wanglab/gogpt-training-data huggingface dataset:
Protein: HotDog ACOT-type domain-containing protein (Q580L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Succinyl-CoA:3-ketoacid-coenzyme A transferase
- Acetyl-coenzyme A synthetase
- Enoyl-CoA hydratase/Enoyl-CoA isomerase/3-hydroxyacyl-CoA dehydrogenase, putative
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
Sequence:
MLRRCFTPSHLIPFLCGGCLSSRRQLVVGNSKNGTKPVASVDWTDLVGKELWSENRLAAGELLAMMDLCAKRVSEVYLSSMKPRVSCSTVGVSTTTFYSPVLHGDVVRMHGRLIYCGSSSMGIHIRFYRRSPSTITESLTGESYFTMVAIDENLRAVKTVPAVELTDENDVSYHNGYLAARNIAAEAKKISSDLQKKSITCSDVECTVNAAKPIRVPIASTRTSAHRIFLLYHLNNNRTIFGGELMRWMERHAVHCGRMFTGNRHISTVAMHNVEFHHPVFGTDWVTLEADIIYVHNTTMEVDVKLVVERDGHVVTTNRASFVLINLNEIGQKTIIPKGLDLSAATEEELLRFAEAKERYRRSRNSRR
Protein: Aquaporin-1 (AQP-1) (Aquaporin-CHIP) (Water channel protein CHIP29) (P47865)
Organism: Bos taurus (Bovine)
Function: Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P29972}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P29972}.
Interaction partners:
- Aquaporin 10
- Aquaporin-11
- Aquaporin
- Aquaporin-3
- Ammonium transporter Rh type A
- Aquaporin-3
- von Willebrand factor
- Aquaporin-3
- Anion exchange protein
Sequence:
MASEFKKKLFWRAVVAEFLAMILFIFISIGSALGFHYPIKSNQTTGAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISVLRAIMYIIAQCVGAIVATAILSGITSSLPDNSLGLNALAPGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSGPLAIGFSVALGHLLAIDYTGCGINPARSFGSSVITHNFQDHWIFWVGPFIGAALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK
Protein: Glucosamine-6-phosphate deaminase (EC 3.5.99.6) (GlcN6P deaminase) (GNPDA) (Glucosamine-6-phosphate isomerase) (O30564)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Interaction partners:
- N-acetylglucosamine-6-phosphate deacetylase
- Pts system, iibc components
- Glucose-6-phosphate isomerase
- mannose-6-phosphate isomerase
- Glucose-6-phosphate 1-dehydrogenase
- beta-N-acetylhexosaminidase
- Pts system, maltose and glucose-specific iiabc component
Sequence:
MRLIIRPTYEDISKWAANHVAQKINEFSPTKENPFILGLPTGSSPIGMYKNLIELNKNKKISFQNVITFNMDEYIGIEENHPESYHSFMWNNFFSHIDIKKENINILNGNASNLKKECEEYEKKIKSFGGIMLFVGGIGPDGHIAFNEPGSSLTSRTRIKTLTQDTIIANSRFFEGDVNKVPKNALTVGIGTIMDSQEVLIIVNGHNKARALKHAIEKGVNHMWTISALQLHKNAIIVSDKNATYELKVGTVEYFNDIERKNFNNDLK
Protein: N-alpha-acetyltransferase 38, NatC auxiliary subunit (I3L310)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRIRMTDGRTLVGCFLCTDRDCNVILGSAQEFLKPSGQCPGNAHPPDSFSAGEPRVLGLAMVPGHHIVSIEVQRESLTGPPYL
Protein: Uncharacterized protein C354.04 (O43018)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C13G6.13
Sequence:
MSENPAHKDLDSLQVDEKAKSWIAEKVEEELRRLESVGAKAIPLDVKNYSVMLDEDTDTVVNRIELMTSFDFDHVQQILLSAVQPYPYDKNLMFVYLVILTPLPHPMLIPYLFAPKVVGKNLLPRADGLVENTLKRWTFINDKLKRSDTVVREFQEIEEEATK
Protein: Uncharacterized protein (A5VK67)
Organism: Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri)
Interaction partners:
Sequence:
MKVTKLIVGIIMIVLAIIIFVQSIVRGFGNPNPAIHIYARTAELIVSLLYLASGIVYIATCGIDGLGGDIAGLSMMLISWVLGLLTCTIYLPLQLWAWLALIIGVGFFVWHIMLRRE
Protein: Leucine-rich repeat-containing protein 4 (Netrin-G2 ligand) (NGL-2) (Q45R42)
Organism: Rattus norvegicus (Rat)
Function: Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays an important role for auditory synaptic responses. Involved in the suppression of glioma.
Subcellular location: Membrane {ECO:0000269|PubMed:16980967}; Single-pass type I membrane protein {ECO:0000269|PubMed:16980967}. Postsynaptic cell membrane {ECO:0000269|PubMed:16980967}. Note=LRRC4 and DLG4 are interdependent for synaptic localization. {ECO:0000250}.
Interaction partners:
- Netrin G2
- Netrin-G1
- Adhesion G protein-coupled receptor L3
- Disks large homolog 4
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
Sequence:
MKLLWQVTVHHTWNAVLLPVVYLTAQVWILCAAIAAAASAGPQNCPSVCSCSNQFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNAIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGELKKLEYISEGAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLREYIPTNSTCCGRCHAPMHMRGRYLVEVDQASFQCSAPFIMDAPRDLNISEDRMAELKCRTPPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSRVLLIDTGVYTCMVTNVAGNSNASAYLNVSSAELNTPNFSFFTTVTVETTEISPEDITRKYKPVPTTSTGYQPAYTTSTTVLIQTTRVPKQVPVPSTDTTDKMQTSLDEVMKTTKIIIGCFVAVTLLAAAMLIVFYKLRKRHQQRSTVTAARTVEIIQVDEDIPAAASAAATAAPSGVSGEGAVVLPTIHDHINYNTYKPAHGAHWTENSLGNSLHPTVTTISEPYIIQTHTKDKVQETQI
Protein: Protein transport protein SEC23 B (AtSEC23B) (Protein transport protein SEC23 C) (AtSEC23C) (Q8H0S3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (By similarity). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P15303}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15303}; Cytoplasmic side {ECO:0000250|UniProtKB:P15303}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P15303}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15303}; Cytoplasmic side {ECO:0000250|UniProtKB:P15303}. Membrane {ECO:0000250|UniProtKB:P15303}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15303}; Cytoplasmic side {ECO:0000250|UniProtKB:P15303}.
Interaction partners:
- Protein transport protein SEC24 A
- Protein transport protein SEC24 C
- Protein transport protein SEC13 homolog A
- Protein transport protein SEC24 B
- Protein transport protein SEC13 homolog B
- Protein transport protein SEC31 homolog B
- Protein transport protein SEC31 homolog A
- Protein transport protein SEC23 D
- small monomeric GTPase
- Small COPII coat GTPase SAR1B
Sequence:
MSEMASMDPEGIDGVRMTWNVWPRTKVEASKCVIPVAACISPIRYHRDIPSVEYAPLRCRICTAALNPFARVDFLAKIWICPICFQRNHFPPHYHVMSETNVPCELYPQYTTVEYTLPNPSQPTGVGNFDQTGAVSGQPSPSVFVFVLDTCMIEEEFGYAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSDLTKVYVFRGDKEISKDQVLEQLGLGASGRRNPVGGFPMGRDNSANFGYSGVNRFLLPASDCEFTIDLLLEELQTDQWPVQAGRRQSRCTGVAISVATGLLGACFPGTGARIVALIGGPCSEGPGTIVSKDLSEPLRSHKDLDKDAAPFYKKAEKFYDALANQLVNQGHVLDLFASALDQVGVAEMKAAVERTGGLVVLSESFGHSVFKDSFKRVFEDGEESLGLCFNGTLEICCSKDIKIQGIIGPCASLQKKGPSVADTVIGEGNTTQWKMCGLDKRTCLTVFFDLSSSDQSSAPGGVNNQLYLQFMTSYQNSKGKTLQRVTTVTRQWVDTGLSTEELVQGFDQETAAVVVARLASLKMETEEGFDATRWLDRNLIRLCSKFGDYRKDDPASFTLNPNFSLFPQFTFNLRRSQFVQVFNNSPDETAYNRMLLNRENISNAAVMIQPSLTTYSFNSLPQPALLDVASIGADRILLLDSYISVVVFHGMTIAQWRNLGYQNQPEHQAFAQLLEAPQEDAQMIIRDRFPVPRLVVCDQHGSQARFLLAKLNPSATYNNASEMNAGSDIIFTDDVSLQVFFQHLQKLAVQS
Protein: Cilia- and flagella-associated protein 61 (Flagellar-associated protein 61) (A8IF44)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: As component of a spoke-associated complex, regulates flagellar dynein activity by mediating regulatory signals between the radial spokes and dynein arms.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:17967944}.
Interaction partners:
Sequence:
MSNITARQTLTRDVQSVDALVRQACKAEANATLLLGTGLLNLTAVDDKDTVVGYLSLDDVSCTRLGSGGPGADTWVQQAAASRFKLGSTAFVRVCATAHLSEIEASAALLRTAFLHMPSLQTLLMVAGGELSFTEPGLAAVFSRVGAHKESGAVLYEAGRDAVVPPLAIRPARVEDHDDMLPILQRCEVAFPALAKLPEASRPHEPFALTRVVAGQDERNRVLVAEAEGRLVGFIVMTSDVDTGSLAETFDLHAYDNFLPPEVYEQQYEAARDSVRGQKLAMLRHQRQQEKEAEGEGAGEAGGQGGNGGVSAGMQTDPEQGEDGEGAAEGEGEGAGEGAGEGGAAAPGTGADKADDSEEAEAQLLAAAEPTDEETRAEMLAMFAGQAPPADPTLFAVTMLCMDPAFEAQAIEFLTPAFAAYTDKLYCVVTLPHDSREPALMGTMTRVAPNPGSLFPEVLFMFHRHALIPDFAVRLGEPGDLDAVASLVAGMPNADDIVASFSGAAAAGSAAVALCQGELVGLVTVNPEVDLELLQANFGLSNHVDLGYQPREQHGEIDMYTMNPIFVHRHRTLVAATMRLLGKTALYYALPPGQQPPDMLEVLEQVAPRHRTASDKQLQAEFALYVFTRQAAFKRRRSVNSQIVVVGASECGLAVVERLLLDPELQFNYLTLLAPGGIKVGGMACQFTAGVIARLGLEARVMLLDAEVIGLDRGSKLLDLSDGSQIFYNQLVLAAGLQDQSRYRFAEADPEVAGLLVTELELAADFSMNDAMVMNSILVYGNAMGAYHSLAVLEAKGAGEKTRFVAPPGQQPPLVGVLHALAGEAGVALPSPEPRDLAGLSVVQPVGPELHASATLIDPADPGPREELPVDLVVGCEPPSVSRSLFTCLNDASLVFDGRLVVDGAFRTNDPAIYAGGSLAKLSRRYGGTHLEHYNSRDVGSRLASSLVSFFNAGPDEPQPAATAAAPPPALHRARAVGCSLPGGNYFVYAGCPAALQRPSTAAPEGGYEMKTASERGLTRITLDGEGRVHSLMYLGRVAVNAPRLGSLVGLHANYLNSLAPKYQAGDIKCLLSFITEPWSELLYNESFPELRETLLEVALAELSAGGREVDGGMVEWVTHAQDAVLEFARAHAAELPGYTMPSAART
Protein: Pteridine reductase 1 (EC 1.5.1.33) (H region methotrexate resistance protein) (Q01782)
Organism: Leishmania major
Function: Exhibits a NADPH-dependent biopterin reductase activity. Has good activity with folate and significant activity with dihydrofolate and dihydrobiopterin, but not with quinonoid dihydrobiopterin. Confers resistance to methotrexate (MTX).
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Putative 3-oxoacyl-ACP reductase
- Dihydropteridine reductase
Sequence:
MTAPTVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNARRPNSAITVQADLSNVATAPVSGADGSAPVTLFTRCAELVAACYTHWGRCDVLVNNASSFYPTPLLRNDEDGHEPCVGDREAMETATADLFGSNAIAPYFLIKAFAHRFAGTPAKHRGTNYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVGPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYITGTCVKVDGGYSLTRA
Protein: Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase (EC 3.5.1.118) (Gamma-glutamyl hercynylcysteine S-oxide hydrolase) (A0R5M9)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the hydrolysis of the gamma-glutamyl amide bond of hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce hercynylcysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine.
Interaction partners:
- Hercynine oxygenase
- Probable hercynylcysteine sulfoxide lyase
- Histidine N-alpha-methyltransferase
- Glutamate--cysteine ligase EgtA
Sequence:
MCRHVAWLGAPRSLADLVLDPPQGLLVQSYAPRRQKHGLMNADGWGAGFFDDEGVARRWRSDKPLWGDASFASVAPALRSRCVLAAVRSATIGMPIEPSASAPFSDGQWLLSHNGLVDRGVLPLTGAAESTVDSAIVAALIFSRGLDALGATIAEVGELDPNARLNILAANGSRLLATTWGDTLSVLHRPDGVVLASEPYDDDPGWSDIPDRHLVDVRDAHVVVTPL
Protein: Alpha/beta-Hydrolases superfamily protein (At1g18360/F15H18_2) (Q8VYJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Triacylglycerol lipase SDP1L
- Triacylglycerol lipase SDP1
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Glycerol kinase
- Aldo-keto reductase family 4 member C10
- 
- Non-specific phospholipase C3
- 
- RHOMBOID-like protein 5
Sequence:
MICSSKGTVVIATRSSFPRLLNRIQNRNDVPISVIATRRSSMSVEAFPMRLKSSQKKRKMNIGCGVSPSSPTTTVVDEEVAIRRKLAMRRVLEDNGGDGSSVRDFSLFTTKRGDTLFTQSWTPVDSAKNRGLVVLLHGLNEHSGRYSDFAKQLNVNGFKVYGIDWIGHGGSDGLHAYVPSLDYAVADLKSFIEKVIAENPGLPCFCIGHSTGGAIILKAMLDAKIEARVSGIVLTSPAVGVQPTYPIFGVIAPFLSFLIPRYQLSAAKKKIMPVSRDPEALLAKYSDPLVYTGFIRARTGNEILRLGAHLLQNLNRIKVPFLVMHGTADTVTDPKGTQKLYNEASSSDKSIKLYDGLLHDLLFEPERETIAGVILDWLNRRV
Protein: DNA topoisomerase 2 (EC 5.6.2.2) (Q383C4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Structural maintenance of chromosomes protein
- Small ubiquitin protein, putative
- Bifunctional dihydrofolate reductase-thymidylate synthase
- SUMO-conjugating enzyme UBC9
- DNA topoisomerase I
- DNA topoisomerase type IB small subunit
- Structural maintenance of chromosomes protein
- DNA topoisomerase
- Ubiquitin-conjugating enzyme E2, putative
- Proliferating cell nuclear antigen
Sequence:
MSGRTVEEIYQKKTQHEHILARPDMYIGTIEPVTEDVWVYDEADNVMKLRKCTWTPGLYKIFDEILVNAADNKVRDPHGQTTIKVWVDAARGLVRVYNNGEGIPVQRHREHDLWVPEMIFGHLLTSSNYDDTEAKVTGGRNGFGAKLTNVFSTRFEVETVHSRSRKKFFMRWRNNMLENEEAVITPCDGPDYTVVTFYPDFEKFNLEGFTEDMVLIMQRRVYDIAGCTDKSLCCYLNDTRIACRSFPEYVDLYPTMGEERKPSSYSRVNDRWEVCVRVSNVGFQQVSFVNSIATTRGGTHVKYIVDQIIAKVTDQAMRKSKTEVKPHMIRPHLFIFVNSLIENPSFDSQTKETLNTPKARFGSTCDLPASLIDCVLKSSIVERAVEMANSRLNREMAMKMRNTNRKQILGIPKLDDANEAGGKYSQRCTLILTEGDSAKALCTAGLAVENRDYFGVFPLRGKPLNVRDASVKKVMGCAEFQAVSKIMGLDLSQKYTSTEGLRYGHLMIMSDQDHDGSHIKGLIINMIHNYWPDLLKVPGFLQQFITPIVKARKKGRGNNDEGTISFFSMPDYFEWKNAVGEGIKNYELRYYKGLGTSGAKEGREYFENIDRHRLNFVYEDRKDDDDIVMAFAKDKVDERKRWITEFKANTNINESMNYNVRNVSYSEFVHKELILFSVADCERSIPSVVDGLKPGQRKIMFSAFKRNLVRSLKVAQLAGYVSEHAAYHHGEQSLVQTIVGLAQDYVGANNVPLLYRDGQFGTRLQGGKDHAAGRYIFTRLTDIARRIYHPSDDFIVEYRDDDGLSVEPFYYVPVIPMVLVNGTAGIGTGFATNIPNYSPLDVIDNLNRLLSGEELQPMKPWYFGFTGTIEEREKGKFVSSGCATVRPDGVVHITELPIGTWTQQYKKFLEDLREREIVIQYREHNTDVTVDFEVFIHPEVLRQWVAQGCVEERLQLREYIHATNIIAFDREGKITKYLDAESVLKEFYLVRLEYYARRREFLLEQLQRAALKLENMVRFVNEVIDGTFIVTRRSMKDVLKDLKQRGYTPFPPQQKKKMSSTTIVDEEDNDGARKILPDVFEFESVPLCEQVIGKILCTAEPEEINMWKGVLVEYDYLLSLRMVDLTVEMAMYFRTKREQMLNKHNFVLSASSKDLWREDLDLLRSDIEKLFDERRREIALIQCKKLEKRQFFDVSRLRVPLLSDAARKADRSLALRQSNCKREMSSKCASESFALLVDAGVRVSGLTEGSSICDINEARRKYGHSVAGGKRRLVRHDEVSKRGKFSSCGDQRHVSLSDGSDTDDCSIGAPSVSPSDATPATQKSRKISDSSYGFGIEGEVDIFFEDTVGEDFSEPATQANIVRSKSESPVLDFSAEYATEPKSRKRPRSIEDNDENTCPFYVDVVGEDVEYDSDQCIGFDACVF
Protein: Probable electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF) (P78790)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Probable electron transfer flavoprotein subunit beta
- Secretory component protein psh3
- Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
- Acetyl-CoA acetyltransferase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Putative acyl carrier protein, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- ATP synthase subunit alpha
- Uncharacterized protein C14C4.04
Sequence:
MLRTTSRTFSRALSSSNFKINCGRRHWFSVLTLLEHQGGNLSPASLSAVEAAKRTGGDVFGFVIGKDSSQISQKVAKSVNDLKKVIYVENPSYEHNIPDQIANVLFENVKKNEISHVFSAHSTVGKGVMPRLAAMFDVMQISDIIGVVSADTFVRPTYAGNVNVTVSTKDPIKIVTVRASAFDAAPSSGEGAATVVEGIDPKPAALQEWVSENIIKNARPDLSSAERVVAGGRPLKDKETFERILTPLADKLGAAIGATRVAVDSGYADNSLQIGQTGKIIAPKLYIAVGIDGAIQHLAGIKDSKVIAAINRDENAPIFQTADVGIVGDLFEIVPELTEKL
Protein: Macrophage migration inhibitory factor (MIF) (EC 5.3.2.1) (Delayed early response protein 6) (DER6) (Glycosylation-inhibiting factor) (GIF) (L-dopachrome isomerase) (L-dopachrome tautomerase) (EC 5.3.3.12) (Phenylpyruvate tautomerase) (P34884)
Organism: Mus musculus (Mouse)
Function: Pro-inflammatory cytokine involved in the innate immune response to bacterial pathogens (By similarity). The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense (By similarity). Counteracts the anti-inflammatory activity of glucocorticoids (By similarity). Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity.
Subcellular location: Secreted {ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:8234256}. Cytoplasm {ECO:0000250|UniProtKB:P14174}. Note=Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens (By similarity). {ECO:0000250|UniProtKB:P14174}.
Interaction partners:
- H-2 class II histocompatibility antigen gamma chain
- C-X-C chemokine receptor type 4
- C-X-C chemokine receptor type 2
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Tyrosine aminotransferase
- 4-hydroxyphenylpyruvate dioxygenase
- Putative aspartate aminotransferase, cytoplasmic 2
- L-amino-acid oxidase
- Amine oxidase
Sequence:
MPMFIVNTNVPRASVPEGFLSELTQQLAQATGKPAQYIAVHVVPDQLMTFSGTNDPCALCSLHSIGKIGGAQNRNYSKLLCGLLSDRLHISPDRVYINYYDMNAANVGWNGSTFA
Protein: Rhombotin-2 (LIM domain only protein 2) (LMO-2) (zlmo2) (Q9PTJ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that acts synergistically with tal1/scl in primitive and definitive hematopoiesis, and in endothelial development. Specifies mesodermal precursors to a hemangioblast cell fate. Hemangioblasts are bipotential precursors of blood and endothelium, and in the absence of hematopoietic induction cues such as gata1, tal1/scl-lmo2-induced haemangioblasts differentiate into endothelial cells.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P25801}.
Interaction partners:
- T-cell acute lymphocytic leukemia protein 1 homolog
- GATA-binding protein 1a.
- LIM domain-binding protein 1-A.
- Endothelial transcription factor GATA-2a
- BHLH domain-containing protein.
- Transcription factor 3a.
- Runt-related transcription factor
- LIM domain-binding protein 1-A
- Fli-1 protein
- Growth factor-independent 1A transcription repressor b.
Sequence:
MASTIERKTLEANEEPVDEVLQMPPSLLTCGGCQQSIGDRFFLKAIEQYWHEDCLSCDLCGCRLGEVGRRLYYKLGRKLCRRDYLRLFGQDGLCASCEKRIRAFEMTMRVRDKVYHLECFKCAACQKHFCVGDRYLLINSDIVCEQDIFEWTKLNGSIV
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (A0A024R625)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL
Protein: RanBP2-type domain-containing protein (Q38B21)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYLHSMKRYIRAPLAPLLNVGRSNSSCGGAVCFCAPCAGRTAYCPAYATQVAAFCMPTAALLQSWAVRTNRTWMCVKEECRHVNAPGATHCESCGEVKPNLKGWLCVECSTRNHKGVKKCHKCAAPAEKSSEFWMCAACEKNNRIDDLDDNSCCGFCGYDMAPMTMTEAEALRIQQERSERLRETQERFDALSAKDADEQFGDEMAGASELPAALKQGVPPAPRTMFDIPEVKPFAPTPQGTKHSRILRKPRPASSPGAPSGPPGFDWMCREPSCAVINSGDEECCTGCGKHIEPTEWECCHCGAVNHMTRARCFNCRVTISISWVCSDCRTATCIYERSCRACNKARPPTEPKEARDVQPPSQNAGRAGFSANRRRMPFKQDWNCEECQGLNFASRTSCYQCGAARSTADASYNGGASGGDGGFDGGAGLSVSHNNWFCRHCQASNFRTRASCWQCGRASSESGATTWSEDDSAPHFEKEGFQQTSDDNVAEGQVNVWNKKTDDWTCGKCFSKNFKNRQECHKCGATKTVAVAPRRAFVRKPVKI
Protein: Rad21/Rec8-like protein N-terminal domain-containing protein (A0A1D8PDC0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Structural maintenance of chromosomes protein
- separase
- Irr1p
- Serine/threonine-protein kinase
- Structural maintenance of chromosomes protein
- Pds5p
- DNA topoisomerase
- Sister chromatid cohesion protein
- Structural maintenance of chromosomes protein 5
- DNA repair protein
Sequence:
MELINQSNNSLSTGLHTAWLLATLGSKPSIRSKLIKKSTINYLSIPELCHELLASTNSTINDAQDKDAIIYEPPTPGNNIRYVSNIMHGISILYRTKINYLMNDLIYIESRLKCHYQNSYNDIVDLSSGSLIKTCLAPSMAKKRAIQYLSDDPAFSIQLGLVAPFTEETDEIAKRRKLDILRKDNDDFPLVNGNGGGLVDQLNFHSMTFTLHPQLDNSFEAEDHSSLNNGNNIGLSTDSEVIPDFEFDNNGDIVGIAGENLLLDSRSPTRELIHNEQADALNVTFDGNDVHEVNPIPLNQTTSISNDLNFYTTTDTPLPNSTQRPIPQQTLGMEKLPFRKLLIDNHTRIDSDSMIHFVMNYESRMNTVMEPVKSVDEVVNNIYGVVDAAPPFTRFVNKITLPNANNNNHNNSVEQSFFTRTASILQKTEETGNENTEEGRNTMNIRNYTMEPEIPDPNMYFEDGSHFELPRESEHIFNLEFDYNDINDVEEDDSIDGANSKNGSQQNSMSFDGSGDNLMTMDSKLNKFYRYIKARSNEFGKLVVGTYLISQAINENNVVLTEHTGDYYQTKFQILVPDSTHALDIDEPPVPRRVAANAFACVLTLATKSLINIEVIQETDELQNNNDINIILPLE
Protein: Visual system homeobox 2 (Ceh-10 homeodomain-containing homolog) (Homeobox protein CHX10) (X2JDS9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- AT27166p
- Protein Optix
Sequence:
MPQRSPFAIQELLGLAVAAATEAPTDLTTTAGATVAKERQTPTPPKTTNATMATAATSAATAATPTNAAEGNLTSVSEPQQQPQQQQQEQQHHQPHHHQYREHHQMTMAAASRMAYFNAHAAVAAAFMPHQLAAAVHHHHQHQHQHHPHHHPHHPHGAVGGPPPPPPMQHHHPHHPHHPLLHAQGFPQLKSFAAGAGTCLPGSLAPKDFGMESLNGFGVGPNSKKKKKKRRHSRTIFTSYQLEKLEEAFKEAHYPDVYAREMLSLKTELPEDRIQVWFQNRRAKWRKTEKVWGGSTIMAEYGLYGAMVRHSLPLPDTILKSAKDNDAVAPWLLGMEQKCMHRKSIEAQSALKDDSGVSDHEDSAGSKSAHSEDLSRSRCHALSSSTESLNVVSPAPSSCPTSASTSAPPTSTSGYAGAASSAATTPTGASTTNSSSSPHIELGSPSPQQQQHLQLQQQQQQQASLYLGAGAVVTGCAPPSYHPLLDAANAAGAGAAASSKDFHMIMNTAVAAAAAAAQQQHQQQQQQQQQATATAPGLHAHNLAAALMEHDPDAFRNNSIACLRAKAQEHQARLLNNGGLFLQVRRFAQGQAQIQDPSDMLKLSEEHNNNSPIPIPPAHSTVNTQVNVKMELTANGGSMKNYEEA
Protein: 2-iminobutanoate/2-iminopropanoate deaminase (EC 3.5.99.10) (Enamine/imine deaminase) (Q7CP78)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities and to avoid they are captured by anthranilate phosphoribosyltransferase (TrpD) to generate PRA, an intermediate in the alternative pyrimidine biosynthetic (APB) pathway. Also required for full activity of IlvE which is involved in the isoleucine biosynthesis. RidA also accelerates the release of pyruvate produced by IlvA from L-serine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- L-Threonine dehydratase biosynthetic IlvA
- L-threonine dehydratase catabolic TdcB
- Diaminopropionate ammonia-lyase
- Aspartate carbamoyltransferase regulatory chain
- Branched-chain-amino-acid aminotransferase
- Thiamine import ATP-binding protein ThiQ
- Aspartate carbamoyltransferase catalytic subunit
- Bifunctional protein TrpGD
- Arginine repressor
- Translation initiation inhibitor
Sequence:
MSKTIATENAPAAIGPYVQGVDLGSMVITSGQIPVDPKTGAVAEDVSAQARQSLENVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVRR
Protein: Nucleolin (H7BY16)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSDDSRKTDQSSAYVRTTSRTLQHVLGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE