wanglab/gogpt-training-data huggingface dataset:
Protein: Acetylcholine receptor subunit gamma (P04760)
Organism: Mus musculus (Mouse)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Acetylcholine receptor subunit delta
- Neuronal acetylcholine receptor subunit alpha-4
- Acetylcholine receptor subunit beta
- Neuronal acetylcholine receptor subunit alpha-6
- Neuronal acetylcholine receptor subunit beta-2
- Acetylcholine receptor subunit alpha
- Syntaxin-binding protein 5
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-2
- Neuronal acetylcholine receptor subunit alpha-5
Sequence:
MQGGQRPHLLLLLLAVCLGAQSRNQEERLLADLMRNYDPHLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPKDYEGLWILRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSSCSISVTYFPFDWQNCSLIFQSQTYSTSEINLQLSQEDGQAIEWIFIDPEAFTENGEWAIRHRPAKMLLDSVAPAEEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIYFLPAKAGGQKCTVATNVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLMVVTILIVVNSVVVLNVSLRSPHTHSMARGVRKLFLRLLPQLLRMHVRPLAPAAVQDARFRLQNGSSSGWPIMAREEGDLCLPRSELLFRQRQRNGLVQAVLEKLENGPEVRQSQEFCGSLKQASPAIQACVDACNLMARARRQQSHFDSGNEEWLLVGRVLDRVCFLAMLSLFICGTAGIFLMAHYNQVPDLPFPGDPRPYLPLPD
Protein: Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 1 (Na(+)/K(+)-transporting ATPase subunit beta-1-interacting protein 1) (Protein FAM77C) (Q9D035)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGKCSGRCTLVAFCCLQLVAALQRQIFDFLGYQWAPILANFLHIMAVILGIFGTVQYRSRYLILYAAWLVLWVGWNAFIICFYLEVGQLSQDRDFIMTFNTSLHRSWWMENGPGCLVTPVLNSRLALEDHHVISVTGCLLDYPYIEALSSALQIFLALFGFVFACYVSKVFLEEEDSFDFIGGFDSYGYQAPQKTSHLQLQPLYTSG
Protein: Zinc finger protein Aiolos (Ikaros family zinc finger protein 3) (O08900)
Organism: Mus musculus (Mouse)
Function: Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Binds to GGGAA. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:9155026}. Cytoplasm {ECO:0000269|PubMed:9155026}.
Interaction partners:
- Protein cereblon
- DNA-binding protein Ikaros
- Zona pellucida-binding protein 2
- Paired box protein Pax-5
- Forkhead box protein P3
- DNA damage-binding protein 1
- Interferon regulatory factor 4
Sequence:
MEDIQPTVELKSTEEQPLPTESPDALNDYSLPKPHEIENVDSREAPANEDEDAGEDSMKVKDEYSDRDENIMKPEPMGDAEESEMPYSYAREYSDYESIKLERHVPYDNSRPTGGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRAFLQNPDLGDAASVEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDANYNPGYMYEKENEMMQTRMMDQAINNAISYLGAEALRPLVQTPPAPTSEMVPVISSVYPIALTRADMPNGAPQEMEKKRILLPEKILPSERGLSPNNSAQDSTDTDSNHEDRQHLYQQSHVVLPQARNGMPLLKEVPRSFELLKPPPICLRDSIKVINKEGEVMDVFRCDHCHVLFLDYVMFTIHMGCHGFRDPFECNMCGYRSHDRYEFSSHIARGEHRAMLK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A1ZBL9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 14-3-3 protein epsilon
- Bazooka, isoform B
- AT08303p
- Dual specificity mitogen-activated protein kinase kinase dSOR1
- Raf homolog serine/threonine-protein kinase Raf
- Tyrosine-protein kinase Src42A
- Connector enhancer of KSR protein CNK
- Protein aveugle
- Atypical protein kinase C
- Maternal effect protein oskar
Sequence:
MSTAMRTTLQSVPEALPADSVSNGTASNVAAPAAPVSSATNAVPPLAAVSSTTATYATNSISTSSHSVKDQQQQQQQQQHDSANANIVSLPPTTTPVANTNTMMPIVTSSNSATSNSTAATPTPASGAAATGGVGSVSQGPATVSASAANTNHSHQHSHQHHHHVANNMTTDGARLSSNNSAVVASSAINHHHHHTPGSGVAPTVNKNVLSTHSAHPSAIKQRTSSAKGSPNMQMRSSAPMRWRATEEHIGKYKLIKTIGKGNFAKVKLAKHLPTGKEVAIKIIDKTQLNPGSLQKLFREVRIMKMLDHPNIVKLFQVIETEKTLYLIMEYASGGEVFDYLVLHGRMKEKEARVKFRQIVSAVQYCHQKRIIHRDLKAENLLLDSELNIKIADFGFSNEFTPGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGSTLRELRERVLRGKYRIPFYMSTDCENLLRKFLVLNPAKRASLETIMGDKWMNMGFEEDELKPYIEPKADLADPKRIEALVAMGYNRSEIEASLSQVRYDDVFATYLLLGRKSTDPESDGSRSGSSLSLRNISGNDAGANAGSASVQSPTHRGVHRSISASSTKPSRRASSGVGPTNAAATVAAATGAVGAVNPSNNYNAAGSAADRASVGSNFKRQNTIDSATIKENTARLAAQNQRPASATQKMLTTADTTLNSPAKPRTATKYDPTNGNRTVSGTSGIIPRRSTTLYEKTSSTEKTNVIPAETNLFDRLRMASAVKSSRHFPRNVPSRSTFHSGQTRARNNTALEYSGTSGASGDSSHPGRMSFFSKLSSRFSKRPTIADEAAKPRVLRFTWSMKTTSPLMPDQIMQKIREVLDQNNCDYEQRERFVLWCVHGDPNTDSLVQWEIEVCKLPRLSLNGVRFKRISGTSIGFKNIASRIAFDLKLXLNQTNNEGNAAATASRPTDPTDTMTTTNCRRPSNDSTSRLSELSLLCRSLTSQQGSQRRKKSRLSTGGSEDQKKSNSLLSAFQMYSPFSSKENMQSSEEVEDLHVIDTQPGHSVDVPLFADFSPINPIMEEDAEGVEGGKTSEAKVISGGSGQKVKGDGGGGGGGNRLKRNIKHTGSLIVRKLTAGRHNDADKKGAIRKKDKEQQEVADTDKERPTSKPEGKVAMLRTTTL
Protein: Protein RD3 (Retinal degeneration protein 3) (Q8BRE0)
Organism: Mus musculus (Mouse)
Function: Plays a critical role in the regulation of enzymes involved in nucleotide cycle in photoreceptors. Inhibits the basal catalytic activity and the GCAP-stimulated activity of GUCY2E and GUCY2F, two retinal guanylyl cyclases involved in the production of cGMP in photoreceptors. Involved in the transport of GUCY2E and GUCY2F to their target sites in the photoreceptor outer segment. Up-regulates the activity of GUK1, a kinase that also plays an essential role for recycling GMP and indirectly, cGMP (By similarity). Plays an important role for the survival of rods and cones in the retina.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:29515371}. Photoreceptor inner segment {ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:29515371}. Endosome {ECO:0000269|PubMed:21078983}. Nucleus {ECO:0000269|PubMed:17186464}. Cytoplasm {ECO:0000250|UniProtKB:Q7Z3Z2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7Z3Z2}. Note=Colocalizes with GUCY2E and GUCY2F in rods and cones photoreceptors. Colocalizes with GUK1 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer (PubMed:29515371). Strong dot-like perinuclear staining in the epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q7Z3Z2, ECO:0000269|PubMed:29515371}.
Interaction partners:
- Peripherin-2
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Guanylyl cyclase-activating protein 1
- Spermatogenesis-associated protein 7 homolog
- Retinal guanylyl cyclase 1
- Aryl-hydrocarbon-interacting protein-like 1
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Membrane frizzled-related protein
- Retinol dehydrogenase 12
Sequence:
MSLIPWLRWNDTPPRLSARTPAEMVLETLMMELAGQMREVERQQRERRSAVRKICTGVDYSWLANTPRPTYDISPGERLQLEDVCAKIHPSYCGPAILRFRQLLAEREPEVQEVARLFRSVLQEALEKMKQEEEAHKLTRQWSLRPRGSLSSFKTRARIAPFASDIRTISEDVERDAPPPPRTWSMPEFRAPQAD
Protein: Staufen double-stranded RNA binding protein 1 (Staufen isoform Stau+I6) (Q9ET50)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Regulator of nonsense transcripts 1
- Fragile X messenger ribonucleoprotein 1
- Cytoplasmic polyadenylation element-binding protein 1
- Endoribonuclease Dicer
- RNA-binding protein FXR1
- Fxr2 protein
- Y box binding protein 1, pseudogene 20
- Y-box-binding protein 1
- Double-stranded RNA-binding protein Staufen homolog 2
- Polyadenylate-binding protein 1
Sequence:
MYKPVDPHSRMQSTYSYGMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKMRPPVKHDATARALRTLQSEPLPERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFESFPLTQVARESGPPHMKNFVTRVSVGEFVGEGEGKSKKISKKNAARAVLEQLRRLPPLPAVERVKPRIKKKSQPTCKLQTAPDYGQGMNPISRLAQIQQAKKEKEPEYMLLTERGLPRRREFVMQVKVGHHTAEGAGTNKKVAKRNAAENMLEILGFKVPQAQPAKPALKSEEKTPVKKPGDGRKVTFFEPSPGDENGTSNKEDEFRMPYLSHQQLPAGILPMVPEVAQAVGVSQGHHTKDFARAAPNPAKATVTAMIARELLYGGTSPTAETILKSNISSGHVPHGPRTRPSEQLYYLSRAQGFQVEYKDFPKNNKNECVSLINCSSQPPLVSHGIGKDVESCHDMAALNILKLLSELDQQSTEMPRTGNGPVSACGRC
Protein: Troponin C, slow skeletal and cardiac muscles (TN-C) (P19123)
Organism: Mus musculus (Mouse)
Function: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
Interaction partners:
- Troponin I, cardiac muscle
- Troponin T, cardiac muscle
- Troponin I, fast skeletal muscle
- Troponin I, slow skeletal muscle
- Troponin T, slow skeletal muscle
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Troponin C, skeletal muscle
- Myosin-7
- Troponin T, fast skeletal muscle
- Myosin light chain 3
Sequence:
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKMMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Protein: Beta-1,4-glucuronyltransferase 1 (EC 2.4.1.-) (I-beta-1,3-N-acetylglucosaminyltransferase) (N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase) (Poly-N-acetyllactosamine extension enzyme) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1) (L7YAI7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE, during synthesis of phosphorylated O-mannosyl glycan (By similarity). Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:O43505, ECO:0000250|UniProtKB:Q8BWP8}; Single-pass type II membrane protein. Note=Localizes near the trans-Golgi apparatus. {ECO:0000250|UniProtKB:O43505}.
Interaction partners:
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannose kinase
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Xylosyl- and glucuronyltransferase LARGE1
- Xylosyl- and glucuronyltransferase LARGE2s
- Protein O-mannosyl-transferase 1
- Fukutin.
- Ribitol-5-phosphate transferase
- Protein O-mannosyl-transferase 2
Sequence:
MHFSKKCSVFKVVLSALLIVALLQLLYLSFLSKLHGKQQRYKYSELFGSKKNANQGEKNPRREHLRYSLSTGGIFDGSGQYRVYKNLIKSDFSTNQKPGADPRSHHLALATHTTINNLHHLESLLERWKNPISVAIFANGEDVKFATAIIYALSLFCPQVQALVDFHLVCHSGEMATFPDQDREHFVGLQEMGCPAVFAKLESHRDKYKNYAIGSNVSYPNNLLRNVARGGTDAAYILVIDIDMIPSANLHHQFVTMLMKREPAADEVLVLPAFEIRHIRKMPASKPELVQLYQVGEVRPFYDELCSRCQAPTNYSLWVNLASKSSGPLEVSYTINWVDPWEPFYIGARSVPLYDESFRQYGFNRISQACELHIAGYRFSVVSNAFLLHKGFKVQGEFHSRKDEENRKNRILFRSFKESLKAKYPTSPRRC
Protein: Suppressor of organelle fusion 1 (Q23533)
Organism: Caenorhabditis elegans
Function: Together with sorf-2 negatively regulates the levels of phosphatidylinositol 3-phosphate (PtdIns3P) to enable the conversion of early endosomes to late endosomes. Binds to sorf-2 and the sorf-1-sorf-2 complex likely acts through bec-1, a non-catalytic subunit of phosphatidylinositol 3-kinase (PI3K), to suppress PI3K activity, thereby negatively regulating endosomal PtdIns3P levels.
Subcellular location: Early endosome {ECO:0000305|PubMed:26783301}. Late endosome {ECO:0000305|PubMed:26783301}. Cytoplasm {ECO:0000269|PubMed:26783301}.
Interaction partners:
- Suppressor of organelle fusion 2
- SAC domain-containing protein
- Vacuolar protein sorting-associated protein 18 homolog
- Myotubularin-related protein 5
- UV radiation resistance-associated gene protein-like
Sequence:
MSHVSNSTDEVVRNYLAAKSMVTSLKAFDQESSFAKEANYQVDRCIDEMTDAIDKHDVDTLCAMWESWNARVFHSLDTEGIKQAQCYEASAYRLFLVRCVQKKNISKCNEFFRKMSSLTLNNPQWADWFAFPYNHHAKDTEPFRKYFDKTWIEIYYVSLHNFLSTSLANVSPSVIGTIVEGIARDPTGNDHVDFDEDLIDDFAVIAQCSAPVKRGHSKPSLRNLLKSLTSSKKPSPSTD
Protein: Siderophore iron transporter ARN1 (Ferrichrome permease) (P38731)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the transport of siderophore ferrichrome and so has a role in iron homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12721368}; Multi-pass membrane protein {ECO:0000269|PubMed:16847258}. Endosome membrane {ECO:0000269|PubMed:10748025}; Multi-pass membrane protein {ECO:0000269|PubMed:16847258}.
Interaction partners:
- Iron transport multicopper oxidase FET3
- Plasma membrane iron permease
- Facilitator of iron transport 2
- Facilitator of iron transport 3
- mRNA decay factor CTH2
- Iron-regulated transcriptional activator AFT1
- Ferric/cupric reductase transmembrane component 1
- Facilitator of iron transport 1
- Copper-transporting ATPase
- Ferric/cupric reductase transmembrane component 2
Sequence:
MESVHSRDPVKEEKKHVFMGMEHELNPETHNDSNSDSYGLPQLSEKYNALRQNRSLIIQQTEIIGSAYNKWYLQAILLLSAFICGYGYGLDGNIRYIYTGYATSSYSEHSLLSTINVINAVVSAASQIIYARLSDVFGRLYLFISAVILYVVGTIIQSQAYDVQRYAAGAIFYNAGYVGVILILLIILSDFSSLKWRLLYQFVPTWPFIINTWIAGNITSRANPVVNWSWDVGMWAFIFPLSCVPIVLCMLHMQWRARKTPEWHALKGQKSYYQEHGFIKILKQLFWMLDVVGVLLMGCSLGCILVPLTLAGGVKTTWNDSRLIGPFVLGFVLIPILWIWEYRFARDPILPYRLVKDRAVWSSMGISFLIDFIYYMAADYLYTVMIVAVNESVKSATRIATLSSFVSTVASPFFALLVTRCTRLKPFIMFGCALWMVAMGLLYHFRGGSQSHSGIIGALCVWGVGTTLFTYPVTVSVQSAVSHENMATVTALNYTLYRIGSAVGSAVSGAIWTQTLYKQILKRMGDVALATTAYESPYTFIETYTWGTPQRNALMNAYKYVQRLETIVALVFCVPLIAFSLCLRDPKLTDTVAVEYIEDGEYVDTKDNDPILDWFEKLPSKFTFKRE
Protein: cAMP-activated global transcriptional regulator Vfr (P55222)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Global cAMP-dependent transcriptional regulator that controls virulence gene expression by distinct cAMP-dependent and -independent mechanisms, which allow to fine tune its virulence program in response to specific host cues or environments. Controls the expression of many regulatory targets including type II, type III and type IV secretion systems, flagellar-mediated motility, and quorum sensing systems. Transcriptional control is exerted by binding to a well-characterized consensus site (5'-ANWWTGNGAWNYAGWTCACAT) within target promoters. Directly binds to the toxA upstream region to regulate exotoxin A production, to the lasR gene promoter to activate the las quorum-sensing system or to the exsA promoter to regulate type III secretion system. Autoregulates as well its own expression.
Interaction partners:
- CyaB
- Adenylate cyclase
- Probable transcriptional regulator
- Response regulator GacA
- Cyclic AMP
- Transcriptional activator protein LasR
- RNA polymerase sigma factor RpoD
- HTH-type transcriptional regulator ExsA
- Scaffold protein FimL
- histidine kinase
Sequence:
MVAITHTPKLKHLDKLLAHCHRRRYTAKSTIIYAGDRCETLFFIIKGSVTILIEDDDGREMIIGYLNSGDFFGELGLFEKEGSEQERSAWVRAKVECEVAEISYAKFRELSQQDSEILYTLGSQMADRLRKTTRKVGDLAFLDVTGRVARTLLDLCQQPDAMTHPDGMQIKITRQEIGRIVGCSREMVGRVLKSLEEQGLVHVKGKTMVVFGTR
Protein: Prune exopolyphosphatase 1 (A0A3B3ITN0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEDYLQGCRAALQESRPLHVVLGNEACDLDSTVSALALAFYLAKKVHIPESILIFRDEIDLHALYQAGQLTLILVDHHILSKSDTALEEAVAEVLDHRPIEPKHCPPCHVSVELVGSCATLVTERILQGAPEILDRQTAALLHGTIILDCVNMDLKIGKATPKDSKYVEKLEALFPDLPKRNDIFDSLQKAKFDVSGLTTEQMLRKDQKTIYRQGVKVAISAIYMDLEAFLQRSNLLADLHAFCQAHSYDVLVAMTIFFNTHNEPVRQLAIFCPHVALQTTGQSLAMLPRLVSNSWTQVIHQPQLPRVLELQICEVLERSHSPPLKLTPASSTHPNLHAYLQGNTQVSRKKLLPLLQEALSAYFDSMKIPSGQPETADVSREQVDKELDRASNSLISGLSQDEEDPPLPPTPMNSLVDECPLDQGLPKLSAEAVFEKCSQISLSQSTTASLSKK
Protein: Protein SPEAR2 (SPL-like, EAR-containing protein 2) (TCP interactor containing EAR motif protein 4) (F4IGU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Adapter-like transcriptional repressor recruiting TPL/TPR corepressors to inhibit TCP transcription factors (By similarity). May be involved in leaf development.
Interaction partners:
- Protein SPEAR1
- Protein SPEAR3
- Homeobox-leucine zipper protein ATHB-21
- Homeobox-leucine zipper protein ATHB-53
- Homeobox-leucine zipper protein ATHB-40
- Transcription factor TCP18
Sequence:
MCSNNNTSSGSYGELQLHDESSGSCRKKQKKDKVRRRGPGVAELEKIRLQEEYKPPLSSSPSLPNIDHHHHTLFAPASSVYDLVMTSPNFSFPEKLASTLPVFPISYGSLIPPAPIFQRSQHSLMMNLPNPSPGAGRFYQFIEPPSNQRSCVDSVSQFLEEENKKIFTAKKRPWPFLTDTTKPSVGPTTTSTIIRPDATQNRSMGITPVQETGTTTSNPIAIDSPTSIPRHYPRFIPLGLQYEQQQQKLKDLDETMQWRSKKPFYSFIPSGDPSNDDQEQRPCDLFGSAADHGIDLNLKL
Protein: 2Fe-2S ferredoxin (P0A9R4)
Organism: Escherichia coli (strain K12)
Function: Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.
Interaction partners:
- Co-chaperone protein HscB
- Chaperone protein HscA
- Iron-sulfur cluster assembly scaffold protein IscU
- Protein IscX
- Cysteine desulfurase IscS
- Iron-binding protein IscA
- Iron-sulfur cluster assembly protein CyaY
- HTH-type transcriptional regulator IscR
- Uncharacterized ferredoxin-like protein YfaE
- Protein SseB
Sequence:
MPKIVILPHQDLCPDGAVLEANSGETILDAALRNGIEIEHACEKSCACTTCHCIVREGFDSLPESSEQEDDMLDKAWGLEPESRLSCQARVTDEDLVVEIPRYTINHAREH
Protein: Inhibitor of growth protein 5 (Inhibitor of growth family member 5) (Q9VJY8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Enok complex which has a histone H3 acetyltransferase activity.
Subcellular location: Nucleus {ECO:0000255|RuleBase:RU361213, ECO:0000269|PubMed:27198229}. Chromosome {ECO:0000250|UniProtKB:Q8WYH8}.
Interaction partners:
- Chromatin modification-related protein MEAF6
- histone acetyltransferase
- Bromodomain-containing protein homolog
- histone acetyltransferase
- SAGA-associated factor 29kDa
- Transcriptional adaptor 3, isoform C
- Transcriptional adapter 2b
- Protein chiffon
- Histone acetyltransferase
- Histone deacetylase HDAC1
Sequence:
MSSAIYLENYLDGLESLPTELERNFKLMRKLDDRAQTAMKSIDSHAKDFMRKLGENGAMSEDERRERQEDIKALFGKAKEYSDDKVQLAIQTYELVDKQIRRLDNDLARFEGEIQEKASSTRAKSEEVVAKKGRKKTKDSKTTGKKKKSASSDEETGRGNNQSNANSSVNSSSNAGQGSKKKKSKVNQEKETRKGGAQKKTVEVDDSEKESCHTAATHPSDVMDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVGLTTKPKGKWFCPKCTQDRKKK
Protein: Flagellar motor protein (Q0PBH3)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
- Flagellar motor proton channel
- histidine kinase
- Chemotaxis protein
- Flagellar motor switch protein FliG
- Flagellar M-ring protein
- Flagellar hook-associated protein 1
- Flagellar basal-body rod protein FlgC
- Flagellar protein FliL
- Flagellar secretion chaperone FliS
- Flagellar hook-associated protein 2
Sequence:
MAKKHKCPECPAGEKWAVPYADFLSLLLALFIALWAISKTNPAKVEALKTEFVKIFDYTSTQTVKEESKTQEKYKGAAKEESDELKSLKQMTMTQQETIKRLQAALDQSDNQVALNLPSKVEFERGSAQIVSADIQDYLKRMAELTTYLPPQAKIEIRGYTDNSDSIIRSYELAYQRAENVLKYFIEGGANLKNISIKSYGLNNPINGNPQTLENNRVEIYFKVDTADTSTQKSVLELINKIGTKAP
Protein: Delta-aminolevulinic acid dehydratase (EC 4.2.1.24) (Q8IL68)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- hydroxymethylbilane synthase
- Ferrochelatase
- 5-aminolevulinate synthase
- Ornithine aminotransferase
- serine C-palmitoyltransferase
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen oxidase
- coproporphyrinogen oxidase
Sequence:
MLKSDVVLLLYILIINLICCLNGNSKKRAYILNTPKSSNCKRSSFRRWNNPVNNNNSQILSKNEGSIEDVYNKKISGRCNIKNFSKDINNNIYIETNRRERRIKRNKYLLSLYNNTNIKTSNFIYPLFIHEEDVEKKHTQLEGIYTYNVDGIIKEIEECIKLNIHHFMFFPVIREENKTVYCEESYNENSYFCKTISRIKEKFSDDIIVYTDVALDPYNIYGHDGIYDDNKKEILNDITVHTLVKQSLCLAKSGADVVCPSDSMDKRIELIRKNLDFHNFRDILILSYTCKYSSSMYKPFRSILNSNILKNFVKNKQSYQHDFNSYMDLNNVDKHIIEGADIIMVKPSMFYLDIIHKIKNRIKDDVQIPIAVYNVSGEYMMIKNYVKYLNEDINYENEIITELFKSYLRAGANIIITYFAKQYGLYMKKLYDKNIIIDDNSNNNFNIELTL
Protein: Oligodendrocyte-myelin glycoprotein (P23515)
Organism: Homo sapiens (Human)
Function: Cell adhesion molecule contributing to the interactive process required for myelination in the central nervous system.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Reticulon-4 receptor
- Myelin-associated glycoprotein
- Reticulon-4
- Tumor necrosis factor receptor superfamily member 19
- Tumor necrosis factor receptor superfamily member 16
- Protein EVI2A
- Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
- Protein EVI2B
- Transforming protein RhoA
- Rho GDP-dissociation inhibitor 1
Sequence:
MEYQILKMSLCLFILLFLTPGILCICPLQCICTERHRHVDCSGRNLSTLPSGLQENIIHLNLSYNHFTDLHNQLTQYTNLRTLDISNNRLESLPAHLPRSLWNMSAANNNIKLLDKSDTAYQWNLKYLDVSKNMLEKVVLIKNTLRSLEVLNLSSNKLWTVPTNMPSKLHIVDLSNNSLTQILPGTLINLTNLTHLYLHNNKFTFIPDQSFDQLFQLQEITLYNNRWSCDHKQNITYLLKWMMETKAHVIGTPCSTQISSLKEHNMYPTPSGFTSSLFTVSGMQTVDTINSLSVVTQPKVTKIPKQYRTKETTFGATLSKDTTFTSTDKAFVPYPEDTSTETINSHEAAAATLTIHLQDGMVTNTSLTSSTKSSPTPMTLSITSGMPNNFSEMPQQSTTLNLWREETTTNVKTPLPSVANAWKVNASFLLLLNVVVMLAV
Protein: La ribonucleoprotein 4 (X6RLN4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
EVKGLFKSENCPKVISCEFAHNSNWYITFQSDTDAQQAFKYLREEVKTFQGKPIMARIKAINTFFAKNGYRLMDSSIYSHPIQTQAQYASPVFMQPVYNPHQQYSVYSIVPQSWSPNPTPYFETPLAPFPNGSFVNGFNSPGSYKTNAAAMNMGRPFQKNRVKPQFRSSGGSEHSTEGSVSLGDGQLNRYSSRNFPAERHNPTVTGHQEQTYLQKETSTLQVEQNGDYGRGRRTLFRGRRRREDDRISRPHPSTAESKAPTPKFDLLASNFPPLPGSSSRMPGELVLENRMSDVVKGVYKEKDNEELTISCPVPADEQTECTSAQQLNMSTSSPCAAELTALSTTQQEKDLIEDSSVQKDGLNQTTIPVSPPSTTKPSREPRKLSYAEVCQKPPKEPSSVLVQPLRELRSNVVSPTKNEDNGAPENSVEKPHEKPEARASKDYSGFRGNIIPRGAAGKIREQRRQFSHRAIPQGVTRRNGKEQYVPPRSPK
Protein: Peripheral myelin protein 22 (PMP-22) (Growth arrest-specific protein 3) (GAS-3) (P16646)
Organism: Mus musculus (Mouse)
Function: Might be involved in growth regulation, and in myelinization in the peripheral nervous system.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q01453}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q01453}.
Interaction partners:
- Laminin subunit beta-2
- Integrin beta-1
- Laminin subunit alpha-3
- Integrin alpha-7
- Laminin subunit beta-1
- Integrin beta-4
- Laminin subunit gamma-2
- Laminin subunit alpha-1
- Tetraspanin-32
- Integrin beta-8
Sequence:
MLLLLLGILFLHIAVLVLLFVSTIVSQWLVGNGHTTDLWQNCTTSALGAVQHCYSSSVSEWLQSVQATMILSVIFSVLALFLFFCQLFTLTKGGRFYITGFFQILAGLCVMSAAAIYTVRHSEWHVNTDYSYGFAYILAWVAFPLALLSGIIYVILRKREL
Protein: PDZ domain-containing protein (Q8MNT0)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein espinas
- LIM domain-containing protein unc-97
- Zyxin
- PDZ and LIM domain protein Zasp
- LIM domain-containing protein unc-95
- CRE-UNC-96 protein
- Protein vav
- CTD small phosphatase-like protein 1
- Zinc finger protein unc-98
- Alpha-actinin, sarcomeric
Sequence:
MENDYAVKVAKYPPNLGSDYPEDEFGPGAKMLRGPGQKSSDPFQFVAVNKGGDEMAESAKSTLQMAQQQKAQREKMLQGQKQTLKFDDCEPWQENLDTWRKKRKEKFGDRATSDTTVPETTIHRRSEEYTSYQPRKSKEEILQVNSASRPALPRQHSASTVSPLQSSSDELNNDSGIDNRTVGSPSTSEFSPRSTDLFVSPKSIIDEEPPHHPPPPPPVEEKLDQVLIPLKLSRGQDYAPIYRSLEQDTYYDQSPSESEKDEDLGLTNTKRYTENFRSVEKNQYMPVMSARVEATFKQPPPREGVKPFVSRAAQDITHNGESKVENIDLTIELNREQKATVTATKYPRTDFIMEDYHRPQTQILAPAPKKPNSTTRIYHAVDIPFDESPASYYPKQNNGYQRQRRYSASSASKQDGMFTLNVIMGSQPVHKGMGFSTVKRDERVIVESVIVGSPADKAGLLVGDTILSINGEEMSDKYQSGVTRILHEAARVGEADVLILRAPVPAPMLSKQMSTSSSNSSNYDKARSVFTENKSFDSYAEFKRKHTRTSRDSNSSNATRSSRDFNSLPRGTTAQSSLDRKRDTSLSSYRTAKDNFNSSSNRSSGRSEYGDYRVSNYQEKNAPGRLTDFVPEVDRRLSRREQSEEIYSRSQRDEEPRTIRNYHLSNENIARTNLNYDGRRDSEEESTTTTLKRTTLPRSGTAQWKNEYSDGEEVTEKLPVTSRDSSPLRSALKKSSHNYYHQSSDPVAPPPRRYYSTESLQLPKTSSYQRYSEEEDEEIEETYSSMRRHRQEIPRHVDEFHTVGSYGVMPQRSRSQQPARLPRYDSVPDDVDEVSGVSHRFYDRSGNHVRAPRERIHDIQIQRDYGDRAPSRDLDFVRNTYKWEEQLEDTKVTTTTKIYEKESRDWRDVINQQRQAAPGNSADRRGIAATSSSLSNLPSYINRRMEKEREREIEYRRDREYSMPPADPPVITEKYERDEYSRVEERTYPVPVARNKMRREETQMQSSLQQMHSQSSQKDDSVVAVSGKHRCAHCNEELGRGAAMIVESLNLFYHLACFKCYVCKTSLGSGATGADVRVRDGRLHCQTCYSNDRVQLSKV