wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein, isoform C (A0A0B4KHU4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLHIVSVVIIALSLGCAVGQDLRRVDDTELIQLLTGSSNVVVLFNKNNCQRCVEYENMVTKIRAQLEETLSAIVVQSVDSNLVSIYDPSKEPALVFFRRGIPILYHGEINDDEILDFFNDNLEPAVKELSDDNFEHLTQASSGATTGDWFIFFSSAECTVCQRLYAVWESVGGKLKRKLNIARMNSLESGISTATRLGVLEAPAFIFLRQGKMYKYSAKQYSPEAFVQFAEKGYTQSHPQPVPAIPSAVDL
Protein: HTH-type transcriptional regulator ArgR (G3XCU2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: ArgR could be a transcriptional activator of the dauBAR operon in response to the presence of L-Arg.
Interaction partners:
- Arginine/ornithine transport ATP-binding protein AotP
- Histidine/lysine/arginine/ornithine transport system permease protein HisM
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Arginine N-succinyltransferase subunit beta
- Succinylglutamate desuccinylase/Aspartoacylase catalytic domain-containing protein
- Succinylornithine transaminase/acetylornithine aminotransferase
- Oligopeptide transporter, OPT family
- Arginine N-succinyltransferase subunit alpha
- Transcriptional regulator DauR
- Ornithine carbamoyltransferase, anabolic
Sequence:
MTAQPQRIGFLLWPATRALTLSLAEEALRAARRLHPEALYEPLFLLAEAPAEEEGWRLPGTAWNGRLEQCSRLFLVADEAPAAVSPALGLALKQLARSGAAIGALSAGIYPLAQLGLLDGYRAAVHWRWHDDFTERFPKVIATNHLFEWDRDRMTACGGMAVLDLLLALLSRDHGAELAGAVSEELVVERIREGNERQRIPLKNRLGSSHPKLTQAVLLMEANIEEPLTTDEIAQHVCVSRRQLERIFKQYLNRVPSQYYLELRLNRARQMLMQTSKSIIQIGLSCGFSSGPHFSSAYRNFFGVTPREDRNQRRGGSAFETTFTPVERG
Protein: Importin subunit alpha (F4HXL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSYKPSAKTEVRRNRYKVSVDADEGRRRREDNMVEIRKNKREENLQKKRREGFNPSMASQPGQDFSSSLPTETRLENIQQMIAGVMSEDRDLQLEATASFRRLLSIERNPPINEVVQSGVVPHIVQFLSRDDFTQLQFEAAWALTNIASGTSENTRVIIDSGAVPLFVKLLSSASEEVREQAVWALGNVAGDSPKCRDHVLSCEAMMSLLAQFHEHSKLSMLRNATWTLSNFCRGKPQPAFEQQTKAALPALERLLHSTDEEVLTDASWALSYLSDGTNEKIQTVIDAGVIPRLVQLLAHPSPSVLIPALRTIGNIVTGDDIQTQAVISSQALPGLLNLLKNTYKKSIKKEACWTISNITAGNTSQIQEVFQAGIIRPLINLLEIGEFEIKKEAVWAISNATSGGNHDQIKFLVSQGCIRPLCDLLPCPDPRVVTVTLEGLENILKVGEAEKNLGNTGNDNLYAQMIEDADGLDKIENLQSHDNNEIYEKAVKILESYWAADDEEEDIGGVDAPENVQSSGFQFGNQSGNAPTGGFNFG
Protein: phosphopyruvate hydratase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (A0A024R4F1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK
Protein: Nuclear receptor coactivator 4 (E9Q2H3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNTSLEQSGCYSNRETLLRCSDARRELELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLNEQVDLIYQLKEETLQQQAQQLYWLMGQFNCLIHQLEYTQNKDLANQVSVCLERLGSLALKPEDSTVLLFEADTSALRQTITTFGSLKTIQIPEHLMAHASSSSIGPFLEKRGYIQVPEQSASSGTAVSLSEWLLVSKPAIGLQAPYVPSTNPQDWLIPKQTSENSQTSARACSFFSDAWGNLKGLENWLLNSHQQEIAGKPSSSKCNSHCSTSSFSPEAEKAEDVELLDQDELDLSDWLVTPQEPCELEKPVDGSWETSEKFKLLFQ
Protein: Laminin subunit beta-1 (Laminin B1 chain) (P11046)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (By similarity). Required for Ndg localization to the basement membrane.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:30260959}.
Interaction partners:
- Laminin subunit gamma-1
- Laminin subunit alpha
- Integrin beta-PS
- Integrin beta-nu
- LP17136p
- Nidogen
- Viking, isoform A
- Collagen alpha-1
- FI24025p1
- Netrin receptor unc-5
Sequence:
MLELRLIVVIVLALLSWQWDPVDSQRPPQHGRRDRPKYPPNKFIKTHPCERSSCYPATGNLLIGRENRLTASSTCGLHSPERFCILSHLQDKKCFLCDTREETKHDPYKNHRIGQIIYKTKPGTNIPTWWQSENGKENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENITDVMCTSRYSNVEPSRNGEVIFRVLPPNINVTDPYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENEEKYYYGISNMVVRGSCSCYGHASQCLPLDPAFSQADNEDGMVHGRCECTHNTKGMNCEECEDFFNDLPWKPAFGKKTNACKKCECNDHAVSCHFDEAVFTASGFVSGGVCDNCLHNTRGQHCEECMPYFYRDPEQDITSERVCQPCDCDPQGSSDDGICDSLNELEEGAVAGACHCKAFVTGRRCNQCKDGYWNLQSDNPEGCEPCTCNPLGTLNNSGCVMRTGECKCKKYVTGKDCNQCMPETYGLSESPEGCSLCNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYFIPLLPEVHEAEVVDECISYGANGNCSLVAETPDGSFTGIGFTRVPENSELVFTVGDIPRSMPYDAVIRYQSTSRGDWENAFITLVRPDQVDPEGGCGELAAATSSETRIPFSLPDRSRQVVALNEVCLEAGKVYKFRIYFERKRHDVDSPTATILVDSLTLIPRIDVTPIFQGSVLADIRKKDYEKYNCKSSLYDMNYKSDPKCQNLDNILSVFVHDGASMCNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGCKACDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPECRVCQCNGHAATCDPIQGTCIDCQDSTTGYSCDSCLDGYYGNPLFGSEIGCRPCRCPETVASGLAHADGCSLDTRNNNMLCHCQEGYSGSRCEICADNFFGNPDNGGTCSKCECSNNVDLYDTGNCDRQTGACLKCLYQTTGDHCELCKDGFFGDALQQNCQQCECDFLGTNNTIAHCDRFTGQCPCLPNVQGVRCDQCAENHWKIASGEGCESCNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKCQPCECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGQFPHCSPCGECFNNWDLILSALEDATTATILRAKEIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGALNLTRHAYERVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIPELNNQVCGKPGDPCDSLCGGAGCGHCGGFLSCEHGAKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDRVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQCYT
Protein: Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M) (P38174)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays only a minor role in N-terminal methionine removal. Less efficient when the second residue is Val, Gly, Cys or Thr.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Methionine aminopeptidase 1
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL29A
- Ribosome assembly factor MRT4
- Large ribosomal subunit protein uL24B
- Large ribosomal subunit protein uL24A
- Large ribosomal subunit protein uL3
Sequence:
MTDAEIENSPASDLKELNLENEGVEQQDQAKADESDPVESKKKKNKKKKKKKSNVKKIELLFPDGKYPEGAWMDYHQDFNLQRTTDEESRYLKRDLERAEHWNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGAENLLAMEDPKSQGIGFPTGLSLNHCAAHFTPNAGDKTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEINGETYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDTTKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEDHQVMPTLDSAKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFALNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVSKGDDY
Protein: Replication protein A subunit (Q4Q884)
Organism: Leishmania major
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364130}.
Interaction partners:
- Putative replication Factor A 28 kDa subunit
- Uncharacterized protein
- Serine/threonine-protein kinase ATR
- Putative DNA repair protein
- DNA polymerase
- RecA family profile 1 domain-containing protein
- DNA repair protein RAD51 homolog
- DNA polymerase
- Putative endo/exonuclease Mre11
- DNA primase large subunit
Sequence:
MQQPGSHQIQPIDSLTPFLGGKWWIRARVTDKTDIRTWNKPTSQGKLFSFTLIDESAAIRATVFNDAVDTFEPLIVNGQVYYFSGGQVKNANRRFSNVNNDYELTFDRSSEIMLARQDTSTAALPMQRYNFVPIELLKQREVGSLVDVLGVVLKVDEVSSITQKSTGRELMKRNVKMGDMTAAVEVTFWNDEAKAWCYPVGTVVALRQLKVGSFDGVTLSSTYQTKIDINPTDLPDVKKLATWYVATGGANVTSLSSQGLGAASGAGGESDRGRKYLDEIQSEGIGRGLKPEYVDVRCVPIYFKQDAQWYDACPTCNKKVTEEGAQGDRFRCEKCDKTVTPTQRYLVSIQVTDNVSQAWLTLFNEAGIEFFGMEAAELKRRAQEDPLYIAKLAQGRMNRPVVMRLRVKEEMSSNSMTGEESDRLRMSVVRISEFMPIAGTSEETRRRLAQNLRTECDEILRLIEAYV
Protein: Gamma-tubulin complex subunit, putative (Q383E4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Spindle pole body component
- Spindle pole body component
- Tubulin gamma chain
- Tubulin delta chain
- Voltage-dependent anion-selective channel
Sequence:
MYIFFSCFIFLFFIFFSMSDGVQYSKDVFPAPKWHRAEGDSAANRECVQRVVPFKAVSAGENVDSLTCVGGRLPSVDSLSSPLEGGEIVGNVDDKLKHSHVSVVDDRQPVSSVTGRRGNSFELPGRLIGRRDGSGGVVGSGRFEITPLKPSSTISGITPRHFDVLHPLEDSADRGKHDFVGGVLNAANDAGGAKAIEELEFISDMLFMWMGVDKTKYFAYDNACCRYEMNSGYGTVRQRQAFSAFQECGCLAHQIDDALRGGTSERSFLQQSLRGAVRRHLSQYHTLVASFRGRQTPPMAFGDLVVAFKRVQPKLRVLHTMLKETENVKGGELASKLQRLVQQGSRRLCALLSDVYMEAVSPLLHMTVSSIIKGDVSDPFNEFFVKSDPRVEDTSDTFWSSKFSLLPDMLPTTVSYSLAERIRLVAKNVSFIRNCCRCKQWHMDPSIVAAAQSATFDTLDSVVRDAMRFTNTAVLRLIREEFHLDNVLRMVNAFLLVGNGDFYEVLIHKLDPVLGRMSHMVQTSLVRDHMQSALLDITPHTKNLDTDLFTMLHCEIVKDDKIIGWDAFVVTMSVPSPLNNIFDASAMKVYRRLFRMMFKVKRAEVALKNSWRQSVVLDRIIGGLHNAKRETTAWREVAADAHLLGLQLNHFVNNLWSYLVAEVSTVSWDLLMRALRQCNSMDDIRAAHISYLQYLTLHSLLHGDCTSIRQNIESVLSVVRQFVGAQAVLTSLLERGHGDVFSIKNEYQRLADDFQREISSLLTTLEEQHLQFDFLNFLLLRLNFNHFYHDNAFGDNTEF
Protein: Large ribosomal subunit protein eL6B (60S ribosomal protein L6-B) (L17) (RP18) (YL16) (P05739)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL6A
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS17A
- Small ribosomal subunit protein eS7A
- Large ribosomal subunit protein eL33A
- Large ribosomal subunit protein eL20A
Sequence:
MTAQQAPKWYPSEDVAAPKKTRKAVRPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLVTGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQTKEIKTERVEDQKVVDKALLAEIKKTPLLKQYLSASFSLKNGDKPHLLKF
Protein: Immunoglobulin-binding protein 1 (Alpha4 phosphoprotein) (CD79a-binding protein 1) (Lymphocyte signal transduction molecule alpha 4) (Protein phosphatase 2/4/6 regulatory subunit) (p52) (Q61249)
Organism: Mus musculus (Mouse)
Function: Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein kinase mTOR
- Target of rapamycin complex subunit LST8
- Regulatory-associated protein of mTOR
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Proline-rich AKT1 substrate 1
- DEP domain-containing mTOR-interacting protein
- Immunoglobulin-binding protein 1b
Sequence:
MAASEDELLLPRLPELFETSKKLLEDVEVATEPTGSRTIQDKVSKGLELLEKAAGMLSQLDLFSRNEDLEEIASTDLKYLMVPALQGALTMKQVNPSKRLDHLQRAREHFVHFLTQCHCYHVAEFQLPQTKTNSAENNTASSSMAYPNLVAMASQRQAKIERYKQKKEVEHRLSALKSAVESGQADDERVREYHLLHLRRWIAVSLEELESIDQEIKILKEKDSPREETACHSSLPEKPPMKPFILTRNKAQAKVFGTGYPSLATMTVSDWYEQHQKYGVLPDRGIAKPASADFQRAAQQQEDQEQKDEESEEKALHRMREWDDWKDTHPRGYGNRQNMG
Protein: Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i) (O35955)
Organism: Mus musculus (Mouse)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Plays a role in determining the T-cell repertoire for an antiviral T-cell response.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-4
- Proteasome subunit beta type-8
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-9
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-1
Sequence:
MLKQAVEPTGGFSFENCQRNASLEHVLPGLRVPHARKTGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAITAGILSDLGSGGNVDACVITAGGAKLQRALSTPTEPVQRAGRYRFAPGTTPVLTREVRPLTLELLEETVQAMEVE
Protein: Transcription factor HES-4-B (Hairy and enhancer of split 4-B) (Protein hairy-2) (Xhairy2) (Protein hairy-2a) (Xhairy2b) (Q90VV1)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'. Promotes floor plate development and prechordal plate development. Required for lens development as early as the stage of lens field formation, partly through regulation of gene expression of the cell cycle inhibitor cdknx/p27(xic1). Required for formation of the neural crest downstream of multiple signaling pathways, and acts at the neural plate border via both DNA-binding dependent and independent mechanisms; acts in a DNA-binding dependent manner to repress pro-apoptotic and neural crest differentiation genes, including id3, delta1, and cdknx/p27(xic1), and thus promote the cell survival of neural plate border cells and maintain them in an undifferentiated state. Represses transcription of id3, at least in part through the repression of bmp4. On the other hand, acts in a DNA-independent manner separate from the transcriptional repressor function, to stimulate cell proliferation and promote neural crest formation. Via this DNA-independent route, acts in neurulae upstream of stat3 to transiently up-regulate the notch ligand dll1/delta1, which in turn up-regulates id3 expression. Then interacts directly with id3, which blocks the transcriptional repressor function of hes4-B/hairy2b to allow the progression of neural crest progenitors through specification and differentiation. Also acts via repressor-dependent and repressor-independent mechanisms in early gastrulae to establish the prospective anterior prechordal mesoderm identity in the Spemann organizer; induces specific genes independently from direct transcriptional regulation, and represses the genes specific for neighboring tissues through direct transcriptional repression. Modulates lateral inhibition during notch signaling and regulates the cell context dependent effects of notch (which can have inhibitory, permissive or enhancing roles in muscle or neural differentiation). Inhibits myogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P14003, ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MPADSMEKPTASPIAGAPANSAQTPDKPKSASEHRKSSKPIMEKRRRARINESLGQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRVQMTAALTADPSVLGKYRAGFNECMNEVTRFLSTCEGVNTEVRTRLLGHLSSCLGQIVAMNYQQPPSSQQPVHVQLPSSTPVPMPCKVNPAEAISPKVFQGGFQLVPATDGQFAFLIPNPAYTSSPGPVIPLYANATSPGGPPSQSPVQGLTSFAHKMPHMAQAVSPLGGSTRADSAESVWRPW
Protein: Uncharacterized protein (B7ZVW5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRSNPVKPALDYFSNRLVNYQISVKCSNQFKLEVCLLNAENKVVDNQAGTQGQLKVLGANLWWPYLMHEHPAYLYSWEDGDCSHQSLGPLPACDLCDQLHLRSRQGGSVCGCDPCEQLLLLVSQLRAPGVDSAAAGRPV
Protein: Tyrosine-protein kinase receptor (EC 2.7.10.1) (I3PGL2)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
ITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTTYENFIHLMIALPIAVLLIVGGLVIMLYVFHRKRNSSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDML
Protein: Non-hemolytic phospholipase C (EC 3.1.4.3) (PLC-N) (Phosphatidylcholine cholinephosphohydrolase) (Phosphatidylcholine-hydrolyzing phospholipase C) (PC-PLC) (P15713)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Hydrolyzes phosphatidylserine as well as phosphatidylcholine.
Interaction partners:
- Hemolytic phospholipase C
- Cardiolipin synthase A
- Cardiolipin synthase B
- PLD phosphodiesterase domain-containing protein
- Phosphatidylcholine synthase
- Diacylglycerol kinase
- Phosphatidylglycerophosphatase A
- Phosphatidylserine decarboxylase proenzyme
- Nus factor SuhB
- Exotoxin A
Sequence:
MISKSRRSFIRLAAGTVGATVATSMLPSSIQAALAIPAHRRHGNLKDVEHVVILMQENRSFDHYFGTLKGVRGFGDRMAIPLPDGQRVWHQKGSKGEILPYHFDTSTTSAQRVDGTPHTWPDAQQAWNEGRMDKWLPAKTERSLGYYKEQDIAFQFAMANAFTICDAYHCSFQGGTNPNRLFLWTGTNDPLGQHGGPVTTNDHDSNGPVEQGYTWTTYPERLQAAGITWRVYQDMADNFSDNPLIGFRQYRAAAPDSPLIVNGLSTWKLDALKRDVLANSLPQVSWIVAPAKYSEHPGPSSPIWGAEYTSWVLDALTANPEVWSKTALLVMFDENDGFFDHVAPPAAPSLNKDGTLRGKTTADATLEWHTKGDIRYRNQPYGLGPRVPMYVISPWSKGGWVNSQVFDHTSVIRFLEQRFGVMEPNISPWRRAVCGDLTSAFNFANPNNEPFPELPDTSQADAIVASQIKLPKPKPPAVAAMPKQEMGIRPARALPYELGVHARYRSGGDALSLTFANTGKAGAVFQVFDLLDSENPPKRYTVGARKRLHDSFQGDASGDYHLEVHGPNGFLRVFRGNLRRDLAERKAPLPEVRIDYEPLFGNLRVQLINRGRHPVKLTVKDNVYRQGERRTVNVPPGQRREVRYSLRSSGNWYDFSVSAQGADSFLRRFSGRMEDGRSGFSDPGMGLGTLTF
Protein: Splicing factor 3B subunit 1, putative (Q382Z6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Pre-mRNA-processing factor 19
- Splicing factor 3B subunit 10
- Probable eukaryotic initiation factor 4A
- RNA-binding protein, putative
- PRP1 splicing factor N-terminal domain-containing protein
- PHD finger-like domain-containing protein 5A
- Cell division control protein, putative
- Spliceosome-associated protein, putative
Sequence:
MADEDGSVEPTLKAHRWEMSSSASAAPTTSRWGAGTPRQRGGDTPKVVVNTELSAWRGHATPTPSAYAMDPAKTPTMRATGGATPVQGGQTPMFGGQTPVFGGQTPAFGSGTPMFTGATPAAGMAFGATPNYQFEGTTPVQSHFAGGESQSAVTANIGAQARKLEMQWRVKNKRLTEEYLDSILPPEFKLVEPPADYNPPPTEEPNFYELASKSLDVFVVNQNSDAAASMTYDIPESLGDGMPQMQTQDAPVFEVLLKYHNVNPIPDEVLPSYMLMKNLFKIKNGDTNQRRIAMRYLLDKARIFGSGPLFQFTFHVWRSGILDVIEQHYYVDLVKGAISRLQKDVRGSSKEIVHMMEVLLSAQERVLRDDGKEVLILLTRVVGYEAVFEAIKEDFAHAESGVRRHTAKVVAIIAFAVGPEIAIKIIHGMSLSPVALARQTSARAITEMATILMHAITGELVELVPIFEKLLRDEPRVKREAASALAHVAEATYPYGIEELDSLVYIVREECKRGIGTTTGLFVRAFGALIPLMAPYDAQKYTSDMLPTLVNQFNTPDDEHRRVLLQVVRQCVSADGVTVDFIRNVILRPFFEGFWTIRRVAADRKTAGILIDTTVGIARRIGSTEILQYLVQDMKDENEHFQRMVVETVRRVIANVGAVGVPDTLVALLMDGAIAAVKQDETGLNRVVMEGLATICNALGTRLKRHLRQIFDLIKSRRDMPGMIRMQAAELAARIATTVKDAGGALFLQDLGRSLFDRLEDDEAAVMSANLKATRVILVELGAARYQPPVRELLKKLMYIIPNRNSNVQLNTILLVEEIATNCDEDVEAIHLQELATKGLFELLDAHRRETRRACTRTFGVIARKIRPFAIILELVDNFKQDKRKIRICTAVALGAIARECGAFTVIPYLLNESKICEGEQVATIVQHSILKAVRYIFEAIGAAGKDFVYPLVPLLVRALTEMEIQHRRMAVEACRSIVLAVAGNDGFEDLVIHFLNFIHPNIVELLSRNETKISEERLKMVTAVVGYYEAARLVIGSGKLFQYLLQGLFHPAKKVRDIYRRTYNMVYMASPEALVPYYPRLGDDNEHTYVRHELEVLL
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Q9XUS5)
Organism: Caenorhabditis elegans
Interaction partners:
- phosphoglucomutase
- Probable galactose-1-phosphate uridylyltransferase
- Glycogen [starch] synthase
- dTDP-D-glucose 4,6-dehydratase
- Alpha-1,4 glucan phosphorylase
- UDP-glucose 4-epimerase
- Phosphoglucomutase-2
- glycogenin glucosyltransferase
- Glycogenin-1
- UDP-glucose 6-dehydrogenase
Sequence:
MNVSFSTSSLSVSNSRTRLISFRETEHGDQKSSEEWKTSTKLEALGSMEGELAHLLSTCKPETLNHNKTELSGFRNLFARFLRAKPTVDWSKIEPLPEGAIRPYKSLGHVVDKELIASQLRKLVVVKLNGGLGTSMGCKGPKSVISVRNDLTFLDLTMQQIQTLNKTYGVDVPLVLMNSFNTNEDTQKVLKKYANVKVSVHTFSQSQYPRINRETLLPIVKSLEADDNECWYPPGHGNFYEAFHNSGLLDKFLADGKEYCFLSNIDNMGATVDLSILNFVLNPSPDQTAPEFLMEVTDKTRADVKGGTLIQYEGRLMLLEIAQVPKDYVDEFKSISKFRIFNTNNLWAKLDAMRKIVVENKLEMEVIVNPKHLDRGLDVIQLETAAGAAIKSFSGAVGVNVPRSRFLPVKKTSDLLLLMSNLYDIDNGSLTLSHQRSFPTTPLVKLGSSFDKVKDYLGRFNGIPDLLELDHLTVSGDVWFGKDVSLKGTVIIIANHGDRIDIPPGSILENKIVSGNLRILEH
Protein: Probable arabinosyltransferase A (EC 2.4.2.-) (P9WNL9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable arabinosyltransferase B
- Galactan 5-O-arabinofuranosyltransferase
- Meromycolate extension acyl carrier protein
- Alpha-
- Terminal beta-
- Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase
- Small ribosomal subunit protein uS12
- DNA gyrase subunit A
- Catalase-peroxidase
- Arabinogalactan biosynthesis recruiting protein Rv3789
Sequence:
MPHDGNERSHRIARLAAVVSGIAGLLLCGIVPLLPVNQTTATIFWPQGSTADGNITQITAPLVSGAPRALDISIPCSAIATLPANGGLVLSTLPAGGVDTGKAGLFVRANQDTVVVAFRDSVAAVAARSTIAAGGCSALHIWADTGGAGADFMGIPGGAGTLPPEKKPQVGGIFTDLKVGAQPGLSARVDIDTRFITTPGALKKAVMLLGVLAVLVAMVGLAALDRLSRGRTLRDWLTRYRPRVRVGFASRLADAAVIATLLLWHVIGATSSDDGYLLTVARVAPKAGYVANYYRYFGTTEAPFDWYTSVLAQLAAVSTAGVWMRLPATLAGIACWLIVSRFVLRRLGPGPGGLASNRVAVFTAGAVFLSAWLPFNNGLRPEPLIALGVLVTWVLVERSIALGRLAPAAVAIIVATLTATLAPQGLIALAPLLTGARAIAQRIRRRRATDGLLAPLAVLAAALSLITVVVFRDQTLATVAESARIKYKVGPTIAWYQDFLRYYFLTVESNVEGSMSRRFAVLVLLFCLFGVLFVLLRRGRVAGLASGPAWRLIGTTAVGLLLLTFTPTKWAVQFGAFAGLAGVLGAVTAFTFARIGLHSRRNLTLYVTALLFVLAWATSGINGWFYVGNYGVPWYDIQPVIASHPVTSMFLTLSILTGLLAAWYHFRMDYAGHTEVKDNRRNRILASTPLLVVAVIMVAGEVGSMAKAAVFRYPLYTTAKANLTALSTGLSSCAMADDVLAEPDPNAGMLQPVPGQAFGPDGPLGGISPVGFKPEGVGEDLKSDPVVSKPGLVNSDASPNKPNAAITDSAGTAGGKGPVGINGSHAALPFGLDPARTPVMGSYGENNLAATATSAWYQLPPRSPDRPLVVVSAAGAIWSYKEDGDFIYGQSLKLQWGVTGPDGRIQPLGQVFPIDIGPQPAWRNLRFPLAWAPPEADVARIVAYDPNLSPEQWFAFTPPRVPVLESLQRLIGSATPVLMDIATAANFPCQRPFSEHLGIAELPQYRILPDHKQTAASSNLWQSSSTGGPFLFTQALLRTSTIATYLRGDWYRDWGSVEQYHRLVPADQAPDAVVEEGVITVPGWGRPGPIRALP