wanglab/gogpt-training-data huggingface dataset:
Protein: Protein bottleneck (P40794)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a regulator of the microfilament network governing cellularization of the embryo. Determines the timing of a key conformational transition in the cortical microfilament network: the proper coordination of membrane invagination and basal closure of the cells. To do this, bnk possibly physically links neighboring contractile units of the early cycle 14 microfilament network in a manner that prevents basal constriction until the proper stage has been reached. Bnk together with nullo and Sry-alpha may provide auxiliary functions, by acting both to stabilize a large and dynamic microfilament structure and regulate its functions.
Subcellular location: Cytoplasm, cytoskeleton. Note=Colocalizes with the structural transitions in the microfilament network during cellularization. Association is observed only when the network assumes an aligned and tightly apposed hexagonal configuration.
Interaction partners:
- Protein nullo
- Serendipity locus protein alpha
- Transcription factor Zelda
- Protein Z600
- RE03769p
Sequence:
MSISTFNFQFYNYKLSPSSPGFGSTASRSSSSCISELEMDIDEDMSAQPTITSTPKPRFTSQLAVELAKTEPGNGISPLRPKLHTAQKRWSMELREKVLEMSKRNNGQEKPQTARQQEQRQPQEQPLQQEELQHQQQEPTVTDKINFFNKLTNTFESGFSKLMPQASSTNNRFIAMLRTARPQNVATTTANSSTANSFLGSDHSLSGSVTGQVPPPKPKRLSATTAQFATPHVPAMGVGKGGSQRKCSLRRKPSMDKSRATISRQSSSASVRTQNHAIMEDLSLVVPVRLRIAEYEQRISMSA
Protein: Transcription factor E4F1 (EC 2.3.2.27) (E4F transcription factor 1) (Putative E3 ubiquitin-protein ligase E4F1) (RING-type E3 ubiquitin transferase E4F1) (Transcription factor E4F) (p120E4F) (p50E4F) (Q66K89)
Organism: Homo sapiens (Human)
Function: May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription.
Subcellular location: Nucleus, nucleoplasm. Cytoplasm. Note=A small fraction is detected in the cytoplasm. Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis. {ECO:0000250}.
Interaction partners:
- Cellular tumor antigen p53
- Ras association domain-containing protein 1
- Cyclin-dependent kinase inhibitor 2A
- GATOR2 complex protein WDR24
- Zinc finger CCCH-type with G patch domain-containing protein
- Integrator complex assembly factor BRAT1
- Telomere length regulation protein TEL2 homolog
- Leucine-rich repeat-containing protein 14
- Polycomb complex protein BMI-1
- Polycomb complex protein BMI-1
Sequence:
MEGAMAVRVTAAHTAEAQAEAGREAGEGAVAAVAAALAPSGFLGLPAPFSEEDEDDVHRCGRCQAEFTALEDFVQHKIQKACQRAPPEALPATPATTALLGQEVVPAAPGPEEPITVAHIVVEAASLAADISHASDLVGGGHIKEVIVAAEAELGDGEMAEAPGSPRQQGLGLAGEGEQAQVKLLVNKDGRYVCALCHKTFKTGSILKAHMVTHSSRKDHECKLCGASFRTKGSLIRHHRRHTDERPYKCSKCGKSFRESGALTRHLKSLTPCTEKIRFSVSKDVVVSKEDARAGSGAGAAGLGTATSSVTGEPIETSPVIHLVTDAKGTVIHEVHVQMQELSLGMKALAPEPPVSQELPCSSEGSRENLLHQAMQNSGIVLERAAGEEGALEPAPAAGSSPQPLAVAAPQLPVLEVQPLETQVASEASAVPRTHPCPQCSETFPTAATLEAHKRGHTGPRPFACAQCGKAFPKAYLLKKHQEVHVRERRFRCGDCGKLYKTIAHVRGHRRVHSDERPYPCPKCGKRYKTKNAQQVHFRTHLEEKPHVCQFCSRGFREKGSLVRHVRHHTGEKPFKCYKCGRGFAEHGTLNRHLRTKGGCLLEVEELLVSEDSPAAATTVLTEDPHTVLVEFSSVVADTQEYIIEATADDAETSEATEIIEGTQTEVDSHIMKVVQQIVHQASAGHQIIVQNVTMDEETALGPEAAAADTITIATPESLTEQVAMTLASAISEGTVLAARAGTSGTEQATVTMVSSEDIEILEHAGELVIASPEGQLEVQTVIV
Protein: KH domain-containing, RNA-binding, signal transduction-associated protein 3 (RNA-binding protein Etoile) (Sam68-like mammalian protein 2) (SLM-2) (Q9R226)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides (By similarity). Binds poly(A). RNA-binding abilities are down-regulated by tyrosine kinase PTK6. Involved in splice site selection of vascular endothelial growth factor (By similarity). In vitro regulates CD44 alternative splicing by direct binding to purine-rich exonic enhancer (By similarity). Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners such as neuroligins and LRRTM family members. High concentrations in forebrain structures block splicing inclusion of NRXN1-3 AS4 exons while low concentrations favor their inclusion. Targeted, cell-type specific splicing regulation of NRXN1 at AS4 is involved in neuronal glutamatergic synapse function and plasticity and is linked to behavioral aspects. Regulates expression of KHDRBS2/SLIM-1 in defined neuron populations in the hippocampus by modifying its alternative splicing resulting in a transcript predicted to undergo nonsense-mediated decay. Can bind FABP9 mRNA. May play a role as a negative regulator of cell growth. Inhibits cell proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:15471878}. Note=Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one.
Interaction partners:
- Protein-tyrosine kinase 6
- KH domain-containing, RNA-binding, signal transduction-associated protein 1
Sequence:
MEEKYLPELMAEKDSLDPSFTHALRLVNREIEKFQKGEGKEEEKYIDVVINKNMKLGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDLHVLIEVFAPPAEAYARMGHALEEIKKFLIPDYNDEIRQAQLQELTYLNGGSENADVPVVRGKSTLRTRGVTTPAITRGRGGVTARPVAVGVPRGTPTPRGVLSTRGPVSRGRGLLTPRARGVPPTGYRPPPPPPTQETYGEYDYDDGYGTAYDEQSYDSYDNSYSTPAQSAADYYDYGHGLSEDAYDSYGQEEWTNSRHKAPSARTAKGVYRDQPYGRY
Protein: Centrosomin's beautiful sister, isoform A (LD35238p) (Q7K4K7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Golgin-245
- Ras-related protein Rab6
- GRIP and coiled-coil domain containing 88 kDa
- FI04457p
- Ras-related protein Rab-30
- ADP-ribosylation factor-like protein 1
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 54
- FI19713p1
Sequence:
MFATLKNKIKEETGDDVVQSANQRYPGNNNNNYRLRSRRVSINSNSADDVGGGGFYNESEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKDIYCEEQEKIQNLQQIEIDKLKNLLSFREQESVDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEESRLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKLTEFERVQLEIIEKNKTIKTLNQRLIDLKKTVQKELRSAQISTDSESHPTTTPGHRISSSSLEAFSTGDKGNCVIMDEVNFQYLKHVIVKFLTSREVEARHLVRAVSTLLQLTTEEEKLLHDTLNWKMSWFGMKPT
Protein: Autophagy related 16 like 2 (H0YG45)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XAAPGSQDAFYPTRAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWKRPFSFKKRRGHSIGGAPEQRYQIIPVCVAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEANQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVCGDHIIISGHNDQKIRFWDSRGPHCTQVIPVQGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSDWTKAVFSPDRSYALAGSCDGALYIWDVDTGKLESRLQGPHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ
Protein: 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1) (O59713)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P40487}.
Interaction partners:
- 2-
- Diphthamide biosynthesis protein 3
- Diphthine--ammonia ligase
- Diphthamide biosynthesis protein 4
- Diphthine methyl ester synthase
- Diphthine methyltransferase
- Elongation factor 2
- Elongator complex protein 3
Sequence:
MAEVKKSIPKRRFVGKKNRKENNLDGSNRDVENAALVTINSKRSAGRVATQIPEDILNDKAINEAIKLLPQNYNFEIHKTIWHIRLRKAKRVALQLPEGLLMFGCILSDIFEQFCQVETIVMGDVTYGACCIDDFTARALDCDFLVHYGHSCLIPVDQTPIKVLYVFVDIKIDLQHVVSSLKHNLPSNSRLALVGTIQFVGSLNSIKDALQIQDEDGKGGFYVVIPQAKPLSPGEALGCTSPYIEKGSVDALIYIGDGRFHLESVMIANPDLPAYRYDPYSHKLSIESYAHEEMKSIRYSAVEKARTAKKFGLIQGTLGRQGSPKVLENLKNTLRKNNKDFVCVLMSEIFPSRLGQFSDIDAWIQVACPRLSIDWGYAFPAPLLTPYEASAAFNVVPWKEVYPMDFYATNSLGNWTPNNPENRPLPNRKKTGPVSS
Protein: Chemotaxis protein CheA (EC 2.7.13.3) (Q56310)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Chemotaxis protein CheW
- Methyl-accepting chemotaxis protein 4
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Methyl-accepting chemotaxis protein
- Chemotaxis protein CheY
- Methyl-accepting chemotaxis protein
- Methyl-accepting chemotaxis protein, putative
- Purine-binding chemotaxis protein
- Methyl-accepting chemotaxis protein 2
- Chemotaxis protein methyltransferase
Sequence:
MMEEYLGVFVDETKEYLQNLNDTLLELEKNPEDMELINEAFRALHTLKGMAGTMGFSSMAKLCHTLENILDKARNSEIKITSDLLDKIFAGVDMITRMVDKIVSEGSDDIGENIDVFSDTIKSFASSGKEKPSEIKNETETKGEEEHKGESTSNEEVVVLPEEVAHVLQEARNKGFKTFYIKVILKEGTQLKSARIYLVFHKLEELKCEVVRTIPSVEEIEEEKFENEVELFVISPVDLEKLSEALSSIADIERVIIKEVTAVTEESGAEKRTEKEEKTEKTEEKAERKKVISQTVRVDIEKLDNLMDLMGELVIARSRILETLKKYNIKELDESLSHLSRITLDLQNVVMKIRMVPISFVFNRFPRMVRDLAKKMNKEVNFIMRGEDTELDRTFVEEIGEPLLHLLRNAIDHGIEPKEERIAKGKPPIGTLILSARHEGNNVVIEVEDDGRGIDKEKIIRKAIEKGLIDESKAATLSDQEILNFLFVPGFSTKEKVSEVSGRGVGMDVVKNVVESLNGSISIESEKDKGTKVTIRLPLTLAIIQALLVKVNNLVYAIPIANIDTILSISKEDIQRVQDRDVIVIRGEVIPVYRLWEVLQIEHKEELEEMEAVIVRVGNRKYGIVVDDLLGQDDIVIKSLGKVFSEVKEFSGAAILGDGSIALIINVSGIV
Protein: GATA transcription factor 3 (AtGATA-3) (Q8L4M6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein JAGGED
Sequence:
MELWTEARALKASLRGESTISLKHHQVIVSEDLSRTSSLPEDFSVECFLDFSEGQKEEEEEVVSVSSSQEQEEQEHDCVFSSQPCIFDQLPSLPDEDVEELEWVSRVVDDCSSPEVSLLLTQTHKTKPSFSRIPVKPRTKRSRNSLTGSRVWPLVSTNHQHAATEQLRKKKQETVLVFQRRCSHCGTNNTPQWRTGPVGPKTLCNACGVRFKSGRLCPEYRPADSPTFSNEIHSNLHRKVLELRKSKELGEETGEASTKSDPVKFGSKW
Protein: T. brucei spp.-specific protein (Q583K5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRQHSPDGMAGKTRVSSITWEDELLLRGVRLDSDLVPHLQTTLSSPHNRSEHGATTPAGSSAILAMVNAGGSCTSSPRSEVRMKNVSPLRDLSAKLRGKDSAASTCDECGVGYSSDSGLSNTWVRYGPNAMSSPRVVVPSLLPLPQNITPPPRGGKDISHNCALPPLGAEGQKSSGRSTAPLSRTGHEQPGNSPAPKLSSSTIAIRDTEATLVLRTNTPLSCGRKEKKLSLGGTGKSCSNDGRSIATPSKTTIKRAMTPLSKQTTSTSCERSSSQGNGRRCESGRSSIQANGLQVLDPIGSRRDD
Protein: Gem-associated protein 2 (Gemin-2) (Component of gems 2) (Survival of motor neuron protein-interacting protein 1) (SMN-interacting protein 1) (O14893)
Organism: Homo sapiens (Human)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound.
Subcellular location: Nucleus, gem. Cytoplasm. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs. Also found in the cytoplasm.
Interaction partners:
- Gem-associated protein 5
- Gem-associated protein 6
- Small nuclear ribonucleoprotein E
- Serine-threonine kinase receptor-associated protein
- Gem-associated protein 7
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Probable ATP-dependent RNA helicase DDX20
- Survival motor neuron protein
- Gem-associated protein 4
Sequence:
MRRAELAGLKTMAWVPAESAVEELMPRLLPVEPCDLTEGFDPSVPPRTPQEYLRRVQIEAAQCPDVVVAQIDPKKLKRKQSVNISLSGCQPAPEGYSPTLQWQQQQVAQFSTVRQNVNKHRSHWKSQQLDSNVTMPKSEDEEGWKKFCLGEKLCADGAVGPATNESPGIDYVQIGFPPLLSIVSRMNQATVTSVLEYLSNWFGERDFTPELGRWLYALLACLEKPLLPEAHSLIRQLARRCSEVRLLVDSKDDERVPALNLLICLVSRYFDQRDLADEPS
Protein: Myosin light chain 12A (A0A8L2UJI1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSKRAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLGKNPTDEYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEAIGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD
Protein: Phosphatidyl-myo-inositol mannosyltransferase (EC 2.4.1.345) (Alpha-mannosyltransferase) (GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase) (Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase) (Phosphatidylinositol alpha-mannosyltransferase) (PI alpha-mannosyltransferase) (P9WMZ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). PimA plays an essential role for growth in macrophages and during both the acute and chronic phases of infection.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A0QWG6}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0QWG6}; Cytoplasmic side {ECO:0000250|UniProtKB:A0QWG6}.
Interaction partners:
- Phosphatidylinositol mannoside acyltransferase
- Probable conserved membrane protein
- Phosphatidylinositol phosphate synthase
- GDP-mannose-dependent alpha-
- AP-4-A phosphorylase
- Threonine--tRNA ligase
- 1,4-alpha-glucan branching enzyme GlgB
- Malto-oligosyltrehalose trehalohydrolase
Sequence:
MRIGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKKWLAHGDFDVLHLHEPNAPSLSMLALNIAEGPIVATFHTSTTKSLTLTVFQGILRPMHEKIVGRIAVSDLARRWQMEALGSDAVEIPNGVDVDSFASAARLDGYPRQGKTVLFLGRYDEPRKGMAVLLDALPKVVQRFPDVQLLIVGHGDADQLRGQAGRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPVDPPDLQAAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQIMRVYETVAGSGAKVQVAS
Protein: Kinesin-like protein KIF26A (Q9ULI4)
Organism: Homo sapiens (Human)
Function: Atypical kinesin that plays a key role in enteric neuron development. Acts by repressing a cell growth signaling pathway in the enteric nervous system development, possibly via its interaction with GRB2 that prevents GRB2-binding to SHC, thereby attenating the GDNF-Ret signaling. Binds to microtubules but lacks microtubule-based motility due to the absence of ATPase activity (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Growth factor receptor-bound protein 2
- Kinesin-associated protein 3
Sequence:
MVGRGVPLCAAQPAVAEGGPAREPPPLLEVSPRKRLPAGPDQDPCGSRPAPEGAGAGPEQGHSAGGGGWCRHCHTKLVELKRQAWKLVSGPGTTLRDPCLSALLLDKLPAPGALPACRPEAERRCDVCATHLQQLTREAMHLLQAPASHEDLDAPHGGPSLAPPSTTTSSRDTPGPAGPAGRQPGRAGPDRTKGLAWSPGPSVQVSVAPAGLGGALSTVTIQAQQCLEGMWSVSRVNSFLPPACLAEAAVAAVAVADTVRECPPVAGPDGLSKAWGRGGVCTSALVTPTPGSVGGSTGPSAAASFFIRAMQKLSLASKRKKPHPPPPPATRGTSTYPTDFSGVLQLWPPPAPPCLLRAASKTKDNPGSIGKVKVMLRIWPAQGAQRSAEAMSFLKVDPRKKQVILYDPAAGPPGSAGPRRAATAAVPKMFAFDAVFPQDSEQAEVCSGTVADVLQSVVSGADGCIFSFGHMSLGKSYTMIGKDSSPQSLGIVPCAISWLFRLIEERRERTGTRFSVRVSAVEVCGRDQSLRDLLAEVAPGSLQDTQSPGVYLREDPVCGAQLQNQSELRAPTAEKAAFYLDAALAARSTSRAGCGEDARRSSHMLFTLHVYQYRMEKCGRGGMSGGRSRLHLIDLGSCEAAAGRAGEAAGGPLCLSLSALGSVILALVNGAKHVPYRDHRLTMLLRESLATAGCRTTMIAHVSDAPAQHAETLSTVQLAARIHRLRRKKAKYASSSSGGESSCEEGRARRPPHLRPFHPRTVALDPDRTPPCLPGDPDYSSSSEQSCDTVIYVGPGGAALSDRELTDNEGPPDFVPIIPALSRHRPSKGPRDADHFRCSTFAELQERLECMDGNEGPSGGPGGTDGAQASPARGGRKPSPPEAASPRKAVGTPMAASTPRGSSGPDTHQGTPEPCKAIVWGDQREDSSAWPELLVPEKAAVSGGRRPLPSPAPPPPQLLEACRAPEEPGGGGTDGVARTPPVGMSGQVAGSPMLPGATCPRLAAGSRCPERGLLTTTVTLQRPVELNGEDELVFTVVEELSLGALAGAGRPTSLASFDSDCSLRALASGSRPVSIISSINDEFDAYTSQAPEGGPLEGAAWAGSSHGSSISSWLSEVSVCTADSRDPTPQPRFSPDSLAGLDPGGPPALDGSLGDGSSGFLGPDRPDSPGPTWGPCPGEVAAVAPSRPGREPQAGPSRWASAAQTIHSSLPRKPRTASATTRVGCARLGQSPPGRGGLFEDPWLLRVGECDTQAASAGRAPSPTLGSPRLPEAQVMLACAQRVVDGCEVAARAARRPEAVARIPPLRRGATTLGVTTPAVSWGDAPTEVVACSGSLKASPTSKKGLAPKAGFLPRPSGAAPPAPPTRKSSLEQRSSPASAPPHAVNPARVGAAAVLRGEEEPRPSSRADHSVPRATSSLKARASKVEAAHRLAGHASLERYEGLAHSSSKGREAPGRPPRAVPKLGVPPSSPTHGPAPACRSGAAKAVGAPKPPVGGGKGRGLVAGGSRALGPSVKLSTASVTGRSPGGPVAGPRAAPRAGPSVGAKAGRGTVMGTKQALRAAHSRVHELSASGAPGRGGSSWGSADSDSGHDSGVNVGEERPPTGPALPSPYSKVTAPRRPQRYSSGHGSDNSSVLSGELPPAMGRTALFHHSGGSSGYESLRRDSEATGSASSAPDSMSESGAASPGARTRSLKSPKKRATGLQRRRLIPAPLPDTTALGRKPSLPGQWVDLPPPLAGSLKEPFEIKVYEIDDVERLQRPRPTPREAPTQGLACVSTRLRLAERRQQRLREVQAKHKHLCEELAETQGRLMLEPGRWLEQFEVDPELEPESAEYLAALERATAALEQCVNLCKAHVMMVTCFDISVAASAAIPGPQEVDV
Protein: Formin like 1 (K7EJE6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
ELDMSDFEEQFKTKSQGPSLDLSALKSKAAQKAPSKATLIEANRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREQRPMEELSEEDRFMLCFSRIPRLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNSSKRGAAYGFRLQSLDALLEMKSTDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDDCMVLKEFLRANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYKKAEQEVEQWKKEAAAQEAGADTPGKGEPPAPKSPPKARRPQMDLISELKRRQQKEPLIYESDRDGAIEDIITGKGLARPWSYPQSVLLCFLLTQCAILWGTGCHTASCYLFCFSFLFPFSTPLHLPHPHSVIKTVPFTARTGKRTSRLLCEASLGEEMPL
Protein: Carbonic anhydrase 1 (EC 4.2.1.1) (Carbonate dehydratase 1) (P0ABE9)
Organism: Escherichia coli (strain K12)
Function: Reversible hydration of carbon dioxide. Carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (CynS) diffuses out of the cell faster than it would be hydrated to bicarbonate, so the apparent function of this enzyme is to catalyze the hydration of carbon dioxide and thus prevent depletion of cellular bicarbonate.
Interaction partners:
- Cyanate hydratase
- Carbonic anhydrase 2
- Cyanate transport protein CynX
- C4-dicarboxylic acid transporter DauA
- HTH-type transcriptional regulator CynR
Sequence:
MKEIIDGFLKFQREAFPKREALFKQLATQQSPRTLFISCSDSRLVPELVTQREPGDLFVIRNAGNIVPSYGPEPGGVSASVEYAVAALRVSDIVICGHSNCGAMTAIASCQCMDHMPAVSHWLRYADSARVVNEARPHSDLPSKAAAMVRENVIAQLANLQTHPSVRLALEEGRIALHGWVYDIESGSIAAFDGATRQFVPLAANPRVCAIPLRQPTAA
Protein: Tubby-like F-box protein 1 (AtTLP1) (Q9ZP59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AP-5 complex subunit beta-like protein
- Tetraspanin-13
- Peroxidase 6
- GDSL esterase/lipase At2g19050
- Geranylgeranyl transferase type-2 subunit alpha 1
- Proline transporter 3
- Phospholipid scramblase
- B3 domain-containing transcription factor NGA3
- Mannosyl-oligosaccharide glucosidase GCS1
- Glycine-rich RNA-binding protein 3, mitochondrial
Sequence:
MSFRSIVRDVRDSIGSLSRRSFDFKLSSLNKEGGKSRGSVQDSHEEQLVVTIQETPWANLPPELLRDVIKRLEESESVWPARRHVVACASVCRSWRDMCKEIVQSPELSGKITFPVSLKQPGPRDATMQCFIKRDKSNLTYHLYLCLSPALLVENGKFLLSAKRIRRTTYTEYVISMHADTISRSSNTYIGKIRSNFLGTKFIIYDTQPAYNSNIARAVQPVGLSRRFYSKRVSPKVPSGSYKIAQVSYELNVLGTRGPRRMHCAMNSIPASSLAEGGTVPGQPDIIVPRSILDESFRSITSSSSRKITYDYSNDFSSARFSDILGPLSEDQEVVLEEGKERNSPPLVLKNKPPRWHEQLQCWCLNFRGRVTVASVKNFQLIAANQPQPQPQPQPQPQPLTQPQPSGQTDGPDKIILQFGKVGKDMFTMDFRYPLSAFQAFAICLSSFDTKLACE
Protein: Amino acid transporter (M0QXM4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane {ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361216}.
Interaction partners:
Sequence:
MVSNNPLCVCLCRNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFARLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLMMKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAGLLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESVM
Protein: Aminopeptidase N (EC 3.4.11.2) (B4DP96)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTENSK
Protein: Pituitary homeobox homolog Ptx1 (D-PTX1) (O18400)
Organism: Drosophila melanogaster (Fruit fly)
Function: Appears to control physiological cell functions rather than pattern formation during embryogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138, ECO:0000269|PubMed:9431811}.
Interaction partners:
Sequence:
MDRSSAVGGCGGGGGLGVGVVTSSATALGPGGLTNGGGGVVSGALNGLEAMSAESTGLCLQDLVSAGTANGAGSAGSAESATTTSTALSSGSTGSSTVNGGGSSTSGTEHLHSHHSLHDSSSSVSISPAISSLMPISSLSHLHHSAGQDLVGGYSQHPHHTVVPPHTPKHEPLEKLRIWAETGDFRDSHSSMTAVANSLDSTHLNNFQTSSTSSISNRSRDRKDGNRSVNETTIKTENISSSGHDEPMTTSGEEPKNDKKNKRQRRQRTHFTSQQLQELEHTFSRNRYPDMSTREEIAMWTNLTEARVRVWFKNRRAKWRKRERNAMNAAVAAADFKSGFGTQFMQPFADDSLYSSYPYNNWTKVPSPLGTKPFPWPVNPLGSMVAGNHHQNSVNCFNTGASGVAVSMNNASMLPGSMGSSLSNTSNVGAVGAPCPYTTPANPYMYRSAAEPCMSSSMSSSIATLRLKAKQHASAGFGSPYSAPSPVSRSNSAGLSACQYTGVGVTDVV
Protein: Zeaxanthin 4-ketolase (EC 1.14.99.64) (Beta-carotene 4-ketolase) (CrBKT) (EC 1.14.99.63) (Q4VKB4)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Involved in the biosynthesis of ketocarotenoids which are powerful anti-oxidative molecules. Catalyzes the conversion of zeaxanthin to astaxanthin via adonixanthin. Catalyzes the conversion of beta-carotene to canthaxanthin via echinenone.
Interaction partners:
Sequence:
MGPGIQPTSARPCSRTKHSRFALLAAALTARRVKQFTKQFRSRRMAEDILKLWQRQYHLPREDSDKRTLRERVHLYRPPRSDLGGIAVAVTVIALWATLFVYGLWFVKLPWALKVGETATSWATIAAVFFSLEFLYTGLFITTHDAMHGTIALRNRRLNDFLGQLAISLYAWFDYSVLHRKHWEHHNHTGEPRVDPDFHRGNPNLAVWFAQFMVSYMTLSQFLKIAVWSNLLLLAGAPLANQLLFMTAAPILSAFRLFYYGTYVPHHPEKGHTGAMPWQVSRTSSASRLQSFLTCYHFDLHWEHHRWPYAPWWELPKCRQIARGAALAPGPLPVPAAAAATAATAAAAAAATGSPAPASRAGSASSASAAASGFGSGHSGSVAAQPLSSLPLLSEGVKGLVEGAMELVAGGSSSGGGGEGGKPGAGEHGLLQRQRQLAPVGVMA