wanglab/gogpt-training-data huggingface dataset:
Protein: Very long chain fatty acid elongase 6 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL6) (ELOVL fatty acid elongase 6) (ELOVL FA elongase 6) (Elongation of very long chain fatty acids protein 6) (Fatty acid elongase 2) (hELO2) (Fatty acyl-CoA elongase) (Long-chain fatty-acyl elongase) (Very long chain 3-ketoacyl-CoA synthase 6) (Very long chain 3-oxoacyl-CoA synthase 6) (Q9H5J4)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03206}.
Interaction partners:
- Stearoyl-CoA desaturase
- Very-long-chain enoyl-CoA reductase
- Stearoyl-CoA desaturase 5
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Sterol regulatory element-binding protein 1
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Sterol regulatory element-binding protein 2
Sequence:
MNMSVLTLQEYEFEKQFNENEAIQWMQENWKKSFLFSALYAAFIFGGRHLMNKRAKFELRKPLVLWSLTLAVFSIFGALRTGAYMVYILMTKGLKQSVCDQGFYNGPVSKFWAYAFVLSKAPELGDTIFIILRKQKLIFLHWYHHITVLLYSWYSYKDMVAGGGWFMTMNYGVHAVMYSYYALRAAGFRVSRKFAMFITLSQITQMLMGCVVNYLVFCWMQHDQCHSHFQNIFWSSLMYLSYLVLFCHFFFEAYIGKMRKTTKAE
Protein: Probable monoacyl phosphatidylinositol tetramannoside-binding protein LpqW (A0R2I8)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: May directly or indirectly regulate the accessibility of the key branch point intermediate, monoacyl phosphatidylinositol tetramannoside (AcPIM4), to the elongating alpha-1,6 mannosyltransferases which could regulate the lipoarabinomannans (LAMs) biosynthesis.
Interaction partners:
- Probable alpha-
- Lipoprotein LpqB
- DUF402 domain-containing protein
- Uncharacterized protein
- Probable conserved transmembrane protein
- 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
- Alpha/beta hydrolase family protein
- Uncharacterized protein
- Probable exported protein
- Trehalose monomycolate transport factor A
Sequence:
MGVPTPARRARLTFGALLAVPTLLLGGCTVSPPPAPQSTETTETTPPPPPKAPTQIIMAIDSIGPGFNPHLLSDQSPVNAAIASLVLPSSFRPVPDPTSPTGSRWELDTTLLESAEVTNENPFTVTYKIRPEAQWTDNAPIAADDYWYLWRQMVSQPGVVDPAGYDLITGVQSVEGGKQAVVTFSQPYPAWRELFNDILPAHIVKDIPGGFGAGLARAMPVTGGQFRVETIDPQRDEILLARNDRFWSVPAKPDLVLFRRGGAPAALADSIRNGDTQVAQVHGGAATFAQLSAIPDVRTARIVTPRVMQLTLRAQQPKLADPQVRKAILGLIDVDLLASVGAGDDNTVTLAQAQVRSPSDPGYVPTAPPAMTRDDALELLRDAGYVSEPVPPPDNTADDPPPDNGRERIVKDGVPLTIVLGVASNDPTSVAVANTAADQLRNVGIDASVLALDPVALYGDALVNNRVDAVVGWRQAGGDLATVLASRYGCRALEATPVATAVPGPATTTSQAPTTTTTTTPPATTTPTPTAPIPAPESGELVQAPSNITGICDRSIQPRIDAALDGTDDIADVIQAVEPRLWNMATVLPILQDTTIVAAGPSVQNVSLTGAVPVGIVGDAGDWTKTK
Protein: lactoylglutathione lyase (EC 4.4.1.5) (Glyoxalase I) (O04818)
Organism: Sporobolus stapfianus (Ressurection grass)
Interaction partners:
Sequence:
MASGSDAVLEWHKQDKKRMLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGYGPEDKNFALELTYNYGVDKYDIGEGFGHFAIATEDINKIAEAVKSSGCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGDLERSIKFYEKALGMRLLRKKDVPDYKYTIAMLGYDDEDKTTVIELTYNYGVTEYSKGNAYAQVAIGTNDVYKSAEAVELATKELGGKILKQPGPLPGINTKIASFVDPDGWKVVLVDHADFLKELK
Protein: ATP-dependent RNA helicase FAL1 (EC 3.6.4.13) (Translation initiation factor four A-like protein 1) (Q12099)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9372960}.
Interaction partners:
- Probable ATP-dependent RNA helicase DHR2
- Suppressor of glycerol defect protein 1
- U3 small nucleolar ribonucleoprotein protein LCP5
- Protein PXR1
- Nonsense-mediated mRNA decay protein 3
- RNA annealing protein YRA1
- Pre-mRNA-splicing factor CWC22
- Pre-mRNA-splicing factor SNU114
- ATP-dependent RNA helicase SUB2
- RNA-binding protein SGN1
Sequence:
MSFDREEDQKLKFKTSKKLKVSSTFESMNLKDDLLRGIYSYGFEAPSSIQSRAITQIISGKDVIAQAQSGTGKTATFTIGLLQAIDLRKKDLQALILSPTRELASQIGQVVKNLGDYMNVNAFAITGGKTLKDDLKKMQKHGCQAVSGTPGRVLDMIKKQMLQTRNVQMLVLDEADELLSETLGFKQQIYDIFAKLPKNCQVVVVSATMNKDILEVTRKFMNDPVKILVKRDEISLEGIKQYVVNVDKEEWKFDTLCDIYDSLTITQCVIFCNTKKKVDWLSQRLIQSNFAVVSMHGDMKQEERDKVMNDFRTGHSRVLISTDVWARGIDVQQVSLVINYDLPEIIENYIHRIGRSGRFGRKGVAINFITKADLAKLREIEKFYSIKINPMPANFAELS
Protein: Major facilitator superfamily protein (O23203)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGHARTRTGIISVAFKFFRSLFPRHHRTNSMKIKTGTFLGVSISLILINLAAIMERADENLLPSVYKEVSEAFNAGPSDLGYLTFVRNFVQGLASPLAGVLVITYDRPIVLAIGTFCWALSTAAVGASSYFIQVALWRAVNGFGLAIVIPALQSFIADSYKDGARGAGFGMLNLIGTIGGIGGGVVATVMAGSEFWGIPGWRCAFIMMAALSAVIGLLVFLFVVDPRKNIEREELMAHKMNSNSVWNDSLAAAKSVVKVSTFQIIVAQGIIGSFPWTAMVFFTMWFELIGFDHNQTAALLGVFATGGAIGTLMGGIIADKMSRIYPNSGRVMCAQFSAFMGIPFSIILLKVIPQSTSSYSIFSITLFLMGLTITWCGSAVNAPMFAEVVPPRHRTMIYAFDRAFEGSFSSFAAPLVGILSEKLFGYDSRGIDPLKGSSVREADALSKGLLSMMAVPFGLCCLCYTPLHFVFQKDRENAKIASSKETEMI
Protein: ABC transporter G family member 5 (ABC transporter ABCG.5) (Q54TV2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MVKQDPRDKSSYSPNLSIPINNQEEPTLNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNNNNNNIKHKDEENDFEDSIYQIAKEHEGEEDDEYFPIPLDELMPNHENDELTKKIKQTRPEDKTGLYVYCRNATYTVKHRENKKVKIKLLDDVSFFLRPKQMTLILGTPGCGKSTIFQMLAGQLKDKHFEGELLFNGHPINHKNHHRDISYVTQDDIHVPTLTVKETFRFALDCLGKKELTREEKQVSVDNCMKLLGLKHAENTLVGDNFIRGISGGQKKRVTIGVGVIKGSNLLLMDEPTSGLDSSTSFEILSDVKKFVTYGYSPALITLLQPSVQLTSLFDNLMIMSKGKICYFGPMNRALGYFKKLGFACPSHNNPAEFFQEVVDAPERYSFIHPPKCKTSDDFVKAYRESDIYLELMEKMDANKDGIVDDNKPKVLVDSTAKELGMYPHGIGYQTKICLKRGFIMISRNYYNFATRVFKGIFFGLLLGTLYWRIGHNQSGGMERFGLLFFIMTTIIFSSFAAVNSFFGERKVFYSQKALHYYKTGAYFISSIICDIPAGLIEVAFFGPIVYWLANLRPVFIRFVYFMILLFITDNLSLSFAKMCAAISPTIEIANVTASVILSIWLLFSGFTAPKNDIGGWWIWLYYISPYTWIFQGLSINEFTYQAYGCKDSELIPPRTPQNLLPYPEGFGGNQVCQYTSGEQIMDAFGINNPDYFKWIVYAILGAYIVFFYSVCFFALKYLNFEDKKSKLAVKKLKKKKKVIVCKEDEEPNCKVTTEALERVSDDNDDNADISNYDDDTVIDMKSPLTSPNYNNNNNLSGSGNNIKRRKVKTPSTLSPMVNSPLTNLSPMVNTPSKNGNHSKQKPISTSQKDISSETGSYLQFKKLCYAVDVKADDPDNPKKKKSQRLQLLTDIDGYVKPGQMLALMGPSGAGKSTLLDVLAQRKTGGHITGEILINGKPPSEFTNRIRAYVEQMDVLPPTQTVREAIAFSARCRLPPEVTKEEREIFVDKIVEVLSLSSIKDLKIGVLGNGLSVSQRKRVNIGVELASNPEILFLDEPTSGLDSGDAFKVIDVVNKIAKVMNRTVICTVHQPSAAIFEFFDQLLLLKKGGETIYFGPLGNQSSVILDYCDKLGMHIKPHINPADFVMTLADEGKMVEGPNGEQEHLDAKKAYFESNICKKEYEIMEGQLIPDDFVVKTYDSRFASSWMTQFRALCMRSWLSRLRRPAIFVSNCLRSILLAVLLGTLFVRMDYEQKDARSRVSLLFFSFLFAGMVAIGNIPTTVLERGVFYREVTAGFYHSTAYMISYVLTSYPFILSTGILYIIPTFWIAGLDSGRHSSKFWYCLFIFIITYIMYDAFALCLAVCLPNEVMASTICGIGLSLATLFGGFVIARPNYPSAYYWCHYLDWLRYPLEASCTNEFTGLTFVCTNNKGAVPIPIIENGVQIAIKYYCPITNGDDFMLTYGFHKFMRYIDIAAIFGYIFIFVGLSFWGFKKVRWLNR
Protein: Signal recognition particle subunit SRP54 (EC 3.6.5.4) (Signal recognition particle 54 kDa protein) (Q75K18)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component srpra to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit srpra. SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (By similarity). Requires the presence of srp9/srp14 and/or srp19 to stably interact with RNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P61011}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61011}.
Interaction partners:
- Signal recognition particle subunit SRP68
- Signal recognition particle 14 kDa protein
- Signal recognition particle 19 kDa protein homolog
- Signal recognition particle subunit SRP72
- Signal recognition particle receptor subunit alpha
- Signal recognition particle 9 kDa protein
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein eS30
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL18
Sequence:
MVLADLGNQLSSALRSLNETTIVNEDTINQLLKEVGNALSKSDVSMSLIIQMRKNIKDKIKLDQMAAGLNKRKIIKQVVFDELIRLLDPGVPLWKPTKGKSNIVMFVGLQGAGKTTSVTKLAYFYKKKGFSTAIVCADTFRAGAFDQVRHNAAKAKIHYYGSETEKDPVVVARTGVDIFKKDGTEIIIVDTSGRHKQDSELFEEMKQIETAVKPDNCIFVMDSSIGQAAYEQATAFRSSVKVGSIIITKMDGNSMGGGAISAVAATNTPIIFIGTGEHLTDLELFDPSTFVSKLLGYGDMKGMLEKIKEVIPEDSTSLKEIAQGKFTLRSMQQQFQQIMQLGPIDKLVQMIPGMNQLPQLQGNEGGLKLKAYINILDSLSEKELDGKKPITQKRIITIAQGSGRHPNEVVELLEQHKTFEKLIGKGGPGGGLGSLMAGKGGPKNMEQAMKQMNANGGMQGLMNSLKGMGGMGDLAKMFGGGGGGGGGMPSMGDLAKMMGGMGGGGRGGGGMPNMGDLAKMMGGMGGGAGKGGQNGFPNLDLD
Protein: ATP-binding cassette, sub-family B (MDR\/TAP), member 3 (Antigen peptide transporter 2a) (Q801W2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRKVLVFACMLCFDILIVLILDLAETLLKSPTSSLDYNLFRQWAESGLRCTLLYAGSTLSKDAADPLIRRWITVHCFIGSVYETGRLAMFNNYRLDKFTVWLVGTVAAALACLFWEITLPDTNEESNGKERKQKARVLFIRVIRLYRPDYILLFGAFVFLALAVLCEMFIPLYTGEVIDILGSHYQWDNFRSAIIFMGLFSLGSSFSAGCRGGLFMCAINSFTCRVKVQLFGSLIRQDIGFFETIKTGDITSRLSTDTTLMGRAVALNVNVLLRTLVKTLGMLYLMVSLSWKLTLLMLMETPLTGLLQNIYDTHYQKLSKEVQDSMAQANDAAGEAVSGIRTVKSFKTELGEAHRYDGRLMETHNLKTRRDTVRAIYLLIRRMTELGMKVAMLYYGRLFIQYGQMSTGNLVSFILYQQDLGDNIRTLIYIFGDMLNSVGAAGKVFEYQDRKSEVSIDGNLMPKDLKGHVKFQKLTFSYPRRPDHNVLKDFSLELKPGQITALVGMSGGGKSTCVSLLERFYQPQQGTILLDGKPLQDYQHKYLHSKVAMVGQEPVLFSGTVRDNIAYGLQGCSMERVKEAASKANAHSFISKLEKGYDTDVGERGNLLSGGEKQRIAIARALIREPQVLILDEVTSSLDTESEQMVQQALSCCPTQTLLVIAHRLKTIERADQIVVIDSGELVEKGTHEELMEKKGSYYKLRERLFSDDKTTKQEKEKSDTVKTQ
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (V9HWC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Protein: Mushroom body defect, isoform J (M9NEG4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDTRSWRKVLLQWIGECHFIESNYITLEQSDLDSFFSVFIQKIQETENVKGKNELQDQPTEQSPLVQEFLAHNYPEFIAQQDDKEVDLPLDCLYVYTLLLHYSCVKKPSLFFHNICNKLPELTQTCIASFFRETVDRLLTREYLSQAIANVAVVYRQGVSTSVSPCLPSSSLSPDPRSDDAPCPSTPSSSSSQPSSSTPQLRNHREQLRLNGCEMPPPSTPKTELLEQRTKELRGIRTQLEVVRYEKALLEEQQMEKDELIKVLNKEKMMAKMELEKLRNVKLTEEHHDNESHHIMPYEFEHMKGCLLKEIGLKESLIAEITDKLHDLRVENSELSEKLNLAGKRLLEYTDRIRFLESRVDDLTRIVSSRDVMISSLESDKQELDKCLKEARDDLHNRIEVLNASSDLLDCSLSPNTTPENLASSVIDKQLREKEHENAELKEKLLNLNNSQRELCQALSSFLQKHNIDHEFPVEWTSSSLLSTISAIESKFVNTLEKSTQMKKECDVQSVCVEKLLEKCKLLSVSLGCQPKELDGFEATIPEAMESGFESSRECETILSCCHMKVVDIASKNNDLELDNERLNDKCAELKSIIDRGDQHLADINLQLIEKEKQIKDVGAEIQELRKRNINLENMLSQIADKEASAASHAQHLKQCGELLRAKYEVCRNELIAKNAAQDELVRMMMVPDGETLNGRVRQLIDLEMMHDEHNKMYAQMLKQLNELSAKHDNMTHSHLDFVKRTEIELETKNAQIMAFDEHNNHFDRFLTRIFTLLRSRNCPKSTTMGSATNFLESMHIEKRFENIEMLIEGQLLSADDLKRELDDLRSKNEELAKQNINGIIKRNKFITSLEVNTEKVKQYITDLEEEAFKRKQKVVQLENTLSKEQSNAKEMAQRLDIAQQEIKDYHVEAIRFINTIRDRLQQDFNGVNTPQQLGTCMTEFLKMYDQMEVRYEESSSLVEKLTESQAKLEMQVAELQVELENKDTNQHSGALIKQLNDTIQNLEKVNAKLSEDNTVSHTVHSKLNESLLKAQKELDLRAKIIENLEASERNLSMKLCELKDLKNKLKSSDEKIAQIKETYEEQIKALQAKCDMEAKKNEHLERNQNQSLTQLKEDALENCVLMSTKLEELQAKLQEGQQLVDSQKLELDMNRKELALVKSAYEAQTKLSDDLQRQKESGQQLVDNLKVELEKERKELAHVNSAIGAQTKLSDDLECQKESGQQLVDNLKVELEKERKELAQVKSVIEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAKVKSVIEAQTKLSDDLQRQKESAQQLEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKMELDKERKELAQVKSAIGAQTKLSDDLECQKESVQQLVDNLKVELEKERKELAKVNSAFEAQTKLSDDLKLQKEDAQREVFLVKERLVKEKREFEVKLATLEDIIETLEMRCTQMEEERATAYEQINKLENRCQEKDNVKSSQLQVETFKVECLHHQLKSEMATHNSLVEDLNRKLAEKVSKLDFVQSRLMTEIAEHNQVKDQLAQITDIPKVVELQHRLEAETAEREEAQNKLAVVTGRLDEITRELDNARLEHGAQILRMEETAREVGNKNAELCELIEFYRNRVEALERLLLASNQELEELNSIQSNQAEGVRDLGDTYSAAEGRQTESDQDKERYQKLALDCKILQAKYRDAKDEIKRCEKKIKDQRLEMEGKLEKMKNKMRSLYTAEVTRMKEKQERDAAKSASELEALTAQNAKYEEHTRKLSNQIVRLNEKILEQQKQHAIISTNLRHLQMQPISETKPSSTTLTVSSSSSAPNDDWQPFKRPNVPSSNLAMEDEEGEVFNNTYLTDLKLGRVPADMTAEELIYRNSLQPPHLKSTYAAQYDLGSQDEDLKDGPHSLDDSMSALLSSSSTGTRKKSMGTHYKRPGPPTPSKNGGRLSFGSSEPPREILREFGDHNNTSKTPARFKFLTQRFSVGSSGLPRDENSPPKRRLSNMFKRK
Protein: Bile acid-sensitive ion channel (BASIC) (Acid-sensing ion channel subunit family member 5) (Amiloride-sensitive cation channel 5, intestinal) (Human intestine Na(+) channel) (HINaC) (Q9NY37)
Organism: Homo sapiens (Human)
Function: Cation channel that gives rise to very low constitutive currents in the absence of activation. The activated channel exhibits selectivity for sodium, and is inhibited by amiloride.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9R0W5}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:10767424}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acid-sensing ion channel 4
- Acid-sensing ion channel 3
Sequence:
MEQTEKSKVYAENGLLEKIKLCLSKKPLPSPTERKKFDHDFAISTSFHGIHNIVQNRSKIRRVLWLVVVLGSVSLVTWQIYIRLLNYFTWPTTTSIEVQYVEKMEFPAVTFCNLNRFQTDAVAKFGVIFFLWHIVSKVLHLQEITANSTGSREATDFAASHQNFSIVEFIRNKGFYLNNSTLLDCEFFGKPCSPKDFAHVFTEYGNCFTFNHGETLQAKRKVSVSGRGLSLLFNVNQEAFTDNPALGFVDAGIIFVIHSPKKVPQFDGLGLLSPVGMHARVTIRQVKTVHQEYPWGECNPNIKLQNFSSYSTSGCLKECKAQHIKKQCGCVPFLLPGYGIECDLQKYFSCVSPVLDHIEFKDLCTVGTHNSSCPVSCEEIEYPATISYSSFPSQKALKYLSKKLNQSRKYIRENLVKIEINYSDLNYKITQQQKAVSVSELLADLGGQLGLFCGASLITIIEIIEYLFTNFYWICIFFLLKISEMTQWTPPPQNHLGNKNRIEEC
Protein: Xyloglucan-specific endo-beta-1,4-glucanase A (EC 3.2.1.151) (Xyloglucanase A) (Xyloglucanendohydrolase A) (Q5BG78)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components. Active against tamarind xyloglucan.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKLLALSLASLASAATITRRADFCGQWDTATAGNFIVYNNLWGQDNADSGSQCTGVDSANGNSVSWHTTWSWSGGSSSVKSYANAAYQFTATQLSSLSSIPSTWEWQYSTTDVVANVAYDLFTSSSIGGDSEYEIMIWLAALGGAGPISSTGSSIATVTLGGVTWNLYSGPNGSMQVYSFVASSTTESFSADLMDFINYLVENQGLSNSQYLTHVQAGTEPFTGSDATLTVSSYSVSVS
Protein: N-acetylmuramic acid/N-acetylglucosamine kinase (MurNAc/GlcNAc kinase) (EC 2.7.1.-) (EC 2.7.1.59) (Murein sugar kinase) (Q97ML3)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. May have a role in the rescue of the murein sugars GlcNAc and MurNAc released from muropeptides during cell wall turnover in C.acetobutylicum.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:21784936}.
Interaction partners:
- N-acetylmuramic acid 6-phosphate etherase
- Uncharacterized membrane protein, YBBC B.subtilis ortholog
- beta-N-acetylhexosaminidase
- Similar to beta-lactamase
- Predicted acetyltransferase
- Multimeric flavodoxin WrbA fused to cytochrome c-like domain
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1
- N-acetylglucosamine-6-phosphate deacetylase
- Glutamine--fructose-6-phosphate aminotransferase
Sequence:
MKYVIGIDGGGSKTHMKISTLDYKVLLEVFKGPSNINSSTKEEVKRVLQELIMEGLGKLGQSLEECSAICIGTAGADRTEDKSIIEDMIRSLGYMGKIIVVNDAEIALAGGIEKREGIIVISGTGSICYGRNKEGRSARSGGWGHIIGDEGSGYDIGIKAIKAALKSFDKRGEKTILEGDILDFLKLKSHEDLINYIYRSGVTKKEIASLTRVVNSAYIKGDLVSKRILKEAARELFLSVKAVVEVLSMQNKKVVLTTAGGVINNINYLYDEFRKFLNLNYPKVKIISMKNDSAFGAVIIARSECD
Protein: Partitioning defective 6 alpha (Partitioning defective 6 homolog alpha) (A6YIE1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSRNHRTTLKNEESVVEVKSKFEGEYRRFALKKNTGGFQEFYQLLQTIHRIPGVDVLLGYADIHGDLLPINNDYNFHKALSSANPLLRIIVQKRVVDDTVPFPTGSLQRRKKGPGGLRQAQPKSRPPLIGLPQDFRQISSIIDVDILPETHLRVRLHKHGTHKPLGFYIRDGVSVRVTSHGVEKFPGIFISRLVKGGLADTTGLLGVNDEILEVNGIDVSGKSLDQVTDMMVANSHNLIVTVKPAIYRSLDDTYRTFKTSAGNSSAGSRGSALSHDSAHSPASQNTSQYSNSNSVAEGDSDDDTDLIIENDNLSTYAQNRLTNGNGSHGNAQSSGAFAHRPLPQSVSLPSSSSLSSLTTPTHNGSPTKTSSSQESMREDGNFITL
Protein: Galactose-1-phosphate uridylyltransferase (Gal-1-P uridylyltransferase) (EC 2.7.7.12) (UDP-glucose--hexose-1-phosphate uridylyltransferase) (P09148)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Galactokinase
- UDP-glucose 4-epimerase
- Aldose 1-epimerase
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- UDP-galactopyranose mutase
- UDP-glucose 6-dehydrogenase
- Phosphoglucomutase
Sequence:
MTQFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQVLPAHDPDCFLCAGNVRVTGDKNPDYTGTYVFTNDFAALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAEREDRLQKEYFAEQKSPMLVDYVQRELADGSRTVVETEHWLAVVPYWAAWPFETLLLPKAHVLRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHFRESGV
Protein: Peptide methionine sulfoxide reductase (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (P40029)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product.
Interaction partners:
- Peptide methionine sulfoxide reductase 2
- Thioredoxin-2
- Free methionine-R-sulfoxide reductase
- Kinesin-like protein KIP3
- Glutathione peroxidase-like peroxiredoxin HYR1
- Thioredoxin-1
- DNA polymerase gamma
- Peroxiredoxin DOT5
- Peroxiredoxin TSA1
- Glutaredoxin-2
Sequence:
MSSLISKTIKYDPAKDKLITLACGCFWGTEHMYRKYLNDRIVDCKVGYANGEESKKDSPSSVSYKRVCGGDTDFAEVLQVSYNPKVITLRELTDFFFRIHDPTTSNSQGPDKGTQYRSGLFAHSDADLKELAKIKEEWQPKWGNKIATVIEPIKNFYDAEEYHQLYLDKNPQGYACPTHYLREM
Protein: Kelch domain-containing protein 3 (Testis intracellular mediator protein) (Q9BQ90)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(KLHDC3) complex specifically recognizes proteins with a glycine (Gly) at the C-terminus, leading to their ubiquitination and degradation: recognizes the C-terminal -Arg-(Xaa)n-Arg-Gly, -Arg-(Xaa)n-Lys-Gly, and -Arg-(Xaa)n-Gln-Gly degrons. The CRL2(KLHDC3) complex mediates ubiquitination and degradation of truncated SELENOV and SEPHS2 selenoproteins produced by failed UGA/Sec decoding, which end with a glycine. May be involved in meiotic recombination process.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12606021}.
Interaction partners:
- Cullin-2
- Elongin-B
- E3 ubiquitin-protein ligase RBX1
- Amyloid protein-binding protein 2
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
- Male-enhanced antigen 1
- PRAME family member 6
- Protein fem-1 homolog C
- Protein zer-1 homolog
- demerged
Sequence:
MLRWTVHLEGGPRRVNHAAVAVGHRVYSFGGYCSGEDYETLRQIDVHIFNAVSLRWTKLPPVKSAIRGQAPVVPYMRYGHSTVLIDDTVLLWGGRNDTEGACNVLYAFDVNTHKWFTPRVSGTVPGARDGHSACVLGKIMYIFGGYEQQADCFSNDIHKLDTSTMTWTLICTKGSPARWRDFHSATMLGSHMYVFGGRADRFGPFHSNNEIYCNRIRVFDTRTEAWLDCPPTPVLPEGRRSHSAFGYNGELYIFGGYNARLNRHFHDLWKFNPVSFTWKKIEPKGKGPCPRRRQCCCIVGDKIVLFGGTSPSPEEGLGDEFDLIDHSDLHILDFSPSLKTLCKLAVIQYNLDQSCLPHDIRWELNAMTTNSNISRPIVSSHG
Protein: Zinc finger protein ZAT9 (Q9M202)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may be involved in stress responses.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MESYKCRVCFKSFVNGKALGGHMRSHMSNSHEEEQRPSQLSYETESDVSSSDPKFAFTSSVLLEDGESESESSRNVINLTRKRSKRTRKLDSFVTKKVKTSQLGYKPESDQEPPHSSASDTTTEEDLAFCLMMLSRDKWKKNKSNKEVVEEIETEEESEGYNKINRATTKGRYKCETCGKVFKSYQALGGHRASHKKNRVSNNKTEQRSETEYDNVVVVAKRIHECPICLRVFASGQALGGHKRSHGVGNLSVNQQRRVHRNESVKQRMIDLNLPAPTEEDEVSVVFQ
Protein: Cysteine desulfurase IscS (EC 2.8.1.7) (P0A6B9)
Organism: Escherichia coli O157:H7
Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis (biotin, thiamine, molybdopterin). Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine, then delivers the sulfur to an acceptor protein such as CyaY, IscU, IscX, MoaD/MoeB, ThiI, or TusA. Transfers sulfur to acceptor proteins via a transpersulfidation reaction; the flexibility of the persulfide sulfur-carrying Cys-328 allows it to reach different partners docked on the homodimer surface. May function as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305}.
Interaction partners:
- Iron-sulfur cluster assembly scaffold protein IscU
- Sulfur carrier protein TusA
- Iron-sulfur cluster assembly scaffold protein IscU
- Sulfur carrier protein TusA
- tRNA sulfurtransferase
- HTH-type transcriptional regulator IscR
- Iron-sulfur cluster assembly protein CyaY
- HTH-type transcriptional regulator IscR
- 2Fe-2S ferredoxin
- 2Fe-2S ferredoxin
Sequence:
MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH