wanglab/gogpt-training-data huggingface dataset:
Protein: Krueppel-like factor 4 (Epithelial zinc finger protein EZF) (Gut-enriched krueppel-like factor) (O43474)
Organism: Homo sapiens (Human)
Function: Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q60793}. Cytoplasm {ECO:0000250|UniProtKB:Q60793}.
Interaction partners:
- Transcription factor SOX-2
- Homeobox protein NANOG
- POU domain, class 5, transcription factor 1
- Catenin beta-1
- Protein lin-28 homolog A
- Histone deacetylase 2
- Histone acetyltransferase p300
- Myc proto-oncogene protein
- Cellular tumor antigen p53
- CCAAT/enhancer-binding protein beta
Sequence:
MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLGLEEVLSSRDCHPALPLPPGFHPHPGPNYPSFLPDQMQPQVPPLHYQGQSRGFVARAGEPCVCWPHFGTHGMMLTPPSSPLELMPPGSCMPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF
Protein: rRNA biogenesis protein RRP36 (Q38EB6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU368027}.
Interaction partners:
Sequence:
MPHNDPDGPPPERSARVRPRRQSGVPAVRPHRFVDPRFSDLYGAVDRKQFEDNYKFLREQEEEEQSRRKHCIQCLKYALRRHEREEVGQDEESEEEEDRFEEENRDEINRLMLRPPSDLKAELQQLKRESQLYISRTKDREVRARRQAVRKGIIKREAAAVRDGKKQRAFIPKRSQLKREVLAETFDKLEKKGGKGAVDKYVERKTKKRR
Protein: Proteasome subunit beta type-7-B (EC 3.4.25.1) (20S proteasome beta subunit B-2) (Proteasome component FC) (Proteasome subunit beta type-2) (Q7DLS1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-6-B
- Proteasome subunit beta type-1
- Proteasome subunit beta type-3-A
- Proteasome subunit alpha type-5-B
- Proteasome subunit alpha type-1-A
- Proteasome subunit alpha type-7-A
- Proteasome subunit beta type-2-B
Sequence:
MSQSSVDIPPKGGFSFDLCKRNDMLTQKGLKAPSFLKTGTTIVGLIFKDGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFSYQGHVSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIFNDLGSGSNVDICVITKGHKEYLRNYMEPNPRTYVSSKGYSFTKKTEVLLTKITPLLERVEIVEVAGEAMEE
Protein: EH domain-containing protein 2 (Q8BH64)
Organism: Mus musculus (Mouse)
Function: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane. Regulates the equilibrium between cell surface-associated and cell surface-dissociated caveolae by constraining caveolae at the cell membrane (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14676205}; Peripheral membrane protein {ECO:0000269|PubMed:14676205}; Cytoplasmic side {ECO:0000269|PubMed:14676205}. Membrane, caveola {ECO:0000269|PubMed:24508342}; Peripheral membrane protein {ECO:0000269|PubMed:24508342}; Cytoplasmic side {ECO:0000269|PubMed:24508342}. Endosome membrane {ECO:0000250|UniProtKB:Q4V8H8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4V8H8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q4V8H8}. Cytoplasm, cytosol {ECO:0000269|PubMed:14676205}. Note=Colocalizes with GLUT4 in intracellular tubulovesicular structures that are associated with cortical F-actin (PubMed:14676205). Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes (PubMed:18502764). {ECO:0000269|PubMed:14676205, ECO:0000269|PubMed:18502764}.
Interaction partners:
- EH domain-binding protein 1
- Clathrin heavy chain 1
- Clathrin light chain B
- AP-2 complex subunit alpha-1
- AP-2 complex subunit mu
- AP-2 complex subunit beta
- AP-2 complex subunit alpha-2
- Caveolae-associated protein 1
- AP-2 complex subunit sigma
- Dysferlin
Sequence:
MFSWLKKGGARGQRPEAIRTVTSSLKELYRTKLLPLEEHYRFGSFHSPALEDADFDGKPMVLVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCFVAVMHGETEGTVPGNALVVDPEKPFRKLNPFGNTFLNRFMCAQLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLNKADMVETQQLMRVYGALMWALGKVVGTPEVLRVYIGSFWSQPLLVPDNRRLFELEEQDLFRDIQGLPRHAALRKLNDLVKRARLVRVHAYIISYLKKEMPTVFGKENKKKQLILKLPVIFAKIQLEHHISPGDFPDCQKMQELLMAHDFTKFHSLKPKLLEALDDMLAQDIAKLMPLLRQEELESVEAGVQGGAFEGTRMGPFVERGPDEAIEDGEEGSEDDAEWVVTKDKSKYDEIFYNLAPADGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGHGLPTNLPRRLVPPSKRRQKGSAE
Protein: Ribosome-recycling factor, mitochondrial (RRF) (Ribosome-releasing factor, mitochondrial) (Q9D6S7)
Organism: Mus musculus (Mouse)
Function: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96E11}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein bL9m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL14
Sequence:
MASGIRCFRLLHPAFRSYHAALTRPVSEVSMKTVSGRQHGHRQYSAYPAVPVRHFATKKAKAKGKGQPQARVTVNRALVEDIISLEEVDEDMKSVVEALKDNFNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNMASFPECTAAAIKAIRESGMNLNPEVEGTLIRVPIPKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKKSKDKTSEDTIRLIEKQISQMADDTVAELDQHLAAKTKELLG
Protein: Verruculogen synthase (EC 1.14.11.38) (Fumitremorgin biosynthesis protein F) (B9WZX5)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Verruculogen synthase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Interaction partners:
Sequence:
MTVDSKPQLQRLAADADVDRMCRLLEEDGAFILKGLLPFDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVATTCPTFRNTILINPVIHAICEAYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHYQPLEAPPISLSVIFPLTEFTEENGATEVILGSHRWTEVGTPERDQAVLATMDPGDVLIVRQRVVHAGGGNRTTAGKPRRVVLAYFNSVQLTPFETYRTMPREMVESMTVLGQRMLGWRTMKPSDPNIVGINLIDDKRLENVLQLKAADSPA
Protein: FI18622p1 (Semaphorin 2b, isoform A) (Semaphorin 2b, isoform C) (A1ZAF5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPLNAQLKIAQSVNKVTYAKVSDSNCCAKKQQKYSIADFSQAKRQAGSMCATGKGKHRLCSLSALLLVLVAQTVHVEYARADYENTWNLYYEPPCCTGSSAAHHLRHHKEHVQDFSCGPLHYKTFYMDERNNALYVGAMDRIFRLNLRNISQSICERDVLILEPTGSDILNCVSKGKREVECRNHIRVIQPMNFNGQKLYVCGTNAHNPKDYVINANLTHLPRSQYVPGIGLGIGKCPYDPADNSTAVYVENGNPFGLPALYAGTNAEFTKADSVIFRSDLYNLTNGRKEANFKRTVKYDSKLLDKPNFVGSFEIGEFVYFFFREHAVEYINCGKAVYSRVARVCKNDRGGKYMISQNWATYLKARMNCSISSEFPFYFNEIQSVYKMPTDDTKFYATFTTNTNGLIGSAVCSYDIRDINAAFDGKFKEQATSNSAWLPVLNSKVPEPRPGTCHNDTATLPDSVLNFIRKHPLMDKAVDHEFGNPVFFKRDVILTKLVVDKIRIDKLNQEFLVYFVATTSGHIYKIVQFMHYGQRHSNLVDIFEASPHSEPIREMTLSHKTGSLYVATDHQVKQIDIAMCARRYDSCFRCVSDPYCGWDKDVNACRPYQLGLLQDVANETSGICDTSVLRKKVTSSYGQTLHLSCFVKMPEVLRKKQTRWYHHSTEKGRYEVRYTPTKYIDTNEGGLVLLAVNEGDGGRYDSYLDGTLLCSYGVTVDAHRCSPPSQKQDYQKIYSHWCNEFEKYKSAMKQWQAKQEQCGLKDKTGPISSNGKHVNDVFSNDALV
Protein: Fatty acyl-CoA reductase 2, chloroplastic (AtFAR2) (EC 1.2.1.84) (Fatty acid reductase 2) (Male sterility protein 2) (Q08891)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of fatty acyl-CoA and -ACP (acyl carrier protein) substrates to fatty alcohols. Triggers the accumulation of C16 and C18 fatty alcohols; converts palmitoyl-acyl carrier protein to the corresponding C16:0 alcohol with NAD(P)H as electron donor, but seems inactive toward palmitoyl- or other acyl-coenzyme A. Triggers also the formation of some C16:0 aldehydes. Involved in the synthesis of the lipid component in sporopollenin. Required for exine patterning of pollen grain by mediating the formation of pollen wall substances.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21813653}.
Interaction partners:
- Wax ester synthase/diacylglycerol acyltransferase 1
- Type III polyketide synthase B
- Type III polyketide synthase A
- Cytochrome P450 703A2
- Cytochrome P450 704B1
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Beta-glucosidase 20
- NAD
- Protein DETOXIFICATION 6
Sequence:
MEALFLSSSSSSIVASNKLTRLHNHCVWSTVIRDKKRFGPTWCRVGGGGDGGRNSNAERPIRVSSLLKDRGQVLIREQSSPAMDAETLVLSPNGNGRTIEINGVKTLMPFSGASMVGMKEGLGIISFLQGKKFLITGSTGFLAKVLIEKVLRMAPDVSKIYLLIKAKSKEAAIERLKNEVLDAELFNTLKETHGASYMSFMLTKLIPVTGNICDSNIGLQADSAEEIAKEVDVIINSAANTTFNERYDVALDINTRGPGNLMGFAKKCKKLKLFLQVSTAYVNGQRQGRIMEKPFSMGDCIATENFLEGNRKALDVDREMKLALEAARKGTQNQDEAQKMKDLGLERARSYGWQDTYVFTKAMGEMMINSTRGDVPVVIIRPSVIESTYKDPFPGWMEGNRMMDPIVLCYGKGQLTGFLVDPKGVLDVVPADMVVNATLAAIAKHGMAMSDPEPEINVYQIASSAINPLVFEDLAELLYNHYKTSPCMDSKGDPIMVRLMKLFNSVDDFSDHLWRDAQERSGLMSGMSSVDSKMMQKLKFICKKSVEQAKHLATIYEPYTFYGGRFDNSNTQRLMENMSEDEKREFGFDVGSINWTDYITNVHIPGLRRHVLKGRA
Protein: Truncated transposon Ty1-A Gag-Pol polyprotein (TY1B) (Transposon Ty1 TYB polyprotein) [Cleaved into: Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (O13527)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
METFTGYLKSTCFHQISPYPPSIMSIQVKVHANILILSFIECLRMPMHRQIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKLRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: HMG box domain-containing protein (Q57YV2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRRTLWYLLEKDEPIVIRRAVMAKARPHIGGGVTSNATSSTGGTVSTSMMTSDVLSRRNGFIGSEPRSIIDRISSPNGSSVPSTSSRRSALLPSEREGGKASGDASDDAYKFLLHHIDSEIAALKRRVTTVMDQRKNVEDSQNRRIRDLFECIERPWLLLASIPPPQLPNKALDVFAKEFYTRQNGTSTSGWEEDAIFLSTCKRNWRVLTTLQRKPYEIAARRNEQTRKELKKKMSNGCSYFEKLCEQTKEWTAEMVRDEMRKAVAAKTRSSPVASKSRASSVAKKPVARRQGANKTEPKAAASKKEDKIVEVLKFEPVAKKEPKGAAGRSARGRPLKGQIKKAAKGKAPVVAKKGKTSPRPVAAKLKKVKKK
Protein: Alcohol dehydrogenase class-P (AtADH) (EC 1.1.1.1) (P06525)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Alcohol dehydrogenase mostly active on ethanol (EtOH), but exhibits broad substrates selectivity for primary and secondary alcohols (e.g. butanol, propyl alcohol, pentanol, isopentanol, ethylene glycol, isopropanol, methanol and tertiary butyl alcohol). Converts allyl alcohol to highly toxic acryl-aldehyde. Required for survival and acclimation in hypoxic conditions, especially in roots.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:7851777}.
Interaction partners:
- Pyruvate decarboxylase 1
- Pyruvate decarboxylase 2
- Pyruvate decarboxylase 4
- Pyruvate decarboxylase 3
- Probable inactive linolenate hydroperoxide lyase
- S-formylglutathione hydrolase
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- (Z)-3-hexen-1-ol acetyltransferase
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Ethylene-responsive transcription factor RAP2-12
Sequence:
MSTTGQIIRCKAAVAWEAGKPLVIEEVEVAPPQKHEVRIKILFTSLCHTDVYFWEAKGQTPLFPRIFGHEAGGIVESVGEGVTDLQPGDHVLPIFTGECGECRHCHSEESNMCDLLRINTERGGMIHDGESRFSINGKPIYHFLGTSTFSEYTVVHSGQVAKINPDAPLDKVCIVSCGLSTGLGATLNVAKPKKGQSVAIFGLGAVGLGAAEGARIAGASRIIGVDFNSKRFDQAKEFGVTECVNPKDHDKPIQQVIAEMTDGGVDRSVECTGSVQAMIQAFECVHDGWGVAVLVGVPSKDDAFKTHPMNFLNERTLKGTFFGNYKPKTDIPGVVEKYMNKELELEKFITHTVPFSEINKAFDYMLKGESIRCIITMGA
Protein: Cyclin-dependent protein kinase inhibitor SMR6 (Protein SIAMESE-RELATED 6) (Q29Q81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle (By similarity). May inhibit CDKA-1/CYCD complexes during S-phase, preventing the re-initiation of DNA replication.
Interaction partners:
- Cyclin-dependent kinase A-1
- Cyclin-dependent protein kinase inhibitor SMR3
- Cyclin-dependent protein kinase inhibitor SMR11
- Cyclin-dependent protein kinase inhibitor SMR2
- Cyclin-dependent kinase D-1
- E2F transcription factor-like E2FF
- Protein SAMBA
Sequence:
MGFSKKSQFEGGLESDGKKWVIAGISIRASLKPVKTKLRAPPEIVTEVEEDCYNEEEECSTTPTAKETKIPELLECPPAPRKRRPALKCRSNVVREFFTPPSDLETVFLRRR
Protein: Interleukin-1 (A3DTN5)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
Sequence:
MAFVPDLDVLESSSLSEETFYGPSCLCLQKKPRLDSEHTAVGVQVTVRKGRGARSFRQAAVLVVAMTKLLRRPTRRDFADSDLSALLEEVFEPVTFQRLESSYAGAPAFRYTRSQSFDIFDINQKCFVLESPTQLVALHLQGPSSSQKVRLNIALYRPRGPRGSAGAGQTPVALGIKGYKLYMSCVLSGAEPTLQLEEADVTRDIDSAELTRFVFYRLDSPAEGTTRFESAAFPGWFICTSLQPRQPVGITNRPDQVNIATYKLSGR
Protein: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT) (P9WPA5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
Interaction partners:
- Dephospho-CoA kinase
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Pantothenate kinase
- RNA/DNA methyltransferase Rv2966c
- Type III pantothenate kinase
- Riboflavin biosynthesis protein
- Phosphoheptose isomerase
- Guanylate kinase
- 3,4-dihydroxy-2-butanone-4-phosphate synthase
- Dihydroneopterin aldolase
Sequence:
MTGAVCPGSFDPVTLGHVDIFERAAAQFDEVVVAILVNPAKTGMFDLDERIAMVKESTTHLPNLRVQVGHGLVVDFVRSCGMTAIVKGLRTGTDFEYELQMAQMNKHIAGVDTFFVATAPRYSFVSSSLAKEVAMLGGDVSELLPEPVNRRLRDRLNTERT
Protein: T-complex protein 1 subunit epsilon (TCP-1-epsilon) (CCT-epsilon) (P80316)
Organism: Mus musculus (Mouse)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48643}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P48643}.
Interaction partners:
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta-2
- Chaperonin containing TCP1 subunit 8-like 1
- Guanine nucleotide-binding protein subunit beta-5
Sequence:
MASVGTLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTITNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARIAIQHLDKISDKVLVDINNPEPLIQTAKTTLGSKVINSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVVDAKIAILTCPFEPPKPKTKHKLDVMSVEDYKALQKYEKEKFEEMIKQIKETGANLAICQWGFDDEANHLLLQNGLPAVRWVGGPEIELIAIATGGRIVPRFSELTSEKLGFAGVVQEISFGTTKDKMLVIEKCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKESNPALGIDCLHKGSNDMQYQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE
Protein: Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180) (Unsaturated glucuronyl hydrolase) (SpnUGL) (Q8DR77)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Function: Catalyzes the hydrolysis of unsaturated hyaluronate and chondroitin disaccharides. Also degrades unsaturated heparin disaccharides. Releases 4-deoxy-4,5-didehydro D-glucuronic acid or 4-deoxy-4,5-didehydro L-iduronic acid from chondroitin disaccharides, hyaluronan disaccharides and heparin disaccharides and cleaves both glycosidic (1->3) and (1->4) bonds. Prefers sulfated glycosaminoglycans compared to unsulfated glycosaminoglycans. Probably required for mammalian cells invasion through the degradation of extracellular sulfated glycosaminoglycans such as chondroitin and hyaluronan.
Interaction partners:
- 5-keto-D-gluconate 5-reductase
- 2-keto-3-deoxygluconate kinase
- Hyaluronate lyase
- Ribose-5-phosphate isomerase C-terminal domain-containing protein
- 2-keto-3-deoxy-6-phosphogluconate aldolase
- Phosphotransferase system sugar-specific EII component
- Phosphotransferase system sugar-specific EII component
- Uncharacterized protein
- Phosphotransferase system sugar-specific EII component
- Phosphotransferase system sugar-specific EII component
Sequence:
MIKKVTIEKIKSPERFLEVPLLTKEEVGQAIDKVIRQLELNLDYFKEDFPTPATFDNVYPIMDNTEWTNGFWTGELWLAYEYSQQDAFKNIAHKNVLSFLDRVNKRVELDHHDLGFLYTPSCMAEYKINGDGEAREATLKAADKLIERYQEKGGFIQAWGDLGKKEHYRLIIDCLLNIQLLFFAYQETGDQKYYDIAESHFYASANNVIRDDASSFHTFYFDPETGQPFKGVTRQGYSDDSCWARGQSWGVYGIPLTYRHLKDESCFDLFKGVTNYFLNRLPKDHVSYWDLIFNDGSDQSRDSSATAIAVCGIHEMLKHLPEVDADKDIYKHAMHAMLRSLIEHYANDQFTPGGTSLLHGVYSWHSGKGVDEGNIWGDYYYLEALIRFYKDWNLYW
Protein: Melatonin receptor MEL1B (Q8TEV7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
YHRIYRRWHTPLHICLIWLLTVVALLPNFFVGSLEYDPRIYSCTFIQTASTQYTAAVVVIHFLLPIAVVSFCYLRIWVLVLQARRKAKPESRLCLKPSDLRSFLTMFVVFVIFAICWAPLNCIGLA
Protein: Replication factor C, subunit 4, putative (Q383X4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Replication factor C, subunit 3, putative
- Replication factor C, subunit 2, putative
- Proliferating cell nuclear antigen
- Replication factor C, subunit 5, putative
- Checkpoint protein HUS1
- Chromosome transmission fidelity protein 18 homolog
- Replication factor C, subunit 1, putative
- DNA polymerase eta
- BRCT domain-containing protein
- AAA+ ATPase domain-containing protein
Sequence:
MTQQTVPWVEKYRPMSMEDIVGNADAVARLQVIAREGNLPNLLLCGPPGTGKTTSMLCLARSLLSDPDGGGSNNNALKDAVLELNASDDRGLDVVREKIKLFAQTKKTLPQRVGDSNNRKINLHKIVILDEADSMTPAAQQALRRTIELHSSTTRFAFACNNSHKIIEPIQSRCAVVRFRKLSHTDILRRLMYIIQQENVAYTDDGLEALLYLADGDLRSAVNALQATCSGYSLVNADNVFKVCDLPHPQLVEAILTSCVKQDLAAAHKEMQRLLGRGYATSDVISTFFRAAQNVKLFRDEKQQLQVLRIIGEVTMRVAEGVGTPLQLASMVCRIIVATKS
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (Q9NH11)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYYKLKTSFLEETLNDVLSEDGYDILEMSQASDLGVSMLDQDVSLNEGPQLPLDISALVGPQSSGNLEEIPQSVEGSFSNLIDLPNRQVLTNLVNRDENHVIRKFEAAEELPINQNAWGLNVSKKPPAPPQPVEASKSAPGHGKQPKAGASLKPSLSAKLFQSSRGFAKRNPRKPLSRCVSSSSSTTSLSSVPTDHHEELLDFETILIRKAQEYKEKQQAIANNPMLASEHSKESIKTLVDDGWLRRNTKENTLDEEVPFAEANNNSGTSKKTNFGLANLDLSKLKPTVKEEKVLQAKPDQMAIIQELQTDMNSSMNQKPDHLNHTPPASSQKSVAPKNKPPPSEQETDSDSDSVVAESEEEQEPQEYRQLSKRRKIVSTASGKVEVAAPVEIPNKVEPETETFAQENPDFSADEDQDATYVPENKKKDKAKRKQAAGKQKTTKPKAEPKPKTEKKAKVKAEKKPKAEKKPRNSKKAIAVEPAPDPEEDERQPLNPEDLKYVLALEAGDITSVPRINVQDLEEADATAQRYIRTFAAGPNPGLSEGSNIRVDEKRAAARKKLEERIAAGKLNENFVTINIQKKKFVRGKKSVNFSKYKKQQWRHKKRVAALSGPDMDMGGCDGGVLTCFQCGGVGHFAQQCKVKGDSLLPLSAQLEEDPSPFPTLAEAQEMASQGAVVAHSRNISRLPQAANAAILQGDELNESEEDDQESSEDEEVQQHPDPNWSSDEMDVDFEALDAAVEASLSQPVSQEKAASPIKTYVGHKIPEEFLKQAGLDTTASSSNRSQHGGVKPLYDLLPDGSVQDTTPEVLEALHMFGHTNFRKGQDRAIMRTLSGLSSLVTLSTGSGKSLCYQLPAYLYSRKVGAITLVISPLVSLMEDQVTGVPHFLRAHCLHTNQTAPQRMKIQQMIANGEIDILLVSPEAVVAGERATGFGAILRQLPPIAFACIDEAHCVSQWSHNFRPSYLMICKVLRKNLGVRTVLGLTATATLPTRVSIINHLGISDGERGIISDIPLPDNLVLSVSKDENRDAALLQLLNSERFEPCQSIIIYCTRRDECERIAGFIRTCVQDRREPTQDQTKKRKRVNWQAEPYHAGMPASRRRTVQKAFMSNELRIVVATIAFGMGINKPDIRAVIHYNMPRNFESYVQEIGRAGRDGLPSHCHLFLDAKGGDQSELRRHVYSNSIDRHVIRKLLQKIFVPCSCDKEASKRTALPIPLEGDGPRVHMCPGHEIGFSVEKTVEMLDIPAENISTLLCYMELDPRWCISVLSSAYVMAKVISYGGPKYLKHAAKECPPLAMAIALQIRDKTFKEDSNIIEFSVTDIAAGIGWNSGVVKYQLKDLEWVKVNGYPKRSPITVSFYDLGFRIKVPGDFTESEIDNALDTLYTRSVKQERTQLIQLQYVAHGLAAVAYSSCGQCCNADFPQDRGEQLKAIVRNYFANDYPQDLELEIEPSNVPDENIIDDVHALINMYPDNTFTGRNIARIFHGIMSPNYPAVIWGRCKFWRAHVKVDFNRILHLANMAIIKRRT