wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 37 (EC 3.4.19.12) (Deubiquitinating enzyme 37) (Ubiquitin thioesterase 37) (Ubiquitin-specific-processing protease 37) (E7F6T8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of APC/C target proteins, thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex (By similarity).
Interaction partners:
- 26S proteasome regulatory subunit 8
- RuvB-like 1
- LYR motif-containing protein 4
- DnaJ
- Mortality factor 4-like protein 1
- F-box protein 28.
Sequence:
MAAAVPRLTSGGAVRIRIRCGELGTTKWREGVIEIQERDNKINLLVKFNSGGAPRVFQLSHNVKSVSWFQTHGPNRMTLTLKDSCIVMMDKLNMLVAKKMKEYLETVKLGKPAVFKTNQGSASFGLVLGNRTAQNDSGLSPSDKQSAPRRSSLDSREDSTPRKPLGSPSRVTSTPARGSLSEIRSEKRKRLMNSDGDLTEDYPKENDSSSNNKAITDSSRKFLLSCKDKLKQSEENRASAPHTPAPLQPTSFYGSRTGAKDYTQTHSFLDRPSSTGSCPSAKRSLVLPNHSTPFKKVRPTLDYGGWNKPRPSVLAQPQPPLQGFSNLGNTCYMNAILQSLFSLPSFSNDLLKQGIPWKRVPINALLRRFAHLLAKKDISPPEVKKDLLRRVKNAISSTAERFSGYMQNDAHEFLSQCLDQLKEDVEKINKSWKNEPSAWDEPQSTRLADEVDTSRIYTCPVTVNMEFEVQHTITCKSCGEVVLKREQFNDLSIDLPRRRKTLPMRSIQDSLDLFFRMEEIEYSCEKCSGKAATVSHKFSRLPRVLILHLKRYSYNTQLSLNSKLGQQVLIPKYLTLLSHCTDATRSPLSLGWSAQNALSRTLKISQSVNSSTLRRASQRPESSGSVLCDSDSDEELVRKVARKHHPDDDRADELQQHHPHAAVEQSEFNGINDEEMLAAVLEMSRHDTSLCAGPDEEPSSSPDTGFGDADAHDLTQHLELLDAEKQPTDALESLDLTMDENKENQTPDGLQGELDWVQQYSLEQEREEQELQQALAQSLQEQEAREMREDDDLKRATELSLQEFNNSLPELLCSDEDSGNEDGLDMEYSEAEAEELKKNAETGELPNSFRLISVVSHIGSSSSSGHYISDVYDMKKQSWLTYNDLDVSRTQESTVQRDRDRSGYIFFYMHKDVFEELSELEKAGVNTDGGRTVLQPL
Protein: 5,10-methylenetetrahydromethanopterin reductase (EC 1.5.98.2) (Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase) (Methylene-H(4)MPT reductase) (Q8TXY4)
Organism: Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Function: Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.
Subcellular location: Cytoplasm.
Interaction partners:
- Acetyl-CoA decarbonylase/synthase complex subunit beta
- Tetrahydromethanopterin S-methyltransferase subunit A
- F420-dependent methylenetetrahydromethanopterin dehydrogenase
- Coenzyme F420 hydrogenase subunit beta
- Coenzyme F420-reducing hydrogenase, beta subunit
- Tetrahydromethanopterin S-methyltransferase subunit H
- Coenzyme F420-reducing hydrogenase, gamma subunit
- Coenzyme F420-reducing hydrogenase, gamma subunit
- Ni,Fe-hydrogenase maturation factor
- Tetrahydromethanopterin S-methyltransferase subunit E
Sequence:
MAEVSFGIELLPDDKPTKIAHLIKVAEDNGFEYAWICDHYNNYSYMGVLTLAAVITSKIKLGPGITNPYTRHPLITASNIATLDWISGGRAIIGMGPGDKATFDKMGLPFPCKIPIWNPEAEDEVGPATAIREVKEVIYQYLEGGPVEYEGKYVKTGTADVNARSIQGSDIPFYMGAQGPIMLKTAGEIADGVLVNASNPKDFEVAVPKIEEGAKEAGRSLDEIDVAAYTCFSIDKDEDKAIEATKIVVAFIVMGSPDVVLERHGIDTEKAEQIAEAIGKGDFGTAIGLVDEDMIEAFSIAGDPDTVVDKIEELLKAGVTQVVVGSPIGPDKEKAIELVGQEVIPHFKE
Protein: MICOS complex subunit MIC13 homolog QIL1 (Q9VVH3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5XKP0}; Single-pass membrane protein {ECO:0000255}. Note=Enriched at crista junctions. {ECO:0000250|UniProtKB:Q5XKP0}.
Interaction partners:
- MICOS complex subunit
- Coiled-coil-helix-coiled-coil-helix domain containing 3
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- GH23780p
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Cytochrome c oxidase subunit 5B, isoform A
Sequence:
MVLGFLVRGGLVAATVYYTQKVGIWGDSDQTDKLYNDIKSELRPHVQKLEKQLPFEVPQLPKTGEMRFLAKHYYNEGVKNTFRFIHMLPCYAGRGLKKVKDTFQDFAQSPAIAGGAESSPPK
Protein: Enoyl-CoA hydratase EchA2 (Enoyl hydrase) (Unsaturated acyl-CoA hydratase) (Crotonase) (O07179)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable acyl-CoA dehydrogenase FadE23
- Probable acyl-CoA dehydrogenase FadE4
- Probable acyl-CoA dehydrogenase FadE1
- Probable acyl-CoA dehydrogenase FadE13
- Probable acyl-CoA dehydrogenase FadE2
- Possible acyl-CoA dehydrogenase FadE19
- Acyl-CoA dehydrogenase FadE7
- Probable fatty acid synthase Fas
- Conserved protein
- Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3
Sequence:
MPTPDFQTLLYTTAGPVATITLNRPEQLNTIVPPMPDEIEAAIGLAERDQDIKVIVLRGAGRAFSGGYDFGGGFQHWGDAMMTDGRWDPGKDFAMVTARETGPTQKFMAIWRASKPVIAQVHGWCVGGASDYALCADIVIASEDAVIGTPYSRMWGAYLTGMWLYRLSLAKVKWHSLTGRPLTGVQAAEAELINEAVPFERLEARVAEIATELARIPLSQLQAQKLIVNQAYENMGLASTQLLGGILDGLMRNTPDALEFIRTAQTQGVRAAVERRDGPFGDYSQAPPELRPDPTHVITPDGSM
Protein: Maternal gene required for meiosis, isoform F (Maternal gene required for meiosis, isoform G) (M9NEG1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSEHYCLRWNNYQSNLLGVFSQLLQDGSLVDVTLVCSEGTSIRAHKVVLSACSSYFQSLFLEHPEGHLIVILKDVRFAELQTLVEFMYKGEVNVQYCQLSALLKTAESLKVKGLAEMTNQNTTLREPEREPDRLRPQGGGGSGGSAHKAADSPAAALDATAATQAATATATATAAAATSTSTSATSAAATAAATAATSASTTATAAAGSSNTTTTTAATTTATCATAATSTAATSSSSSVTSAAAAAAAAASASGVAHSEEATSSSSSTGGQKREASDRSSPTPAKRSSRMHPADKVDVAEDREQEQNQADELLSEELLGRNLKDEEDDDVDELDENEETKLRGRDEDDDDEDEEEDTPMPLDLYQRPNVEPKSAAAATAAQQGGSNSLSGSSNACHTNSSSNSNNNNNNNNNSSSNNNNNTSSGKTSASSNGGTASSGGTADSVVAVDDDDDDDDGGHHHQRQVMDDRLEQDVDEEDLDDDVVVVGPATAMARGIAQRLAHQNLQRLHHTHHHAQHQHSQHHHPHSQHHHTPHHQQHHTHSDDEDAMPVIAKSEILDDDYDDEMDLEDDDEADNSSNDLGLNMKMGSGGAGGGGGVDLSTGSTLIPSPLITLPSSSAAAAAAAAAAMESQRSTPAMSAAQAAGAGASDLSIGGCGGRPASRSSRDGGGNDGGRGGASSSSLLSPGTVANLLPVQSVPLSLKKEIDCSEDDNSSHSRHMQQRSASAGGGLGGDLDYRASHESETSESPHQQQQPPPHAVGVGAGGGSAAAAAAAAAALLHQQQQQQPPHSPPPPPLHMFPCIYCRSAFPNQSKLTRHLLTHSLKTLEYREPTTTALLHSHLLGDLNMAAAGLPSPFAFQMNAAAMAATSGSDTQEQVAALAAAFGIDMEAALSLASTGCTFQSLTASCLEASSGGGSGGGGQGSLSRSATSAGNGGGLMLGSGSGSGSGAAAATGGSGSSGCGGGGGTATSGSLSPSTSAAAAAAAAAQSQSAALLGAASSDPNSVVMCKFCAKSFPDVTSLITHLSVHTGDRPFKCEFCGKAFKLRHHMKDHCRVHTGERPFRCNMCGKTFSRSTILKAHEKTHFPKYVRKFLSPSSPVDTKDELPQ
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A8I5ZTX5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGCAPSIHVSQSGVIYCRDSDESNSPRQTSSVSQGPTAPLHGLFVQTDAADAMPPSRAAGPPGAVRVRRSRAELGSGSSTGSSGPAATTCRGRRRHCCSSAEAETQTSYTSVKQVSSAEVRIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKKLCCTTDSSKQIHRIHRDSGDNSQTEPHSFRHKSRRKESIDVKSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLEILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHHSHSHLSMPITINDVPPSIAQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCTETTLRAWLQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPLAAESEGSDCECNPTGKNFPENQILIKRMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSNS
Protein: Tetratricopeptide repeat protein 8 (TPR repeat protein 8) (Bardet-Biedl syndrome 8 protein homolog) (Q8VD72)
Organism: Mus musculus (Mouse)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TAM2}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q8TAM2}. Cytoplasm {ECO:0000250|UniProtKB:Q8TAM2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q8TAM2}. Cell projection, cilium {ECO:0000269|PubMed:25243405}.
Interaction partners:
- BBSome complex member BBS2
- BBSome complex member BBS5
- BBSome complex member BBS1
- BBSome complex member BBS7
- BBSome complex member BBS4
- Protein PTHB1
- BBSome interacting protein 1
- Leucine zipper transcription factor-like protein 1
- ADP-ribosylation factor-like protein 6
- Chaperonin-containing T-complex member BBS12
Sequence:
MGSEMEPLLRAWSYFRRRKFQLCADLCTQMLEKSPYDQEPAPDLPVSQAAWILKARALTEMVYIDEIDVDQEGIAEMILDENAIAQVPRPGTSLKLPGTNQTGGPTQAVRPITQAGRPITGFLRPSTQSGRPGTMEQAIRTPRTAYTARPITSSSGRFVRLGTASMLTSPDGPFINLSRLNLTKYSQKPKLAKALFEYILHHENDVKMALDLASLSTEYSQYKDWWWKVQIGKCYYRLGMYREAEKQFKSALKQQEMVDTFLYLAKVYIILDQPVTALNLFKQGLDKFPGEVTLLCGIARIYEEMNNSSSAAEYYKEVLKQDNTHVEAIACIGSNHFYSDQPEVALRFYRRLLQMGVYNCQLFNNLGLCCFYAQQYDMTLTSFERALSLAENEEEAADVWYNLGHIAVGIGDTNLAHQCFRLALVHNNHHAEAYNNLAVLEMRKGHVEQARALLQTASSLAPHMYEPHFNFATVSDKIGDLQRSYVAAQKSEVAFPEHVDTQHLIKQLKQHFAML
Protein: V-type proton ATPase subunit a (D4A1H0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASVFRSEEMCLSQVFLQVEAAYCCVAELGELGLVQFKDLNANVNSFQRKFVNEVRRCESLERILRFLEDEMQNEIIIQVPDKDPGTPLPREMITLETTLEKLEGELQEANQSHQALKKSFLELTELKYLLKKTQDFFEVNLGFTAGVINRERMASFERLLWRVCRGNVYLKFSEMDTLLEDPVTKEEIKKNIFIIFYQGEQLRLKIKKICDGFRATIYPCPEHAAERREMLASVNVRLEDLITVITQTESHRQRLLQEAASNWHSWVIKVQKMKAVYHVLNMCNIDVTQQCIIAEIWFPVADTRHIKKALEQGMELSGSSMVPIMTEVETKTDPPTFNRTNKFTAGFQNIVDAYGVGSYREINPAPYTIITFPFLFAVMFGDCGHGMVMLMAALWMVLNERHLLAQKSTNEMWNIFFNGRYLILLMGIFSIYTGLIYNDCFSKSFNIFGSSWSVQPMFRNGTWNAHVVEQNPYLQLDPAIPGVYSGNPYPFGIDPIWNLASNKLTFLNSYKMKMSVILGIVHMIFGVILSLFNHIYFRRTLNIILQFIPEMIFMLSLFGYLVFMIIFKWCQYDAHTSQKAPSILIHFIGMFLFDYDDSSNAPLYGHQQEVQTFFVIIALVSVPWMLLIKPFILRAKHQKSQLQSFTIHEDAMEGPSVKKTAGAHGTKEGHEEEFNFGDIFVHQAIHTIEYCLGCISNTASYLRLWALSLAHAELSEVLWTMVMSIGLRLRGWGGLVGVFIIFAVFAVLTVAILLVMEGLSAFLHALRLHWVEFQNKFYEGAGFKFSPFSFKHVLEGAAEE
Protein: Chromo domain-containing protein LHP1 (Protein LIKE HETEROCHROMATIN PROTEIN 1) (Protein TERMINAL FLOWER 2) (Q946J8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Structural component of heterochromatin involved in gene repression, including several floral homeotic genes and FLT that regulates flowering time. Required for maintenance of vernalization-induced repression of FLC. As part of the PRC1-like complex, recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me), leading to epigenetic repression. PcG PRC1 complex maintains the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Transcriptional repressor that binds DNA on GAGA-like motif and 5'-(A/G/T)AACCCTA(A/G)-3' consensus motif in the promoters of target genes. Recognizes and binds histone H3 tails methylated at 'Lys-27' (H3K27me) but depleted in active histone marks such as H3K4me, leading to epigenetic repression. When in complex with LHP1, recognizes and binds histone H3 tails methylated at 'Lys-4' (H3K4me) and 'Lys-27' (H3K27me), mostly corresponding to stress-responsive genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:11731464, ECO:0000269|PubMed:12826620, ECO:0000269|PubMed:16244868, ECO:0000269|PubMed:16361394, ECO:0000269|PubMed:21304947}. Note=Punctuated distribution and in heterochromatic chromocenters.
Interaction partners:
- Putative E3 ubiquitin-protein ligase RING1a
- Protein EMBRYONIC FLOWER 1
- Histone-binding protein MSI1
- Putative E3 ubiquitin-protein ligase RING1b
- Histone H3.1
- Histone H3.3
- Histone H3-like 4
- Histone H3-like centromeric protein CENH3
- Histone H3-like 1
- Histone H3-like 3
Sequence:
MKGASGAVKKKPQVLNEAGEAETAVETVGESRKISGDGGFGSDDGGGGGGGGSGESILREIGDDRPTEDGDEEEEEDEDEDDGGDEEDEEGEGEGGQEERPKLDEGFYEIEAIRRKRVRKGKVQYLIKWRGWPETANTWEPLENLQSIADVIDAFEGSLKPGKPGRKRKRKYAGPHSQMKKKQRLTSTSHDATEKSDSSTSLNNSSLPDIPDPLDLSGSSLLNRDVEAKNAYVSNQVEANSGSVGMARQVRLIDNEKEYDPTLNELRGPVNNSNGAGCSQGGGIGSEGDNVRPNGLLKVYPKELDKNSRFIGAKRRKSGSVKRFKQDGSTSNNHTAPTDQNLTPDLTTLDSFGRIARMGNEYPGVMENCNLSQKTKIEELDITKILKPMSFTASVSDNVQEVLVTFLALRSDGKEALVDNRFLKAHNPHLLIEFYEQHLKYNRTP
Protein: PRA1 family protein A2 (AtPRA1.A2) (Q8GWC3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
Interaction partners:
- PRA1 family protein H
- PRA1 family protein G2
- PRA1 family protein C
- PRA1 family protein E
- PRA1 family protein G1
- PRA1 family protein B5
- PRA1 family protein F3
- PRA1 family protein B1
- PRA1 family protein B2
- PRA1 family protein B4
Sequence:
MDWDNVAAEDVIEALREVEWSTPPRSFGEFFSRFAFPRSFSKWKSRLKCNLYYYRTNYFILVIFVLGLALVTRPLALVGAALTALSIAFLNDSFAASFNEKFIRTIRHFSPHMAAKMRPPHMPVIRGRSTARKTVYVCGKPRWVFVITFLTASLVMWFSSCGLLWVLYALLTSLAVIIVHASIRTPNLKARLNTFREEFRAVWRNYSEL
Protein: Serine/threonine-protein phosphatase alpha-3 isoform (EC 3.1.3.16) (Q05547)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- LD24014p
- FI19335p1
- WD repeat-containing protein 82
- Protein phosphatase 1 regulatory subunit
- Cleavage and polyadenylation specificity factor 73
- Nuclear inhibitor of protein phosphatase 1
- Cleavage and polyadenylation specificity factor subunit 1
- Glycogen-binding subunit 76A
- Probable cleavage and polyadenylation specificity factor subunit 2
Sequence:
MAEVLNLESIISRLLEVRGARPGKNVQLSEGEIRGLCLKSREILLAQPILLELEAPLKICGDIHGQYYDLLRLFEYGGYPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYSENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVVAIVDEKIFCCHGGLSPDLTSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDTIGWGENDRGVSFTFGAEVVVKFLQKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDNTLMCSFQILKPVEKRKK
Protein: N-terminal EF-hand calcium-binding protein 1 (EF-hand calcium-binding protein 1) (Neuronal calcium-binding protein 1) (Q8N987)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- N-terminal EF-hand calcium-binding protein 3
- N-terminal EF-hand calcium-binding protein 2
Sequence:
MEDSQETSPSSNNSSEELSSALHLSKGMSIFLDILRRADKNDDGKLSFEEFKAYFADGVLSGEELHELFHTIDTHNTNNLDTEELCEYFSQHLGEYENVLAALEDLNLSILKAMGKTKKDYQEASNLEQFVTRFLLKETLNQLQSLQNSLECAMETTEEQTRQERQGPAKPEVLSIQWPGKRSSRRVQRHNSFSPNSPQFNVSGPGLLEEDNQWMTQINRLQKLIDRLEKKDLKLEPPEEEIIEGNTKSHIMLVQRQMSVIEEDLEEFQLALKHYVESASSQSGCLRISIQKLSNESRYMIYEFWENSSVWNSHLQTNYSKTFQRSNVDFLETPELTSTMLVPASWWILNN
Protein: Probable nonspecific lipid-transfer protein (O06144)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Probable fatty oxidation protein FadB
- Conserved protein
- Probable histone acetyltransferase Rv0428c
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Probable enoyl-CoA hydratase EchA5
- Trk system potassium uptake protein TrkA
- Conserved protein
- Probable enoyl-CoA hydratase EchA15
- Probable enoyl-CoA hydratase EchA3
Sequence:
MRMSAPEPVYILGAGMHPWGKWGNDFTEYGVVAARAALRDAGVDWRHVQLVAGADTIRNGYPGFVAGATFAQKLGWTGVPVSSSYAACASGSQALQSARAQILAGFCDVALVIGADTTPKGFFAPVGGERKGDPDWQRFHLIGATNTVYFALLARRRMDLYGATVEDFAQVKVKNSRHGLDNPNARYRKENSIDDVLASPVVSDPLRLLDICATSDGAAALIVASKSFTEKHLGSVAGVPSVRAISTVTPKYPQHLPELPDIATDSTAAVPAPERVFKDQILDAAYAEAGIGPEDLSLAEVYDLSTALELDWYEHLGLCPKGEAEALLRSGATTLGGRVPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQATGRQVADAKVGVTANQGLFGHGSSVIVAR
Protein: Biofilm regulator BssS (P0AB33)
Organism: Escherichia coli (strain K12)
Function: Represses biofilm formation in M9C glu and LB glu media but not in M9C and LB media. Seems to act as a global regulator of several genes involved in catabolite repression and stress response and regulation of the uptake and export of signaling pathways. Could be involved the regulation of indole as well as uptake and export of AI-2 through a cAMP-dependent pathway.
Interaction partners:
- Biofilm regulator BssR
- 4,5-DOPA dioxygenase extradiol
Sequence:
MEKNNEVIQTHPLVGWDISTVDSYDALMLRLHYQTPNKSEQEGTEVGQTLWLTTDVARQFISILEAGIAKIESGDFQVNEYRRH
Protein: Aminotransferase-like plant mobile domain-containing protein (Q38A62)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRYSTGIENIPSLFDLASALTGFIADFTQVVFGNTQTSFTAAALEETDRGNYDPVARSWEGTGGLNYRVPLYPIPSERHTRERTRNIKILMDNCRRICVEDELPSTKEELQFWTAYRFMKYQMYLTPTCVIMPPLYVMWRMFHDRIPRPFRGRTIPVTLSLALAEQWADATYPGHQFLSTALRAKTPMGDAARAEWLRLQPIDIPYYIYAAYQFQHFFGNVPKEILFGGDIAGYCS
Protein: Long-chain acyl-CoA thioesterase FadM (EC 3.1.2.-) (Acyl-CoA thioester hydrolase) (Thioesterase 3) (Thioesterase III) (P77712)
Organism: Escherichia coli (strain K12)
Function: Long-chain acyl-CoA thioesterase that could be involved in beta-oxidation of fatty acids. Is most active with 3,5-tetradecadienoyl-CoA, a metabolite of oleic acid that is hydrolyzed during oleate beta-oxidation, but can also use other substrates such as 3,5-dodecadienoyl-CoA, 9-cis-octadecenoyl-CoA, octadecanoyl-CoA, hexadecanoyl-CoA, 3-hydroxytetradecanoyl-CoA and tetradecanoyl-CoA.
Interaction partners:
- Fatty acid oxidation complex subunit alpha
- Acyl-CoA thioesterase 2
- Acyl-CoA thioester hydrolase YciA
- 2,4-dienoyl-CoA reductase [
- Thioesterase 1/protease 1/lysophospholipase L1
- Uncharacterized protein YbaV
- Acyl-coenzyme A dehydrogenase
- Long-chain-fatty-acid--CoA ligase
- 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
- 3-ketoacyl-CoA thiolase FadA
Sequence:
MQTQIKVRGYHLDVYQHVNNARYLEFLEEARWDGLENSDSFQWMTAHNIAFVVVNININYRRPAVLSDLLTITSQLQQLNGKSGILSQVITLEPEGQVVADALITFVCIDLKTQKALALEGELREKLEQMVK
Protein: 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase (EC 2.1.1.258) (5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase) (MeTr) (Q46389)
Organism: Moorella thermoacetica (Clostridium thermoaceticum)
Function: Methyltransferase that mediates the transfer of a N5-methyl group of (6S)-methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein (AcsC/AcsD) in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation.
Interaction partners:
Sequence:
MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAVQDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNAEREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEFGLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSNVSQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTVYCDSFVKMFKTR
Protein: Glutathione S-transferase (C8V321)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Maleylacetoacetate isomerase
Sequence:
MSQPVYHYLALGRLGRGEVLNLFLKDAGIATKDVLYPYDESWPATSEKLTQQGLTRTGLLPALEYNGEIYTQHIPTLRFLARELGAYDGETSHEKYIVDAVADTYIDWRSQWVASLKGATDEYKNSVVPKYYRILGQYYSERPGPYLLGEKITYVDFAVYQSIDNERRTGTLPETLPESLVKLQDAIEARPNIKEYIAEHK
Protein: IP16036p (Z band alternatively spliced PDZ-motif protein 66, isoform K) (Q058U1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSPKLHEFAVVLLRDGQATPWGIRLVGGNDLDTPLIITRVQVGSPAHGELLRGDIISKIGEYDARDLSHADAQQLFRGAGNEIRLVVHRDNKIAYTQGATQEAGPGSRSNSTLPPVTPDLMPHRGPSPFLPGPSHFERALQLPVDTLPQTVFPQLNSSGGYEVPSTVFSPKPTRDHQQDVDEEQAAIVNQPYRTTPLVLPGAKVKKDAPTTESYLRHYPNPAVRAHPGHDYHDSIMKQRVADTMLHKVVGSEADTGRVFHKQFNSPIGLYSNNNIEDTIRSTVPYKKTVQYDPRNSETYRAIQEEGGYSNYGQSSPQEVTIPVQTKVYQPNRLVPGKKPVSAPVSRPPYNVVNTHDENIRQSGSFNRLMYSVIGATEY
Protein: Std1p (A0A1D8PKV5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MFGSPFTNNPTQKSSTPTVFKDNARNAIYKQLPVVTSNTASSIRSAPSQFLNNRHHVSSHRSMSSSSSIFSSITGGKRSVRSAPSIYSSSTATIPEDSEPVSTTVEQLVNDIVLHENHYRAVALENNHRNANVDVEEMYKISLGSDLQYQNVPESLIDWNLNVTRCKLILTQLPQITSTDIPYNQNALPQLVGDLAGVCHIILIQPHISDKELIYTLLSSNLYKEHDLDVNFKKSVAEISVKQSRLLQINNGAGSSSINPEHLFLKFKFKEIAIRNYLINLAAAATTAHEYKLKMEHLKGVLKMEQPDKKVKLSKEDKKVLWEQVRSDVFQRAGL
Protein: Probable RNA-binding protein 19 (RNA-binding motif protein 19) (Q9Y4C8)
Organism: Homo sapiens (Human)
Function: Plays a role in embryo pre-implantation development.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16027046}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In discrete foci distributed throughout the cytoplasm and nucleoplasm during the 4 to 8 cell stages and the morula stage, but not in the periphery of the nucleolar precursor body (NPB). During blastocyst development, becomes increasingly localized to the nucleolus and less to the cytoplasm. At the late blastocyst stage, localized predominantly in the nucleolus. Localized in the nucleolus during interphase and to the perichromosomal sheath during mitosis. Does not colocalize in the cytoplasm with GW182 in P-bodies. May translocate to the nucleolus upon early embryonic development (By similarity). Colocalizes with NPM1 during interphase. By late prophase, metaphase, anaphase and telophase, associates with the chromosome periphery. By telophase localizes to NPB. {ECO:0000250}.
Interaction partners:
- Ribosome biogenesis protein BMS1 homolog
- U3 small nucleolar ribonucleoprotein protein IMP4
- Protein AATF
- Protein RRP5 homolog
- Probable ATP-dependent RNA helicase DDX10
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Surfeit locus protein 6
- Nucleolar protein 10
- RRP12-like protein
- Pescadillo homolog
Sequence:
MSRLIVKNLPNGMKEERFRQLFAAFGTLTDCSLKFTKDGKFRKFGFIGFKSEEEAQKAQKHFNKSFIDTSRITVEFCKSFGDPAKPRAWSKHAQKPSQPKQPPKDSTTPEIKKDEKKKKVAGQLEKLKEDTEFQEFLSVHQRRAQAATWANDGLDAEPSKGKSKPASDYLNFDSDSGQESEEEGAGEDLEEEASLEPKAAVQKELSDMDYLKSKMVKAGSSSSSEEEESEDEAVHCDEGSEAEEEDSSATPVLQERDSKGAGQEQGMPAGKKRPPEARAETEKPANQKEPTTCHTVKLRGAPFNVTEKNVMEFLAPLKPVAIRIVRNAHGNKTGYIFVDFSNEEEVKQALKCNREYMGGRYIEVFREKNVPTTKGAPKNTTKSWQGRILGENEEEEDLAESGRLFVRNLPYTSTEEDLEKLFSKYGPLSELHYPIDSLTKKPKGFAFITFMFPEHAVKAYSEVDGQVFQGRMLHVLPSTIKKEASEDASALGSSSYKKKKEAQDKANSASSHNWNTLFMGPNAVADAIAQKYNATKSQVFDHETKGSVAVRVALGETQLVQEVRRFLIDNGVSLDSFSQAAAERSKTVILVKNLPAGTLAAQLQETFGHFGSLGRVLLPEGGITAIVEFLEPLEARKAFRHLAYSKFHHVPLYLEWAPVGVFSSTAPQKKKLQDTPSEPMEKDPAEPETVPDGETPEDENPTEEGADNSSAKMEEEEEEEEEEEESLPGCTLFIKNLNFDTTEEKLKEVFSKVGTVKSCSISKKKNKAGVLLSMGFGFVEYRKPEQAQKALKQLQGHVVDGHKLEVRISERATKPAVTLARKKQVPRKQTTSKILVRNIPFQAHSREIRELFSTFGELKTVRLPKKMTGTGTHRGFGFVDFLTKQDAKRAFNALCHSTHLYGRRLVLEWADSEVTLQALRRKTAAHFHEPPKKKRSVVLDEILEQLEGSDSDSEEQTLQL
Protein: Epididymis secretory protein Li 117 (V9HW50)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICHTDDHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTVLTF