- NAD
Sequence:
MEIAPLINNAVAVVTASASAAVSASASVGSSSKDDNVNNLALLASLTLQKVLNINNNNNQHSKNNNHSDNSNSKQHEQQKQQQQPQRRNLDIKSEYDVLNQLLKTGAVFTATPTAPIAIERRKQTQQQQRPYAQQAHQQQQQKQRLNSSISSTHSSTSTNSSYGSSSSEDAAGTSAPTGAGEVVTSAALTPRASTTKASSNKLPEKSKIPSDILDDLASRFIINVPDMELNNLIRMCFQIELAHWFYLDFFCAPESGEDGETPKCVQRKLPSVGIKQFAMQLFQHIPFLNKHFGTVDQILDEWKNYKLSVPTYGAILVSEDHNHCLLVQSYFARNSWGFPKGKINENEDPAHCATREVYEETGFDITDLIDANDYIEAFINYQYTRLYVVRNIPMDTQFAPRTRNEIKCCDWFRIDALPVNKNDAISKAKLGKTSNSFFMIMPFVKRLKKWVNDRKAGIEPRRRKFSGQQSPKAASPTNMNGNCKKDVTGVRNESQRQRHKSMGDLDGVKLNNLNGKGTVGTGAGSAASASATAAINSMNICNSNGKRNKQNAAAGSNQATPTTIATPMTSNGAVVGGTVSSKRQLFHSQSQNDAQQSASNEKQIVSSFDLIRKEKQQQLKAAKAQKQQQQQQQRSRTKSQSDKQYNPQQPVKILGQQQPTTGMDLIAMLSAAAAAQKTPNNEQQTQEKQQQQQRPRPASVSLNLGAGSATGATTSAPDAQYMHRLQRMASGTNLRILKRAQSQQPQQHHQQQLQLEQQQQQQQQLGIDFTPNLNSWTNFSFTKNFIANVFC
Protein: Bloodthirsty-related gene family, member 20 (A0A0R4IUT0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAESLPTSTKGKAARRRSIDDPPWMSSSSGPLSEELRCSICLEVFTDPVSTPCGHNFCKSCLNKYWNNSQTCSCPNCKETFTQRPDLKINTTLREISEHYKEKRPEEKAEVVCDMCEGRKLKALKSCLVCQISYCQTHLEPHSRIAGLKKHKLMDPVRNLEDYICQKHDRPLELFCRDDQQIICVSCTDGDHRNHNTVSLEKTELMIQDTEQMIQDRIKRIQHIKHSAADRKIYSEKEKAAHVEIFTDLIRSIEGCQIELLEMMEEQQKAAEKQEEELIEELEQEITKLKMRNTKLQQISHTEDLLQIYSSLQCRPADTRNWPEISVKTQENLEDLRGALNQLKDTVGEKLTQIELKWMQQYAVDVTLDPDTAHPKLILSDDGKQVKHGDIRQKLPNKPQRFDRYAMVLGKEGFSSGRFYFEVQVKGKTKWDLGVVRESVDRKGKITLRPSDGFWTVCLRNGNQYKAGADSPVSLSLKVKLQRVGVFVDYEEGLVSFYDVESSSHIYSFTGQTFTDKLYPYFSPEDNDDGKNSAPLIITPVSSK
Protein: IST1 homolog (Charged multivesicular body protein 8) (F1R0S8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLGGGFKSERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLSAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLTRFGLIQSMKELDPGLQEAVSTLIWAAPRLQSEVAELKIVSDQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDAMVRPEVCPGEEADLIDVDSDFKKPGAGGGGGGGGGFTAPAMGMPMPMPMPMPMPTAFNYPPPKGAEPFNGPVGTYDGFSNFQAPMRGGQPPQLPSCPPTYESVIPGPTPAGQVYDNSTLPELPSVPDTLPASSFGAKANTSEDIDFDDLSRRFEELKKKT
Protein: Alpha-actinin-3 (Alpha-actinin skeletal muscle isoform 3) (F-actin cross-linking protein) (O88990)
Organism: Mus musculus (Mouse)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity).
Interaction partners:
- Troponin T, fast skeletal muscle
- Myozenin-1
- Myosin-binding protein C, fast-type
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin C, skeletal muscle
- Troponin I, fast skeletal muscle
- Alpha-actinin-2
- Myosin-4
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Tropomodulin-4
Sequence:
MMMVMQPEGLGAGEGPFSGGGGGEYMEQEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENEKLMEEYEKLASELLEWIRRTVPWLENRVGEPSMSAMQRKLEDFRDYRRLHKPPRVQEKCQLEINFNTLQTKLRLSHRPAFMPSEGKLVSDIANAWRGLEQVEKGYEDWLLSEIRRLQRLQHLAEKFQQKASLHEAWTRGKEEMLNQHDYESASLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERMEKLLETIDQLQLEFARRAAPFNNWLDGAIEDLQDVWLVHSVEETQSLLTAHEQFKATLPEADRERGAILGIQGEIQKICQTYGLRPKSGNPYITLSSQDINNKWDTVRKLVPSRDQTLQEELARQQVNERLRRQFAAQANAIGPWIQGKVEEVGRLAAGLAGSLEEQMAGLRQQEQNIINYKSNIDRLEGDHQLLQESLVFDNKHTVYSMEHIRVGWEQLLTSIARTINEVENQVLTRDAKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETDTAEQVVASFKILAGDKNYITPEELRRELPAEQAEYCIRRMAPYKGSGAPSGALDYVAFSSALYGESDL
Protein: Uncharacterized protein (Q3UVG8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVRSGDIPVHLETMEPGAMYCVRAQALVKAIGRHSAFSQPTCVEMQGESLPLALALFAFVGFMLILVVVLLSVWKMGQLLRYSCCPAVVLPDTLKITSSSQKLISCRKEEVDACAVAVLSSEHLFGVWISQT
Protein: Cutinase 1 (EC 3.1.1.74) (Cutin hydrolase 1) (P11373)
Organism: Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata)
Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:17043825}.
Interaction partners:
Sequence:
MKFLSVLSLAITLAAAAPVEVETGVALETRQSSTRNELETGSSSACPKVIYIFARASTEPGNMGISAGPIVADALERIYGANNVWVQGVGGPYLADLASNFLPDGTSSAAINEARRLFTLANTKCPNAAIVSGGYSQGTAVMAGSISGLSTTIKNQIKGVVLFGYTKNLQNLGRIPNFETSKTEVYCDIADAVCYGTLFILPAHFLYQTDAAVAAPRFLQARIG