wanglab/gogpt-training-data huggingface dataset:
Protein: Slit homolog 2 protein precursor (Slit2) (Q9DE36)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MFVLKSVVLCALLCGAGAQSCPSQCSCSGTAVDCHGQSLRSVPRNIPRNVERLDLNANNLTKITKADFAGLKNLRVLQLMENKISSIERGAFQDLQELERLRLNRNNLQVLPELLFLGTTKLFRLDLSENQIQGIPRKAFRGSTEIKNLQLDYNQISCIEDGAFRALGDLEVLTLNNNNISRLSVASFNHMPKLRTFRLHSNNLLCDCNVAWLSDWLRQRPRLGLYTQCMAPPSLRGHNIAEVQKKEFMCTGPQSHSSCSVLQCPELCTCSNNVVDCRGKGLTEIPTNLPETITEIRLEQNSIKIIPAGAFAPYKRLRRIDLSNNQITELASDSFQGLRSLNSLVLYGNKITELPKGLFDGLFSLQLLLLNANKINCLRVDSFQDLQNLNLLSLYDNKLQTIAKGTFSSLRAIQTLHLAQNPFMCDCHLKWLADYLQDNPIETSGARCTSPRRLANKRIGQIKSKKFRCSGVEDYRSKLGGDCFADLACPEKCRCEGTTVDCSGQKLTKIPDHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINLSNNKITDIEEGTFEGASGVNELILTSNRLEGVHYSMLKGLGGLRTLMLRSNRISCVNNGSFTGLSSVRLLSLYDNLITSMSPGAFDTLHSLSTLNLLANPFNCNCHLAWLGEWLRKKRIVTGNPRCQSPYFLKEIPIQDVAVQDFACEEGNDENSCSPLARCPAECSCLDTVVRCSNKGLKVLPKGIPRDVTELYLDGNEFTQVPLELSNYKHLTLIDLSNNQISTLSNHSFSNMSELLTLILSYNRLRCIPAKAFDGLKSLRLLSLHGNDIAVIPDGAFKDLSSLSHLALGANPLYCDCHMQWLSDWVKSGYKEPGIARCTGPGDMTDKLLLTTPSKKFTCTGPVDVSILAKCNPCLSNPCKNDGTCSNHPVDFYRCTCPYGFKGQDCEEPIHACISNPCQNGGTCHLKDGEENTHWCVCPEGFEGDECEINIDDCEDNDCENNSTCVDGINNYTCLCSPEYTGELCEDKLDFCASELNLCQHDSKCILTAKGFMCECTPGYTGEHCEVDFDDCEDNKCKNGAQCIDAVNGYTCVCPEGYSGLFCEFSPPMVLPRTSPCDHYDCANGAQCVVKDTDPVCQCLPGYEGVHCERLVSVNFINRESFLQIPSNLITEQANISLQIATDEDNGVLLYKGDNEHIAVELYRGRLRVSYDSGSYPPSAIYSVETINDGSFHVVELVAKDQSLSLSIDGGSPKSINTANSPSPVPSPAPLYLGGLPQQSGLASLRQGSGRNGSSFHGCIRNLYINDQLQDLTQFLLQEGVVPGCQPCQRSMCAHGQCHATGQSSFSCECEAGWTGPLCDQQVNNPCDGNKCIHGSCMAINSYSYSCRCLPGFAGVLCDEEEQLSPCQYIACKYGRCRVSGLGKAYCECNSGYTGQSCDREMACRGERVRDHYQTQQGYAACQSTEKVSRLECRGSCGDGTSCCAPLRSKRRKYTFQCTDGSSFVQEVEKVVKCGCTKCPS
Protein: Cell adhesion molecule Dscam1 (Down syndrome cell adhesion molecule homolog) (Q0E9H9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Cell projection, neuron projection {ECO:0000269|PubMed:10892653, ECO:0000269|PubMed:17482551}. Cell projection, axon {ECO:0000269|PubMed:10892653, ECO:0000269|PubMed:15339648, ECO:0000269|PubMed:17482551}. Perikaryon {ECO:0000269|PubMed:15339648, ECO:0000269|PubMed:17482551}. Cell projection, dendrite {ECO:0000269|PubMed:15339648}. Secreted {ECO:0000269|PubMed:16109846}.
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVAQYYEADVNKEHVIRGNSAVIKCLIPSFVADFVEVVSWHTDEEENYFPGAEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVSSSPPKINALTYKPNIVESMASTAILCPAQGYPAPSFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPQVLPFSFGESAADVGDIASANCVVPKGDLPLEIRWSLNSAPIVNGENGFTLVRLNKRTSLLNIDSLNAFHRGVYKCIATNPAGTSEYVAELQVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Anaphase-promoting complex subunit 2 (Cyclosome subunit 2) (Q8H1U5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication.
Subcellular location: Nucleus {ECO:0000269|PubMed:14508008}.
Interaction partners:
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 27 homolog B
- Ubiquitin-conjugating enzyme E2 22
Sequence:
MEALGSSDCNLEILETLSDDAIQEITESYDGFFTTVESLIAGTGDSLVEDEFVSHVYCLCKYGLDSLVRDHFLRSLEQAFEKGGASSFWQHFDAYSEKKHHNYGEEIQIVLCKALEEISIEKQYHEKCLSIVVHALQSFKEQSSDDRQNSDTERVHLFSRFQSMLSSTLMTTLPQHFPEILHWYFKERLEELSAIMDGDGIEEQEDDCMDLDEKLRYKNGEMDVDEGCSQGKRLGHDKLVKNIGKVVRDLRSIGFTSMAENAYASAIFLLLKAKVHDLAGDDYRTSVLESIKEWIQTVPLQFLNALLSYLGDSVSYGTTSSGLTSPLACCPSPSFSRVVTPSEGIVRWKLRLEYFAYETLQDLRIAKLFEIIVDYPESSPAIEDLKQCLEYTGQHSKLVESFISSLKYRLLTAGASTNDILHQYVSTIKALRAIDPAGVFLEAVGEPIRDYLRGRKDTIKCIVTMLTDGSGGNANGSGNPGDSLLEELMRDEESQENVGFDDDFHTDDKQAWINASRWEPDPVEADPLKGSLSQRKVDILGMLVDIIGSKEQLVNEYRVMLAEKLLNKTDYDIDTEIRTVELLKIHFGEASMQRCEIMLNDLIDSKRVNTNIKKASQTGAELRENELSVDTLTSTILSTNFWPPIQDEPLELPGPVDKLLSDYANRYHEIKTPRKLLWKKNLGTVKLELQFEDRAMQFTVSPTHAAIIMQFQEKKSWTYKDLAEVIGIPIDALNRRVNFWISKGVLRESTGANSNSSVLTLVESITDSGKNEGEELLTGEEEGETSIASVEDQLRKEMTIYEKFIMGMLTNFGSMALERIHNTLKMFCVADPSYDKSLQQLQSFLSGLVSEEKLEFRDGMYLLKK
Protein: V-type proton ATPase subunit H (V-ATPase subunit H) (Nef-binding protein 1) (NBP1) (Protein VMA13 homolog) (V-ATPase 50/57 kDa subunits) (Vacuolar proton pump subunit H) (Vacuolar proton pump subunit SFD) (Q9UI12)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:O46563}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit F
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit d 1
Sequence:
MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRSPEEKQEMLQTEGSQCAKTFINLMTHICKEQTVQYILTMVDDMLQENHQRVSIFFDYARCSKNTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQKLRGSGVAVETGTVSSSDSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQQVRYNALLAVQKLMVHNWEYLGKQLQSEQPQTAAARS
Protein: COX17 cytochrome c oxidase assembly homolog (S. cerevisiae) (Cox17 protein) (Cytochrome c oxidase copper chaperone) (Q66I53)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
- Cytochrome c oxidase assembly protein COX11
- Mitochondrial intermembrane space import and assembly protein 40
- Copper transport protein ATOX1
- Protein SCO2 homolog
- Coiled-coil-helix-coiled-coil-helix domain-containing 4b.
- Cytochrome c oxidase assembly protein COX19
- ATPase copper-transporting alpha.
- Protein SCO1 homolog, mitochondrial
- Cytochrome c oxidase assembly factor 6
- Mitochondrial import inner membrane translocase subunit Tim10
Sequence:
MSSLSAASVEASPAAIEGAEQKKPLKPCCACPETKKERDACIIEKGEESCTHLIEAHKECMRALGFNI
Protein: CAAX prenyl protease 1 homolog (EC 3.4.24.84) (Farnesylated proteins-converting enzyme 1) (FACE-1) (Q9XVE5)
Organism: Caenorhabditis elegans
Function: Proteolytically removes the C-terminal three residues of farnesylated proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P47154}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12487630}.
Interaction partners:
- CAAX prenyl protease 2
- Protein farnesyltransferase subunit beta
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein-S-isoprenylcysteine O-methyltransferase
- Protein-S-isoprenylcysteine O-methyltransferase
- GrpE protein homolog
- 10 kDa heat shock protein, mitochondrial
- Probable 26S proteasome non-ATPase regulatory subunit 9
- Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein
- GTP cyclohydrolase 1
Sequence:
MDASCLFKALLATNWALFLWDQYITFRQYKAHKNAVKRPNEVKELIGEEDYKKARDYKIDNHLFGFFHSWFNQLLLTAQLIGGYYPFLWYATASYPLHVAVFLSINSIIETIIDLPWDLYSTFIIEDAHGFNKQTIGFYFVDKIKKMLVGFALTMPIVYGIEWIIVNGGPYFFVYIWLFVSVVVLLLMTIYPTFIAPLFDKYFPLPDGDLKTKIEQLAASLSYPLTELYVVNGSKRSAHSNAYMYGFWKNKRIVLYDTLLSGAEKEKVHELYVAAGEKIEETENDKKRGMNNDEVVAVLGHELGHWALWHTLINLVITEVNLFFSFAVFGYFYKWEALYQGFGYHDTPPVIGMMLIFQFVLALYNQLASIGMVIHSRSAEFGADEFAANLGHGENLIGALTKLGVDNLSMPINDSLYSWCTHTHPPVVERVAAVRAFQAKNK
Protein: Isoprenyl synthetase (Q8KFR6)
Organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Interaction partners:
- Isopentenyl-diphosphate delta-isomerase
- Isoprenyl transferase
- Polyprenyl synthetase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Geranylgeranyl diphosphate reductase
- Phytoene desaturase
- DprA/SMF protein, putative DNA processing factor
Sequence:
MSSPITQAQVESKYRQYHAKINEALAACFPKEKPATLYDPARYILEGKGKRIRPFLTLLAAEAVSGKSDNALGVALGIEVLHNFTLMHDDIMDQADLRHGRPTVHKQWNVNAAILSGDMMIAYAYELALKAISSRHAEIIHIFNDANITICEGQALDMELEQRKDVTIADYLDMISKKTGRLISAALEAGGVAGDGTPEQIAALVTFGEKIGRAFQIQDDYLDIMAGDGKSGKVPGGDVINGKKTWLLLRSLELAEGADRELLQSIFDNNGTSPDNVPAVKAIFEKCGVLNETRAKINEDTEAALAALDALPFEEGRGYLRGFANILMKRDF
Protein: DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (P63037)
Organism: Mus musculus (Mouse)
Function: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis.
Subcellular location: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}.
Interaction partners:
- Heat shock 70 kDa protein 1B
- Heat shock cognate 71 kDa protein
- Heat shock protein HSP 90-alpha
- Heat shock 70 kDa protein 1A
- Heat shock protein HSP 90-beta
- Heat shock protein 105 kDa
- Stress-induced-phosphoprotein 1
- Heat shock 70 kDa protein 1-like
- DnaJ homolog subfamily B member 1
- Endoplasmic reticulum chaperone BiP
Sequence:
MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
Protein: Beta-glucuronidase (Q5ZIA4)
Organism: Gallus gallus (Chicken)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MAAAAPCGVAGQCRLQLLVLVAAAAAGRAATAVRGGMLYPRESPSRELKELGGIWSFRADFSPGRDAGFEQRWYRQPLRQTGPVVDMPVPASFNDITQDPHLENYIGWVWYEKEVLIPQRWLQDDLSTRVVLRFGSAHYYSIVWVNGVQVVEHEGGHLPFEADISRIVQRSPGVLCRITVALNNTLTPHTLPPGSIQYMNDRTRYPKNYFVQNTRFDFFNYAGIHRPVVLYTTPSVYIDDITVTTTSSESVAMVRYQISVVGSELYSLSLSLRDQEGKVVATGDGPSGELKVPNPNLWWPYLMHENPGYRYFLEVKMQAQASGVPQEDIYTLPVGIRTVHVTSTQFLINGKPFYFHGVNKHEDADIRGKGLDWALIVKDFNLLRWLGANSFRTSHYPYAEEIMDLCDTYGIVVIDECPGVGIKMPESFGNKSLQHHLVVMEELIRRDKNRPSVVMWSVANEPASELPPAAYYFKTLIAHTKALDPSRPVTFVSDTNYAVDHGAPYVDVICVNSYFSWYHDPGHLEVIPLQLTAQFENWYKTYQKPIIQSEYGADSIPGLHSDPPAMFSEEYQKAMLKEYHSVFDKKRKEYVIGELIWNFADFMTDQGTTRVLGNKKGIFTRQRQPKSAAFVLRERYWKIANESSCVPPIIKSHILFL
Protein: Protein mono-ADP-ribosyltransferase PARP15 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 7) (ARTD7) (B-aggressive lymphoma protein 3) (Poly [ADP-ribose] polymerase 15) (PARP-15) (Q460N3)
Organism: Homo sapiens (Human)
Function: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. Acts as a negative regulator of transcription.
Subcellular location: Nucleus {ECO:0000305|PubMed:16061477}.
Interaction partners:
- E3 ubiquitin-protein ligase DTX3L
- Protein mono-ADP-ribosyltransferase PARP16
- Poly [ADP-ribose] polymerase 1
- Ganglioside-induced differentiation-associated protein 2
- Protein mono-ADP-ribosyltransferase PARP9
- Protein mono-ADP-ribosyltransferase PARP3
- Protein mono-ADP-ribosyltransferase PARP4
- Interferon-induced helicase C domain-containing protein 1
- Protein mono-ADP-ribosyltransferase PARP6
Sequence:
MAAPGPLPAAALSPGAPTPRELMHGVAGVTSRAGRDREAGSVLPAGNRGARKASRRSSSRSMSRDNKFSKKDCLSIRNVVASIQTKEGLNLKLISGDVLYIWADVIVNSVPMNLQLGGGPLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPITSPLQEVHFLVYTNDDEGCQAFLDEFTNWSRINPNKARIPMAGDTQGVVGTVSKPCFTAYEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNIFYDSMKKRDLSASLNFQSTFSMTTCNLPEHWTDMNHQLFCMVQLEPGQSEYNTIKDKFTRTCSSYAIEKIERIQNAFLWQSYQVKKRQMDIKNDHKNNERLLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTPPPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITFTA
Protein: LP10995p (Male-specific RNA 98Cb) (Sperm protein) (Q24404)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- AT13777p
- Cytosol aminopeptidase
- LD30122p
- Male-specific sperm protein Mst84Dc
- Cytosol aminopeptidase
- GEO12122p1
- Male-specific sperm protein Mst84Dd
- Cytosol aminopeptidase
- Testis-enriched HMG-box-containing protein 2, isoform B
- AT14585p
Sequence:
MCSPCGPCSPCDPCCGPFECSPKCYNAAQLEALPQCAPRIPPPFPKCITVQQPPRMICKKRVVFTEKIVPEPMVVNRCRQITIPKVVDATRVIKVPKLIWVSQMVREPRVIYYPSMIPDPYVVCYPKRVCEPREVCQSILCQPKPQTIDIPPPREYCCYPNGPINYKPSAACPPCPIGPCAPGGPCCPLPCFSTNQYPVAEGRCGPCGPCGPGCGPCGPCGPWGPGCGPCGPCGPCGPFGPGCGPCGPCGPCGPGPCGFGPCGPC
Protein: RAN GTPase-activating protein 2 (AtRanGAP2) (RanGAP2) (Q9M651)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.
Subcellular location: Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Localized in patchy areas at the nuclear envelope of interphase cells. During mitosis, associates with mitotic spindles at the anaphase. Associated to the microtubular phragmoplast and the surface of the daughter nuclei at the telophase.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- RAN GTPase-activating protein 1
- Ran-binding protein 1 homolog b
- Ran-binding protein 1 homolog a
- F2O10.4 protein
- GTP-binding nuclear protein Ran-3
- GTP-binding nuclear protein Ran-2
- GTP-binding nuclear protein Ran-4
- GTP-binding nuclear protein Ran-1
- Ran-binding protein 1 homolog c
Sequence:
MADILDSRPHAFSIKLWPPSLPTRKALIERITNNFSSKTIFTEKYGSLTKDQATENAKRIEDIAFSTANQQFEREPDGDGGSAVQLYAKECSKLILEVLKKGPVAKVAARELISEDSVSPRETFFDISKGKRAFIEAEEAEELLKPLKEPGNAYTKICFSNRSFGLGAARVAEPILASLKDQLKEVDLSDFVAGRPELEALEVMNIFSDALQGSILSSLNLSDNALGEKGVRAFGALLKSLSSLEELYLMNDGISKEAAQAVSELIPSTENLRVLHFHNNMTGDEGALAIAEVVKRSPLLENFRCSSTRVGSKGGIALSEALEHCTHMEKLDLRDNMFGTEAGVSLSKTLSSFKHMTELYLSYLNLEDEGAIAIVNALKESASPIEVLEMAGNDITVEAASAIAACVAAKQDLNKLNLSENELKDEGCVQIANCIEEGHSKLQYIDMSTNYIRRAGARALAHVVVKKEAFKLLNIDGNIISEEGIEELKEIFKKSPELLGALDENDPDGEEDDDDEEDEEDEENEGNGNGELESKLKNLEVNQED
Protein: COX3 mRNA-specific translational activator PET494 (P07390)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the expression of the mitochondrial gene for cytochrome c oxidase subunit III (COX3).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:8389363}; Peripheral membrane protein {ECO:0000269|PubMed:8389363}.
Interaction partners:
- Protein PET111
- Cytochrome c oxidase subunit 3
- Protein PET54
- Protein PET122
- Mitochondrial COX1 translation regulator PET309
- Cytochrome B translational activator CBS2
- Mitochondrial translation factor 2
- Protein MSS51, mitochondrial
Sequence:
MHLKKGKRSISTVWRLLWKRFYSVNSKTNMHFSRSRKKPVTNFTRTNGLLLSCNGDTFPYLRTLWRYFNAPGNLMFVTTNIVAFMGIVTYNTLVTISSERAFEEQMMAAQVSLAKQREELETTALSLPRDIELRGEEDDIKWEQPDVAHVREDPLVEEQNAKLDTPIKQYTLGDLILNKRENVTDYDSQRAKASIFHMLYAYMLYRDVIQPTTMTQNNNSEEWRREVELLTKGKEVQGTHRRIDVFYDLWNKNFDKIVTSPEKVQNFQLPNWSKYPTILKFICTELHDNSLKTLGEFKQFYGKVRSNEVKKLLGLWLYDHSFLFPHNIYDNRTEEDFYDILINDSMQDNRIFQKYSSIVMNPYNERTQLFFPNVNSPSVNKPVPSISLETYTRLLKGYINLQETGCKYDYNDNIFKLISILKLNCFLQRNKKKHAGPTVRILLPRDEDRSQILGTISQAEKRTCYQILSKNRDVVALLKRISDIQADSS
Protein: Immunoglobulin heavy constant gamma 1 (Ig gamma-1 chain C region) (Ig gamma-1 chain C region EU) (Ig gamma-1 chain C region KOL) (Ig gamma-1 chain C region NIE) (P01857)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen. Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells.
Subcellular location: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIIPDYRNMIGQGA
Protein: SURF1-like protein (Q5APC5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363076}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363076}.
Interaction partners:
- Cox11p
- Cox15p
- Activator of stress genes protein 1
- Protoheme IX farnesyltransferase, mitochondrial
- Msu1p
- Cu-binding protein
- Cytochrome c oxidase subunit 1
- Cytochrome c
- Cytochrome c oxidase subunit 2
Sequence:
MFNIHTTRLVKLKPIRLLQFNRSVKTLTMDWKPMKAVPGNLRTLEHQSKMPTIRRVLLGLMYAMPIISFALGCWQVHRLQWKTDLIAKCENNLAAPVIPELPPNLDPSVIADFEYRRFKCRGRFDYDQEMFLGPRLKDGELGYLVVTPFIRKNGGDPILIERGWISKDKVVPSSRSSGYLSHLARPQGEIEIEALFRVMPKKSFLQLEHEQGSRLFHVPDVPAMAKQSGSLPIYCQMIYDLHDHIDWRKDENGQQQKPSVISSLLFSKKKDSDAAFIATNANKDETLQFQEFEFVNEGVPIAAKPFIKFSNNHLQYLITWFGLSIGSTVLLLFSIYKSKQFATAEQLLAAKRKDMQKKA
Protein: Putative antitoxin VapB10 (P9WLZ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Putative antitoxin component of a possible type II toxin-antitoxin (TA) system. The cognate toxin is VapC10.
Interaction partners:
- Ribonuclease VapC10
- RNA polymerase-binding transcription factor CarD
Sequence:
MKRTNIYLDEEQTASLDKLAAQEGVSRAELIRLLLNRALTTAGDDLASDLQAINDSFGTLRHLDPPVRRSGGREQHLAQVWRATS
Protein: O-methyltransferase gsfC (EC 2.1.1.-) (Griseofulvin synthesis protein C) (D7PI17)
Organism: Penicillium aethiopicum
Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of griseofulvin, an important antifungal drug that has been in use for a long time for treating dermatophyte infections. The first step of the pathway is the formation of the heptaketide backbone by gsfA which is initiated by priming with acetyl-CoA, followed by sequential condensations of 6 malonyl-CoA units. The resulting benzophenone can undergo a spontaneous dehydration to form norlichexanthone. However, the true precursor for the griseofulvin biosynthesis is not norlichexanthone, but the heptaketide benzophenone that is O-methylated at 3-OH by gsfB to produce griseophenone D which is further methylated at 9-OH by gsfC to yield griseophenone C. Griseophenone C is then substrate of halogenase gsfI which is responsible for the regio-specific chlorination at the C13 position to form griseophenone B. The cytochrome P450 gsfF catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A which is further methylated at 5-OH by gsfD to yield dehydrogriseofulvin. Finally, gsfE performs stereospecific reduction of enone 18 of dehydrogriseofulvin to afford the final product griseofulvin.
Interaction partners:
Sequence:
MTLDQISRIQALVAEIADLSQTFEGPSERFMVDGLPFLRKSEELVTLVQSPAEHATSLIIKTMETAVIRTLLSLNVLQTIPTTGSITLQSLAVATETQESLLERLLRVVTKTGFIIRENGGYSHSHTSLAYAGPLGALFAPCYDEGIRALVRLPEYLSVKDKEEAKNARYSLFTWNEGQEGKATFEILSTMPARTEGIHTLAMNVQHLRPYTGFFDYSKLVSEDRERPVFVDVGGGNGHVIKEILQAFPQIRPEQCVLEDRAETLELARTTGLLPAGVQLLEHDYLTRQPVSNAKAYHLRAVAYNLGDAELVQLLKQIVPVMGADSKVLIAENILFDDNSTVFSTVSDMIMLGIGGKERTEQNFREVLYEAGLTIEGIHRAPGLEYGIMEASLATS