wanglab/gogpt-training-data huggingface dataset:
Protein: L-type lectin-domain containing receptor kinase S.1 (LecRK-S.1) (EC 2.7.11.1) (Q9M9E0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Subcellular location: Cell membrane {ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSWQWRRRQWPSPLLLILIVLHLVSSSSAIDFLYNSFSSVTNRTDVILIEDSRVESTVISLINDSDPLSFGRVFYPQKLTIIPDPTRNPTRLSSFSTSFVFSILPDISTSPGFGLCFVLSNSTSPPNAISSQYFGLFTNATVRFNAPLLAVEFDTGRNSEVNDIDDNHVGIDLNNIESTTSVTAGYYDSVNGSFVRFNMRNGNNVRAWIDFDGPNFQINVSVAPVGVLRPRRPTLTFRDPVIANYVSADMYAGFSASKTNWNEARRILAWSLSDTGALREINTTNLPVFFLENSSSSLSTGAIAGIVIGCVVFVALIGFGGYLIWKKLMREEEEEEIEEWELEFWPHRFSYEELAAATEVFSNDRLLGSGGFGKVYRGILSNNSEIAVKCVNHDSKQGLREFMAEISSMGRLQHKNLVQMRGWCRRKNELMLVYDYMPNGSLNQWIFDNPKEPMPWRRRRQVINDVAEGLNYLHHGWDQVVIHRDIKSSNILLDSEMRGRLGDFGLAKLYEHGGAPNTTRVVGTLGYLAPELASASAPTEASDVYSFGVVVLEVVSGRRPIEYAEEEDMVLVDWVRDLYGGGRVVDAADERVRSECETMEEVELLLKLGLACCHPDPAKRPNMREIVSLLLGSPQEDLLTGLTPAAAAADSTAAHA
Protein: Peptide transporter PTR2 (Peptide permease PTR2) (P32901)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Uptake of small peptides.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Homeobox protein CUP9
- Oligopeptide transporter 2
- Oligopeptide transporter 1
- E3 ubiquitin-protein ligase UBR1
- SPS-sensor component PTR3
- SPS-sensor component SSY1
- General amino acid permease AGP1
- Leu/Val/Ile amino-acid permease
- General amino-acid permease GAP1
- Allantoate permease
Sequence:
MLNHPSQGSDDAQDEKQGDFPVIEEEKTQAVTLKDSYVSDDVANSTERYNLSPSPEDEDFEGPTEEEMQTLRHVGGKIPMRCWLIAIVELSERFSYYGLSAPFQNYMEYGPNDSPKGVLSLNSQGATGLSYFFQFWCYVTPVFGGYVADTFWGKYNTICCGTAIYIAGIFILFITSIPSVGNRDSAIGGFIAAIILIGIATGMIKANLSVLIADQLPKRKPSIKVLKSGERVIVDSNITLQNVFMFFYFMINVGSLSLMATTELEYHKGFWAAYLLPFCFFWIAVVTLIFGKKQYIQRPIGDKVIAKSFKVCWILTKNKFDFNAAKPSVHPEKNYPWNDKFVDEIKRALAACKVFIFYPIYWTQYGTMISSFITQASMMELHGIPNDFLQAFDSIALIIFIPIFEKFVYPFIRRYTPLKPITKIFFGFMFGSFAMTWAAVLQSFVYKAGPWYNEPLGHNTPNHVHVCWQIPAYVLISFSEIFASITGLEYAYSKAPASMKSFIMSIFLLTNAFGSAIGCALSPVTVDPKFTWLFTGLAVACFISGCLFWLCFRKYNDTEEEMNAMDYEEEDEFDLNPISAPKANDIEILEPMESLRSTTKY
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (Oligosaccharyl transferase subunit DAD1) (Defender against cell death 1) (DAD-1) (P61804)
Organism: Mus musculus (Mouse)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2
Sequence:
MSASVVSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG
Protein: Neural F box protein NFB42 (Q9Z1X8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDGDGDPESVSHPEEASPEEQPEEAGARASAEEEQPREEEEEETEAVEYLAELPEPLLLRVLAELPATELVQACRLVCLRWKELVDGAPLWLLKCQQEGLVPEGSADDERDHWQQFYFLSKRRRNLLRNPCGEEDLEGWCDVEHGGDGWRVEELPGDSGVEFTHDDSVKKYFASSFEWCRKAQVIDLQAEGYWEELLDTTQPAIVVKDWYSGRTDAGSLYELTVRLLSEHEDVLAEFNTGQVAVPEDGSWMEISHTFTDYGPGVRYVRFEHGGQDSVYWKGWFGARVTNSSVWVEP
Protein: Retrotransposon hotspot (RHS) protein 1 (B2ZWB7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFSKRCFALPLCGSLRRYSTRPYFCPPLSVTLPLWSAHRNIFRYSPTLYFSGKETNCPKWVLGSNVKNVLLEDYEGLRDMTLHEFLLNKFLNTYNTRNVAMDVFVKNPRRYIVDAEVLENIQDTDEFKTVRTVIDLSEKVNYLIGKEISTLRQWEEKGKGEIRDFVGPVVGGRLDAAVITAKEERERAAQTAGGAVEIKGVYESIYNATWSYVESGHREEPLGMKVFNGRPQHMWTKEEVDISHTPETMNEPLPRHGNLEIAVLTSQVGWPCTFFKADPKDYDMNSRKEVGHVFMTDVYIRREVMRVWYKVEQRLNWWLMGEVPIKATPYVLIGTPGIGKSFSVGSFLLYKLLHYEASQLQIIIYVVEGKAHVFRKPKGGRPGYVTFYKSYDDAFVTINAITRASSNTEDIKGYLIFDVGKGHPAPMSLPYGFTGIALSSPDVKQFHEWAKQNTALSIYINCDTLEDLEAIHISRWGKIAPAYGWNPSDAKEKIETEWQKIESRIRIVGPPLRHIVGSDSFKNQFDAMKDPITDIQVERMEDYINIFRHRTRWRTAKPSHKLVQVVRVKEDNDDGDQYCCKPLSSYTGEAILDQLKPWLLKNHTLATGLLSNRAVVALLFEQNGAGAMLHEDALIELAKGLRSLPFVKNEIQQSVLQVLKKPKLAEPLIDAPEDARVITGAEIEYMKLYKPQSSNFPVVDAFFFVENPKTFVGLQHTISERHPCSVGGLVKMKKYLRSYFKHWDNFSNDMVWEIIYVQRVDSEIFTRPQKCERSTGKGKHNNEDEEKFWREKVRQFSVSLNGHITALYVELQVRGNNNNRVNNRGGNIA
Protein: Protein Vpu (U ORF protein) (Viral protein U) (P05923)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo.
Subcellular location: Host membrane {ECO:0000255|HAMAP-Rule:MF_04082}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04082}.
Interaction partners:
Sequence:
MQPIQIAIAALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDIDDL
Protein: Zinc finger CCCH domain-containing protein 4 (AtC3H4) (Q9LNV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-processing-splicing factor 8A
- Pre-mRNA-splicing factor SPF27 homolog
- DExH-box ATP-dependent RNA helicase DExH12
- AT3G18790 protein
- Cell division cycle 5-like protein
- Pre-mRNA-processing factor 19 homolog 1
- Tetratricopeptide repeat
- Protein pleiotropic regulatory locus 1
- Pre-mRNA-processing factor 19 homolog 2
- Pre-mRNA-splicing factor SYF2
Sequence:
MAHRILRDHEADGWERSDFPIICESCLGDNPYVRMTKANYDKECKICTRPFTVFRWRPGRDARYKKTEICQTCCKLKNVCQVCLLDLEYGLPVQVRDTALNISTHDSIPKSDVNREYFAEEHDRKARAGLDYESSFGKMRPNDTILKLQRTTPYYKRNRAHVCSFFIRGECTRGAECPYRHEMPETGELSQQNIKDRYYGVNDPVAMKLLGKAGEMGTLESPDDESIKTLYVGGLNSRILEQDIRDQFYAHGEIESIRILADKACAFVTYTSREGAEKAAQELSNRLVINGQRLKLTWGRPKPDQDGANQQGGVAHSGLLPRAVISQQHNQPPPMQQYYMHPPPANQDKPYYPSMDPQRMGAVISTQEAGGSSTENNGASSSSYMMPPHQSYPPPPYGYMPSPYQQQYPPNHHHQPSPMQHYAPPPAAYPYPQQPGPGSRPAPSPTAVSAISPDSAPAGSGAPSGSSQQAPDVSTATGSSQ
Protein: Protein APCDD1-like (Adenomatosis polyposis coli down-regulated 1 protein-like) (Q8NCL9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPAAMLPYACVLVLLGAHTAPAAGEAGGSCLRWEPHCQQPLPDRVPSTAILPPRLNGPWISTGCEVRPGPEFLTRAYTFYPSRLFRAHQFYYEDPFCGEPAHSLLVKGKVRLRRASWVTRGATEADYHLHKVGIVFHSRRALVDVTGRLNQTRAGRDCARRLPPARAWLPGALYELRSARAQGDCLEALGLTMHELSLVRVQRRLQPQPRASPRLVEELYLGDIHTDPAERRHYRPTGYQRPLQSALHHVQPCPACGLIARSDVHHPPVLPPPLALPLHLGGWWVSSGCEVRPAVLFLTRLFTFHGHSRSWEGYYHHFSDPACRQPTFTVYAAGRYTRGTPSTRVRGGTELVFEVTRAHVTPMDQVTTAMLNFSEPSSCGGAGAWSMGTERDVTATNGCLPLGIRLPHVEYELFKMEQDPLGQSLLFIGQRPTDGSSPDTPEKRPTSYQAPLVLCHGEAPDFSRPPQHRPSLQKHPSTGGLHIAPFPLLPLVLGLAFLHWL
Protein: Diguanylate cyclase/phosphodiesterase (Q3KK31)
Organism: Pseudomonas fluorescens (strain Pf0-1)
Interaction partners:
Sequence:
MSLFKQLLIAICLFLVVAFTGSFMVSLESSRTQYVNQLRSHAQDAATALALSLTPNIDDPAMVELLVSSIFDSGYYSSIRVVDLKTDQTIVERNGIPAVTNVPDWFVKLIGLEPAGGDALVSRGWEQAARVEVVSHPMFALAKLWQSALGSLGWLLVCGAVSAVLGALLLRRQLKPLDYMVKQSHAIARREFLSLPDLPRTPELRRVVLAMNQMVEKLKALFQEQAERSEKLRTESYQDNLTGLANRRYFEMQLNARVSNPEQASSGYLLLLRVKDLAGLNQRLGGQRTDELLKAVGEQLSRECAKYPETQNLVTRIRGGEFAVLAPGMTREEALQLAQSLDSALSSLYATGATDVAAVASIGLAPFAHGDSPQAVLSLGDQALAQAEGQGEQNWACLDQSLVADVGDDHHAWHRLLDQALNQRRFELFFQPVVAAQDTQLVLHYKVLSRLLDEQGQTIPAGRFLPWLERFGWTARLDRLMLERVLEQMAGHEESLALNLSSATLADPQALNKVFEILRAHSNLGARLTLEIGEEQLPEQAVLEQLTRRLRELGFSLSLQRFGGRFSMIGNLARLGLAYLKIDGSYIRAIDQESDKRLFIEAIQRAAHSIDLPLIAERVETEGELSVIREMGLYGVQGQLFGEPKPWG
Protein: Fibronectin type-III domain-containing protein (Q8C352)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRPLPLWLPSLLLCGLGAAASSPDSFSQLAAPLNPRLHLYNDEQILTWEPSPSSNDPRPVVYQVEYSFIDGSWHRLLEPNCTDITETKCDLTGGGRLKLFPHPFTVFLRVRAKRGNLTSKWVGLEPFQHYENVTVGPPKNISVTPGKGSLVIHFSPPFDVFHGATFQYLVHYWEKSETQQEQVEGPFKSNSIVLGNLKPYRVYCLQTEAQLIL
Protein: Ubiquitin fusion degradation protein 1 (C0H540)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Thioredoxin-like protein, putative
- Nuclear protein localization protein 4, putative
- Polyubiquitin binding protein, putative
- RING-type E3 ubiquitin transferase
- UBX domain-containing protein, putative
- Cell division cycle protein 48 homologue, putative
- Putative cell division cycle ATPase
- Ubiquitin regulatory protein, putative
Sequence:
MFRIVLYILAICLYSININYAKKITGKTYLTNQLAKGILNKTKKPYSNIFTRLKNYTLKSIYKTKLLSYVNDLNNINLGNDKNEFYLITLPLCEKFNPFVGTFCHNNIQYSDKASLPIFIYDILLNKHIEVPWNFVIEKVNVKTSENYKNVCMPNITHFNNYKNINNLNRVFINVLDFKAKKNFIFLPTWVMKSLNLNCFDVIRLRFVKLETASSVVLQPHEKKFFDLENPKKILEEKLRYYSCITRNSTISIKHDDVVYYFDVIRIDSEKKKDTEVASIQDADVIFDFVKEKYNS
Protein: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC 2.5.1.58) (EC 2.5.1.59) (CAAX farnesyltransferase subunit alpha) (FTase-alpha) (Ras proteins prenyltransferase subunit alpha) (Type I protein geranyl-geranyltransferase subunit alpha) (GGTase-I-alpha) (P49354)
Organism: Homo sapiens (Human)
Function: Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.
Interaction partners:
- Protein farnesyltransferase subunit beta
- Geranylgeranyl transferase type-1 subunit beta
- Protein farnesyltransferase subunit beta
- Geranylgeranyl pyrophosphate synthase
- CAAX prenyl protease 2
- Farnesyl pyrophosphate synthase
- CAAX prenyl protease 1 homolog
- Dehydrodolichyl diphosphate synthase complex subunit DHDDS
- All trans-polyprenyl-diphosphate synthase PDSS1
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
Sequence:
MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ
Protein: Protein TIFY 11A (Jasmonate ZIM domain-containing protein 5) (Q9LDU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Repressor of jasmonate responses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Transcription factor MYC2
- Coronatine-insensitive protein 1
- Protein TIFY 5A
- Protein TIFY 9
- Protein TIFY 5B
- AFP homolog 2
- Transcription factor MYC3
- Protein TIFY 7
- Protein TIFY 6B
- Protein TOPLESS
Sequence:
MSSSNENAKAQAPEKSDFTRRCSLLSRYLKEKGSFGNIDLGLYRKPDSSLALPGKFDPPGKQNAMHKAGHSKGEPSTSSGGKVKDVADLSESQPGSSQLTIFFGGKVLVYNEFPVDKAKEIMEVAKQAKPVTEINIQTPINDENNNNKSSMVLPDLNEPTDNNHLTKEQQQQQEQNQIVERIARRASLHRFFAKRKDRAVARAPYQVNQNAGHHRYPPKPEIVTGQPLEAGQSSQRPPDNAIGQTMAHIKSDGDKDDIMKIEEGQSSKDLDLRL
Protein: Killer cell lectin-like receptor, subfamily A, member 15 (Lectin-related NK cell receptor Ly49) (Q9JHH8)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTYSMVRFHKSAGLQKQVRPEETKGPREAGYRRCSFHWKFIVIALGIFCFLLLVAVSVLAIKIFQYDQQKKLQEILNHHNNCSNMQSDINLKDELLKNKSIECDLLESLNRDQNRLYNKTKTVLDSLKHTGRGVKVYWFCYGMKCYYFVMDRKPWSRCKQSCQNSSLFLLKIDDEDELKFLQLVVPSDSCWIGLSYDNKKKDWAWIENGPSKLALNTTKYNIRDGGCMFLSKTRLDNNYCDQSFICICGKRLDKFPH
Protein: Microtubule-associated proteins 70-3 (F4IPB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEEGGYAFEVNNGRPTASEFGTTARISSPSLTMSSSFREGGGGGGSKGLTRRRSMKPSFDADNEFITLLHGSDPVKVELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMAAQFAAEATLRRVHAAQKDDDMPPIEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSALAKASMVDDLQNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQRKFQEMNEERRILDRELARAKVSASRVATVVANEWKDGSDKVMPVKQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFQLRLRVLEESLRGPSSSGNRSTPEGRSMSNGPSRRQSLGGADIIPKLTSNGFFSKRSPSSQFRSLNASTSTILKHAKGTSRSFDGGSRSLDRSKVLTNEPRSKFPLNQSSEGTSGGGSPNSTKQGDSEKAAGTNNDSVPGVLHDLLQKEVITLRKAANDKDQSLRDKDEAIEMLAKKVETLTKAMEVEAKKMRREVAAMEKEVSAMRVDNKGSDSRTRRHSTNSKGASTTAQLLSGSRGSGRMGMTRSTQ
Protein: Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 7 (AthCYSTM7) (O22802)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance to abiotic stress.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29272523}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASYHVSHDSYQSPGPSPLYQPIIEAPPPPYPPTRTRYQDYYGGYGQPHPPPLRPYRSDHEYYGDGEYVGCFPFLRSCLTTLCCCWFVEQCCFRSRY
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q5U118)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPQMRAAAAEAVAAGSANGQPLVKIGHYLLGATLGTGTFGKVKIGEHQITRVKVAVKILNRQKIKSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMIMEYVSGGELFDYIVKHGKLQEHQARRFFQQIISGVDYCHRHMIVHRDLKPENLLLDHNMHVKIADFGLSNMMLDGEFLRTSCGSPNYAAPEVISGKLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFRKIKSGIFPIPEYLNKQVVNLVCQMLQVDPLKRANIEEIKKHEWFQKDLPAYLFPSSIEQDSNVIDTYAVAEVCTKFGVKETEVHNSLLSGDPHDQLAIAYHLIIDNKRFADDAANQINEINNFFVAGSPPPPPPPPVPQSSMDHQAPLATVTVGGGTSASSGTATPVPPVAGGTPSSTIPIRPHPERIAPMRDRQLAMSVQTSGGGAFPEKTARGGTPIKRAKWHLGIRSQSKPNDIMLEVYRAMKALSYEWKIINPYHVRVRRQNVKTGKFSKMSLQLYQVDAKSYLLDFKSLTNDEVEQGDDVIMESLTPPPLSVSGVMPLQPTGHHIMEFFEMCAALIIQLAR
Protein: Carbonic anhydrase 9 (EC 4.2.1.1) (Carbonate dehydratase IX) (Carbonic anhydrase IX) (CA-IX) (CAIX) (Membrane antigen MN) (P54/58N) (Renal cell carcinoma-associated antigen G250) (RCC-associated antigen G250) (pMW1) (Q16790)
Organism: Homo sapiens (Human)
Function: Catalyzes the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions).
Subcellular location: Nucleus {ECO:0000269|PubMed:8486430}. Nucleus, nucleolus {ECO:0000269|PubMed:8486430}. Cell membrane {ECO:0000269|PubMed:8486430}; Single-pass type I membrane protein {ECO:0000269|PubMed:8486430}. Cell projection, microvillus membrane {ECO:0000269|PubMed:8486430}; Single-pass type I membrane protein {ECO:0000269|PubMed:8486430}. Note=Found on the surface microvilli and in the nucleus, particularly in nucleolus.
Interaction partners:
- Hypoxia-inducible factor 1-alpha
- Endothelial PAS domain-containing protein 1
- Monocarboxylate transporter 5
- Monocarboxylate transporter 4
- Solute carrier family 2, facilitated glucose transporter member 1
- Aryl hydrocarbon receptor nuclear translocator
- 1,25-dihydroxyvitamin D
- DnaJ homolog subfamily B member 7
- Prolyl hydroxylase EGLN3
- von Hippel-Lindau disease tumor suppressor
Sequence:
MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTVEAPGDPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGRVIEASFPAGVDSSPRAAEPVQLNSCLAAGDILALVFGLLFAVTSVAFLVQMRRQHRRGTKGGVSYRPAEVAETGA
Protein: IGF like family receptor 1 (K7ESC2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGPGRCLLTALLLLALAPPPEASQYCGRLEYWNPDNKCCSSCLQRFGPPPCPDYEFRENCGLNDHGDFVTPPFRKCSSGQCNPDGAELCSPCGGGAVTPTPAAGGGRTPWRCRERPVPAKGHCPLTPGNPGAPSSQER
Protein: Actiflagelin (C0HKZ8)
Organism: Walterinnesia aegyptia (Desert black snake)
Function: Unknown. In vitro, this toxin activates sperm motility when tested on OF1 male mice.
Subcellular location: Secreted {ECO:0000269|PubMed:29410678}.
Interaction partners:
Sequence:
MECYKCGVSGCHLKITCSAEEKFCYKWRDKISNERWLGCAKTCTEENTWRVYNSCCTTNLCNP
Protein: SMC5-SMC6 complex localization factor protein 1 (Ankyrin repeat domain-containing protein 32) (BRCT domain-containing protein 1) (Smc5/6 localization factor 1) (Q9BQI6)
Organism: Homo sapiens (Human)
Function: Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks. Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions.
Subcellular location: Nucleus {ECO:0000269|PubMed:25931565}. Cytoplasm {ECO:0000250|UniProtKB:Q8R3P9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8R3P9}. Note=Relocalizes with RAD18 to nuclear foci in response to DNA damage. Colocalizes with RAD18 in the nucleus and to centrosomes (By similarity). Associates with chromatin (PubMed:25931565). Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner (PubMed:25931565). {ECO:0000250|UniProtKB:Q8R3P9, ECO:0000269|PubMed:25931565}.
Interaction partners:
- SMC5-SMC6 complex localization factor protein 2
- Structural maintenance of chromosomes protein 5
- E3 ubiquitin-protein ligase RAD18
- Cell division control protein 45 homolog
- 26S proteasome non-ATPase regulatory subunit 12
- TP53-binding protein 1
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM5
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosomes element 4 homolog A
Sequence:
MEDGTPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETTYEWGYKIEKDSRYSPQMQSAPKRWREELKRTGAPGAFHRWKVVLLVRTDKRSDSLIRVLEAGKANVILPKSSPSGITHVIASNARIKAEKEKDNFKAPFYPIQYLGDFLLEKEIQNDEDSQTNSVWTEHSNEETNKDFRKDAGFLEMKGALRETMYRTQKEMQNHEDVNVGSILIQHHKKEKFSGSSKDLKFVKMRNTFGSHTYENQKEIKKKDEDIQRSYTLRRKRKKGKESNCKKGVEHEKIKSTLRRHIYNRDQKEMKNSIFAEYAKESKAMAIKTDVDVVEIKNTLRKHIYRAQAVRYNCIRIDKQPVYNVEVKNAEFPRGVLNLIESLIEGHFFKEAIEELSTLQAHYIPPVCVLHALLENVLQDNIDTFSGRYFHILSALLHLHPPWKSPAMSRYYLELFQCPTCMKGAWSLVEVLIRSCLFNESFCHQISENIGSKVLHLTLLKFFFNLIESEVQHLSQKLYDWSDSQNLKITGKAMLLEIFWSGSETSGLLTKPVNMLLEWTIYSHKEKFKSNDVFKHELAYLLAGILGAAIDYWIFLGLKMGRNVMRHMSDDLGSYVSLSCDDFSSQELEIFICSFSSSWLQMFVAEAVFKKLCLQSSGSVSSEPLSLQKMVYSYLPALGKTGVLGSGKIQVSKKIGQRPCFDSQRTLLMLNGTKQKQVEGLPELLDLNLAKCSSSLKKLKKKSEGELSCSKENCPSVVKKMNFHKTNLKGETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQHGGPVLLQQRNAKGELPLDYVVSPQIKEELFAITKIEDTVENFHAQAEKHFHYQQLEFGSFLLSRMLLNFCSIFDLSSEFILASKGLTHLNELLMACKSHKETTSVHTDWLLDLYAGNIKTLQKLPHILKELPENLKVCPGVHTEALMITLEMMCRSVMEFS
Protein: Thebaine synthase 2 (EC 4.2.99.24) (A0A2U9GGW3)
Organism: Papaver somniferum (Opium poppy)
Function: Catalyzes the formation of thebaine from (7S)-salutaridinol 7-O-acetate at the expense of labile hydroxylated by-products, which are preferentially produced by spontaneous allylic elimination. No visible activity toward (7S)-salutaridinol (at pH 7).
Interaction partners:
Sequence:
MAPLGVSGLVGKLSTELEVDCDAEKYYNMYKHGEDVKKAVPHLCVDVKIISGDPTSSGCIKEWNVNIDGKTIRSVEETTHDDETKTLRHRVFEGDVMKDFKKFDTIMVVNPKPDGNGCVVTRSIEYEKTNENSPTPFDYLQFGHQAIEDMNKYLRDSESN
Protein: Sphingoid long chain base kinase 5 (LCB kinase 5) (EC 2.7.1.91) (Sphinganine kinase 5) (Q06147)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively. Redundant to LCB4, is only responsible for few percent of the total activity. Involved in the biosynthesis of sphingolipids and ceramides. Involved in heat-induced transient cell cycle arrest. Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling. Involved in heat-stress resistance.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12493772}; Peripheral membrane protein {ECO:0000269|PubMed:12493772}.
Interaction partners:
- Sphingosine-1-phosphate lyase
- Dihydrosphingosine 1-phosphate phosphatase YSR3
- Dihydrosphingosine 1-phosphate phosphatase LCB3
- Alkaline ceramidase YPC1
- Alkaline ceramidase YDC1
- Sphingoid long chain base kinase 4
- Ceramide synthase LAG1
- Ceramide synthase LAC1
- 3-ketodihydrosphingosine reductase TSC10
- Sphingolipid C4-hydroxylase SUR2
Sequence:
MTLKPSKRRKGRSRHSRKKQITSAILTEEGIMIKAKPSSPYTYANRMADKRSRSSIDNISRTSFQSNISRTSFQSNSDNNSIFETASLISCVTCLSDTDTIDRSETSTTDTSKDDLSANPKLHYPSVNGQLPANTVIPYGRILDARYIEKEPLHYYDANSSPSSPLSSSMSNISEKCDLDELESSQKKERKGNSLSRGSNSSSSLLTSRSPFTKLVEVIFARPRRHDVVPKRVSLYIDYKPHSSSHLKEEDDLVEEILKRSYKNTRRNKSIFVIINPFGGKGKAKKLFMTKAKPLLLASRCSIEVVYTKYPGHAIEIAREMDIDKYDTIACASGDGIPHEVINGLYQRPDHVKAFNNIAITEIPCGSGNAMSVSCHWTNNPSYSTLCLIKSIETRIDLMCCSQPSYAREHPKLSFLSQTYGLIAETDINTEFIRWMGPARFELGVAFNIIQKKKYPCEIYVKYAAKSKNELKNHYLEHKNKGSLEFQHITMNKDNEDCDNYNYENEYETENEDEDEDADADDEDSHLISRDLADSSADQIKEEDFKIKYPLDEGIPSDWERLDPNISNNLGIFYTGKMPYVAADTKFFPAALPSDGTMDMVITDARTSLTRMAPILLGLDKGSHVLQPEVLHSKILAYKIIPKLGNGLFSVDGEKFPLEPLQVEIMPRLCKTLLRNGRYVDTDFDSM
Protein: Ankyrin repeat domain 6b (Ankyrin repeat domain-containing protein 6b) (F6NJE0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Prickle homolog 2a.
- Prickle homolog 2b
- Prickle homolog 1b
- Prickle homolog 1a
- Axin-1
- T-box transcription factor TBX1
- Vang-like protein 2
- Cadherin EGF LAG seven-pass G-type receptor 1
- Vang-like protein
- Axin-2
Sequence:
MSQRDASCVRALSERLLIASHKGQADHVVQLINRGAKVAITKNGRTPLHLAAYKGHIAVVRILLAAGCDLDIEDDGDQTALHRAAVVGNTDVISALVQEGCALDRQDKDGNTALHEAAWHGFSQTVKLLVKAGANVHAKNKAGNTALHLACQNGHVQSCRVLLLGGSRPDSKNSVGDTCLHVSARYNHVSVIRALLGAICSVTDRNHTGDTALHIAATLNHRKTVRMLLEAGADSRIKNNTGETALDQARENNSPEVALLLTKAPQSFSRGRTVRKRRDKMKTEGRAQSVPRDEMLPRKCDSASPAQDTHGSDGSLRRTDNMFLTEPRTNKNCHRKARDRLSPSDALIHRPNKQSDPKKKSKTERSSPSAVPPPPPHNYKAYQLYTLYRGKDGKIMQAPLNGCRCEPLISKLENQLMATKEEMQSEIHTVQELMNSKIGQMDRKSKHQIRALDKMTLERVSAERIECLHRIDKRAVQERLEAEKRQTSVVKDLKNWCLSKIQSLETRLSGERVDSRLQRSSSLTDTLSDCTPVLEPSRAAPHPSPSAEPTDAGETAAASSCAEDAPARYYVIEVDASADKPSSQNQSAPQSPCIVRPKQRSRACSDPHQLRDESEERSVEPRPAAEHRTIRRHRAKSKPSAQSLTLQTCPAAAEGAFAQERDNMHALEVTQYFFEAVTLQMERWYERKIEETRRQADHRVQADRELLLDRIQHLEDELRLLRMNTQDG