wanglab/gogpt-training-data huggingface dataset:
Protein: Ataxin 7 (A0A2R8YDD6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPPPPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPPLAVPPTSVFSFFPSLSKSKGGSASGSNRSSSGGVLSASSSSSKLLKSPKEKLQLRGNTRPMHPIQQSRVPHGRIMTPSVKVEKIHPKMDGTLLKSAVGPTCPATVSSLVKPGLNCPSIPKPTLPSPGQILNGKGLPAPPTLEKKPEDNSNNRKFLNKRLSEREFDPDIHCGVIDLDTKKPCTRSLTCKTHSLTQRRAVQGRRKRFDVLLAEHKNKTREKELIRHPDSQQPPQPLRDPHPAPPRTSQEPHQNPHGVIPSESKPFVASKPKPHTPSLPRPPGCPAQQGGSAPIDPPPVHESPHPPLPATEPASRLSSEEGEGDDKEESVEKLDCHYSGHHPQPASFCTFGSRQIGRGYYVFDSRWNRLRCALNLMVEKHLNAQLWKKIPPVPSTTSPISTRIPHRTNSVPTSQCGVSYLAAATVSTSPVLLSSTCISPNSKSVPAHGTTLNAQPAASGAMDPVCSMQSRQVSSSSSSPSTPSGLSSVPSSPMSRKPQKLKSSKSLRPKESSGNSTNCQNASSSTSGGSGKKRKNSSPLLVHSSSSSSSSSSSSHSMESFRKNCVAHSGPPYPSTVTSSHSIGLNCVTNKANAVNVRHDQSGRGPPTGSPAESIKRMSVMVNSSDSTLSLGPFIHQSNELPVNSHGSFSHSHTPLDKLIGKKRKCSPSSSSINNSSSKPTKVAKVPAVNNVHMKHTGTIPGAQGLMNSSLLHQVGNGL
Protein: Uncharacterized protein (G8BHR6)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- chitinase
- Flo11 domain-containing protein
Sequence:
MFAILFTFFLFNLISAAPIPAIITRYHTAAPVTQVVTQTTGTTTVWLPPVGIYVLADGSSSTSTVWSGQWNTYPATFTSVLTPDNANTQPDAQPTTAADTTPTPATTTAAAETTANTQPTNEQNGETTPAATTAQPETTSTAAPEQQTNQQTTEQDQPTTEQNQQTQQTSSTTSSNDTPSSSSSSTSETSSSSESSGSLSPPSTIVYSPYADDRSCKSSDEINSDLQLIYNKGIKQIRSYGTDCGSLSTVLSKCNQLGIKVNQGVWVSQDGVDSADDQIDQVIEYGQQNGWDIFNLFTFGNEAINSKYVDVDSLMTKLDSVRTKMRNAGYNGPVTTAEPPATYINYPQLCTDTSMDIVAINPHSYFNEGISPDKAGDYVTTQQSQVAKLCKGKSVWITETGYPSQGATLGLNVPSPKNQEIAIKSILDSTGGDVTILTTYNDFWKDPGPYGIEQYFGTINLFS
Protein: Epoxide hydrolase 2 (EC 3.3.2.10) (G5EDL5)
Organism: Caenorhabditis elegans
Function: Catalyzes the hydrolysis of epoxide-containing fatty acids. Active in vitro against trans-1,3-diphenylpropene oxide (t-DPPO), epoxyeicosatrienoic acids (EETs) including 8,9-EET, 11,12-EET and 14,15-EET and the linoleic acid metabolites 12,13-epoxy-9-octadecenoate (12,13-EpOME) and 9,10-epoxy-12-octadecenoate (9,10-EpOME).
Interaction partners:
- Fatty acid synthase
- L-fucokinase domain-containing protein
- Putative fatty acid elongase 4
Sequence:
MGFFADLFKVVYSTWRQYIYTTGALLTLTWKWFTEGNEYFVEHVYPEPECLKNWNHKFVQLKNIRMHYVEEGPADGDVLLMVHGFPEFWYSWRFQLEHFKHTHRCIAIDMRGYNTTDRPSGISDYNLTHLVEDIRQFIEILELKRVTLAAHDWGAIVCWRVAMLHSNLIDRLVICNVPHPFAFFEVYNMSKEQRNKSWYIYLFQSQYIPEIAMRSNKMKMLEAMFRGSKAGIRNSENFTDEDMLAWKHVFSQPGGTTGPLNYYRDLFNAPAIPRKLQIVQPKVLILWGDEDAFLDKKGAELSVQFCRDCRVQMIRGASHWVQQDQPQLVNVYMEQFMNEDSYRPIGEIKTFKSHL
Protein: Bistable expression regulator, BexR (Q9I150)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transcriptional regulator
- HTH-type transcriptional regulator NmoR
- Probable hydrolase
- Probable transcriptional regulator
- Peroxiredoxin
- Ferredoxin
- GbuR
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
Sequence:
MSLRFDDIEAFLNVAELNSVTSAAERMSLSKSVISKRVSDLERRLGVRLLYRTTRNVEPTEAGHFFYKAAKASLQELNNAAEIVALRENDLCGELRIVTPMSFGTLWLSPIIADFMSQHPRLEIVLQMDDRLTDFEKEGYDLSIRVTRLDDSSLIARPLANSQRVVCCSPDYAERHGTLDTLEQLMQHECLGYNNATPSQVWTFEPAFPGAKPRAVSPRGRFSSNNGQAMRDAALRGQGLALLPLFIVAEDLKNGRLVDAAPGLRPLDDVIYAMYSRAAAMSPKVKAFIQHLQQALSIPPWGNG
Protein: Distal-less homeobox 1 (J3KP55)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MTMTTMPESLNSPVSGKAVFMEFGPPNQQMSPSPMSHGHYSMHCLHSAGHSQPDGAYSSASSFSRPLGYPYVNSVSSHASSPYISSVQSYPGSASLAQSRLEDPGADSEKSTVVEGGEVRFNGKGKKIRKPRTIYSSLQLQALNRRFQQTQYLALPERAELAASLGLTQTQ
Protein: Arogenate dehydratase/prephenate dehydratase 2, chloroplastic (AtADT2) (AtPDT2) (EC 4.2.1.51) (EC 4.2.1.91) (Q9SSE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine. Dehydratase that uses arogenate and prephenate as substrates. Utilzes more efficiently arogenate than prephenate. Required for chloroplast division prior to ARC5, but in an ARC3- and ARC6-dependent manner, especially involved in the Z-ring formation.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19136569, ECO:0000269|PubMed:30252596}. Note=Observed in chloroplast stromules, and as a ring around the equatorial plane of dividing plastids, thus colocalizing with FtsZ1 and FtsZ2. {ECO:0000269|PubMed:30252596}.
Interaction partners:
- Arogenate dehydrogenase 2, chloroplastic
- Arogenate dehydrogenase 1, chloroplastic
- Chorismate mutase 1, chloroplastic
- Chorismate mutase 3, chloroplastic
- Chorismate mutase 2
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
- Probable aminotransferase TAT4
- Tyrosine aminotransferase
- Probable aminotransferase TAT1
Sequence:
MAMHTVRLSPATQLHGGISSNLSPPNRKPNNSIVRYGCGSSKRFRIVTVLASLRENDANGRDNSVRAMEVKKIFEDSPLLPKPLSSNQLTESVSNGSRVRVAYQGVRGAYSESAAEKAYPNCEAVPCEEFDTAFEAVERWLVDRAVLPIENSLGGSIHRNYDLLLRHNLHIVGEVKLAVRHCLLANHGVNIEDLRRVLSHPQALAQCENTLTKLGLVREAVDDTAGAAKQIAFENLNDAAAVASEKAAKIYGLNIVAKDIQDDCDNVTRFLMLAREPIIPGTNRLFKTSIVFSLEEGPGVLFKALAVFALRQINLTKIESRPLRKHPLRASGGLKYFDYLFYVDFEASMADEVAQNALRHLEEFATFLRVLGSYPVDTTML
Protein: Myomesin-1 (Myomesin family member 1) (Skelemin) (Q62234)
Organism: Mus musculus (Mouse)
Function: May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. May also contact myosin filaments. Also binds beta-integrins.
Subcellular location: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18177667, ECO:0000269|PubMed:22562206}.
Interaction partners:
- LIM domain-binding protein 3
- Obscurin
- Titin
- Myozenin-2
- Alpha-actinin-2
- Telethonin
- Nebulin-related-anchoring protein
- PDZ and LIM domain protein 3
Sequence:
MSLPFYQRSHQHYDLSYRNKDLRTTMSHYQQEKKRSAVYTHGSTAYSSRSLAARRQESEAFSQASATSYQQQASQTYSLGASSSSRHSQGSEVSRKTASAYDYGYSHGLTDSSLLLEDYSSKLSPQTKRAKRSLLSGEETGSLPGNYLVPIYSGRQVHISGIRDSEEERIKEAAAYIAQKTLLASEEAIAASKQSTASKQSATSKRTTSTLQREETFEKKSRNIAIREKAEELSLKKTLEETQTYHGKLNEDHLLHAPEFIIKPRSHTVWEKENVKLHCSVAGWPEPRLTWYKNQVPINVHANPGKYIIESRYGMHTLEISKCDFEDTAQYRASAMNVQGELSAYASVVVKRYKGELDESLLRGGVSMPLSFAVTPYGYASKFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHFQPEVQWYRNGAPVSPSKWVQPHWSGDRATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVRDADAEIEGAPAAPLDVVSLDANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDTWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKTGIGLPSRVSEPVAALDPAEKARLKSHPSAPWTGQIIVTEEEPTEGVIPGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCDVGAENWQRVNTELPVKSPRFALFDLVEGKSYRFRVRCSNSAGVGEPSETTEVTVVGDKLDIPKAPGKIIPSRNTDTSVVVSWEESRDAKELVGYYIEASVVGSGKWEPCNNNPVKGSRFTCHGLTTAQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIGGGVSPDVWPQLSDTPGGLTDSRGGMNGASPPTSQKDALLGSNPNKPSPPSSPSSRGQKEVSTVSESVQEPLSSPPQEAAPEEEQSQSEPPKKKKDPVAVPSAPYDITCLESFRDSMVLGWKQPDTTGGAEITGYYVNYREVVGEVPGKWREANIKAVSDAAYKISNLKENTLYQFQVSAMNIAGLGAPSTVSECFKCEEWTIAVPGPPHSVKLSEVRKNSLVLQWKPPVYSGRTPVTGYFVDLKEASAKDDQWRGLNEAAIVNKYLRVQGLKEGTSYVFRVRAVNQAGVGKPSDLAGPVVAETRPGTKEVVVSVDDDGVISLNFECDQMTPKSEFVWSKDYVPTEDSPRLEVENKGDKTKMTFKDLGTDDLGTYSCDVTDTDGIASSYLIDEEEMKRLLALSQEHKFPTVPTKSELAVEILEKGQVRFWMQAEKLSSNAKVSYIFNEKEIFEGPKYKMHIDRNTGIIEMFMEKLQDEDEGTYTFQIQDGKATGHSTLVLIGDVYKKLQKEAEFQRQEWIRKQGPHFAEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGFYEVILKDDRGKDKSRLKLVDEAFQDLMTEVCKKIALSATDLKIQSTAEGIRLYSFVCYYLDDLKVNWSHNGTGIKYTDRVKSGVTGEQIWLQINEPTPNDKGKYVMELFDGKTGHQKTVDLSGQAFDEAFAEFQRLKQAAIAEKNRARVLGGLPDVVTIQEGKALNLTCNVWGDPPPEVSWLKNEKPLTSDDHCSLKFEAGKTAFFTISGVSTADSGKYGLVVKNKYGSETSDFTVSVFIPEEELRKGAMEPPKGNQKSK
Protein: Aminoglycoside N(6')-acetyltransferase type 1 (EC 2.3.1.82) (AAC(6')-I) (Aminoglycoside resistance protein) (P10051)
Organism: Citrobacter koseri (Citrobacter diversus)
Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, kanamycin and tobramycin.
Interaction partners:
Sequence:
MNYQIVNIAECSNYQLEAANILTEAFNDLGNNSWPDMTSATKEVKECIESPNLCFGLLINNSLVGWIGLRPMYKETWELHPLVVRPDYQNKGIGKILLKELENRAREQGIIGIALGTDDEYYRTSLSLITITEDNIFDSIKNIKNINKHPYEFYQKNGYYIVGIIPNANGKNKPDIWMWKSLIKE
Protein: Trypanothione synthetase, putative (EC 6.3.1.9) (Q586P2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Trypanothione reductase
- thioredoxin-dependent peroxiredoxin
- Ribonucleoside-diphosphate reductase
- Spermidine synthase, putative
- thioredoxin-dependent peroxiredoxin
- Glutathione peroxidase
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
- Ribonucleoside-diphosphate reductase small chain
Sequence:
MTKSALADTKEEPHVPFGEIQGYTPCGVPAYSNGHDGFFSGERSIDGNLFCGFKYQCVEFARRWLYEAKGLVLPDVNWAAHIFDLTEVHDASTATPVPCVKVSNGTAAKPVADSLLIYAVNEDAPWGHVAVITEVGDKWVRIADQNHRFHKWKGTYSAELLLKHEGGVWTVEDHAAEGIFVPLGWVTFPSRPNRNPKEPLVLHESLYFKQPEKPFLRRVVFTPENRKTDWLDLTNEAEAEFYKTFGKEATRGGVYESCYYLMNRELYLNCVRYGTQLHSFFLEATKQVLESDDKLRRFRIPEEYWPRIRHSWKTQPHAITGRFDFVFDENTQEFKCFEYNADSASTLLECAVIQEKWANSVGLDDNATRSSGKFMPQTLVRAWEMTGLKGRVHFLVDDDGEERYTALYVMEKAREAGIDAKLCVMFDEFHFDEKGAVVDSDGIPVTAVWKTWMWETAISDHQAAREQRGAEWKPTPKDKVRLCDILLGNNWDIRVFEPMWKLIPSNKAILPIIYNNHPDHPAILPASYELTDELRRTGYAKKPIVGRVGRNVTVTEPDGKVLAESDGNFSNRDMVYQQLFRIPKRGDYYAILGGWMLGDTYSGTGVREDKKLITGLESPFGPVRIQM
Protein: Zinc finger protein 691 (Q5VV52)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSLCSPTHSAEMSLFLQGPEEMLPLSSEGSEMGSEKEQSPEPHLPEEGEGGKPWRVDDSEGSWIPPGEKEHGQESLSDELQETHPKKPWQKVTVRARELGDPIAHPRHEADEKPFICAQCGKTFNNTSNLRTHQRIHTGEKPYKCSECGKSFSRSSNRIRHERIHLEEKHYKCPKCQESFRRRSDLTTHQQDHLGKRPYRCDICGKSFSQSATLAVHHRTHLEPAPYICCECGKSFSNSSSFGVHHRTHTGERPYECTECGRTFSDISNFGAHQRTHRGEKPYRCTVCGKHFSRSSNLIRHQKTHLGEQAGKDSS
Protein: Protein kinase C and casein kinase substrate in neurons 3 (A0A0C4DGG1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPEEDAGGEALGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGTVEKGPQYGTLEKAWHAFFTAAERLSALHLEVREKLQGQDSERVRAWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHAARKDEKTAQTRESHAKADSAVSQEQLRKLQERVERCAKEAEKTKAQYEQTLAELHRYTPRYMEDMEQAFETCQAAERQRLLFFKDMLLTLHQHLDLSSSEKFHELHRDLHQGIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRTISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPGSPGTGQDEEWSDEESPRKAATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQ
Protein: 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG) (P62198)
Organism: Rattus norvegicus (Rat)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62195}. Nucleus {ECO:0000250|UniProtKB:P62195}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 10B
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 8
- Proteasome
- 26S proteasome non-ATPase regulatory subunit 6
Sequence:
MALDGPEQMELEEGKAGSGLRQYYLSKIEELQLIVNDKSQNLRRLQAQRNELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK
Protein: SET domain-containing protein (Q57XE0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPVFENKHLLRVLQPPQQLAQNFVAYCKAHQVLTRGLCRVGKTKRGELRGLIANKDIKKDDNIVMLSERACLHPGRALKCERFLAIFPQNVKEMLLQNPLFVQNSRVAERSIIRHNQFLLACYMTYLILRNDENAEGQALKYINFMPRNEGNFEQLISNMNGVLDGAAACQSAQAALSLQFGITQAEVRPLLQWSMAMIFSRMAPIDHRWTLQCAFKNTPFAPAFDIRGPDDDANMVKEPIAFLCPVIDMCNHSDHENVALMVPQRTDSSHESVICLRSLRDIDRGEELTMTYGGSPTELRVIWGMQRVL
Protein: BK channel (H8ESE2)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGEIYSPSQSKGFNQPYGYPMNCNLSRVFMEMTEEDRKCLEERKYWCFLLSSITTFCASMILVVIWRVVTHLCCQRREKEFVEPIPAPEAVQINMNGSKHAPSETDPFLKQQEEKHLGWMTEAKDWAGELISGQSLTGRFLVLLVFILSIGSLIIYFYDASFQNFQVETCIPWQDSPSQQIDLGFNIFFLVYFFIRFIAASDKVWFLLEMYSWIDFFTIPPSFVAIYLQRNWLGFRFLRALRLMTVPDILQYLNILKTSSSIRLTQLVTIFVAVCLTGAGLVHLLENSGDFFKGFINPHRITYADSVYFVLVTMSTVGYGDIYCTTLCGRLFMIFFILFGLAMFASYVPEIADLIGNRQKYGGEYKGEHGKKHIVVCGHITYDSVSHFLQDFLHEDRDDVDVEVVFLHRVVPDLELEGLFKRHFTKVEFFTGTVMDSLDLSRVKIGDADACLVLANKYSTNPDAEDAANIMRVISIKNYSSDIRVIVQLMQYHNKAYLLNIPSWDWKRGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSQTTPDWLNLYLCGAGMEMYTDTLSHSFVGMTFPEAVDLLFNRLGLLLLAIELKDEENKECNIAINPGPHIVIQPQTQGFFIAQSADEVKRAFFWCKQCHDDIKDVSLIKKCKCKNLALFRRNTKHSTAAREKNAKISDYSDFDALFYQNDARATDVLQQFQPQAPAGPMGHLGQQVQLRMINQQSSTSDTHLNTKSLRFAYEIKKLMPSSGGRRNSMSIPPDGRGVDFSKDFEQQFQDMKYDSTGMFHWCPSRNLEDCVLERHQAAMTVLNGHVVVCLFADQDSPLIGLRNFIMPLRSSNFHYHELKHVVIVGDLEYLRKEWKTLYNLPKISILNGSPLSRADLRAVNINLCDMCVIISARVPNTEDTTLADKEAILASLNIKAMQFDDTLGFFPMRHQTGDRSPLGSPISMQKKGAKFGTNVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAISVLDSLMSTTYFNDSALTLIRTLVTGGATPELELILAEGAGLRGGYSTPETLSNRDRCRIAQISLQDNPYDGVVHNTTYGAMFTIALRRYGQLCIGLYRLHDQDNPDSMKRYVITNPPAELRIKNTDYVYVLEQFDPGLEYEPGKRHF
Protein: Beta-2-glycoprotein 1 (Apolipoprotein H) (Apo-H) (Beta-2-glycoprotein I) (B2GPI) (Beta(2)GPI) (P26644)
Organism: Rattus norvegicus (Rat)
Function: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein A-II
- Apolipoprotein B-100
- Apolipoprotein C-III
- Apolipoprotein A-V
- Apolipoprotein C-I
- Apolipoprotein M
- Prothrombin
- Apolipoprotein E
- Alpha-2-HS-glycoprotein
- Apolipoprotein A-IV
Sequence:
MISPALIFFSAFLCHVAIAGRRMWPINTLKCTPRVCPFAGILENGVVRYTTFEYPNTIGFACNPGYYLNGTSSSKCTEEGKWSPELPVCARITCPPPPIPKFAALKEYKTSVGNSSFYQDTVVFKCLPHFAMFGNDTVTCTAHGNWTQLPECREVKCPFPSRPDNGFVNYPAKPVLSYKDKAVFGCHETYKLDGPEEVECTKTGNWSALPSCKASCKLSVKKATVLYQGQRVKIQDQFKNGMMHGDKVHFYCKNKEKKCSYTEEAQCIDGTIEIPKCFKEHSSLAFWKTDASDVTPC
Protein: Short-chain dehydrogenase/reductase family protein (Q75JE7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MGVLTDISLLLTNIIGSIILLIFYPILGFLNYKKKKTNFPTPKAIVITGASSGIGRGIALEYAKRKKNNSLVLGLTGRNIEKLEEIQKECLGLGVQVEIESIDVTDKEKLNDWLIKFDNKYKIDILIANAGTIETILPKELDFTERILTVANTNVIGTLNTVLPMVPIFESRGSGQLVLMSSITPYFDYVMAGYSSSKGYIKSFGLILRNGLASRGVGVSVITPGFIYTPLVDSLDYKDIPMLLPITTDKASKYIVDGISRNDAIISFPPLIYCISHFVATIPPTLRDATNFISNSLLKYPDYSKPVTHYSHHSQYSTNESKREDCPSSPAMNSNSQKNKEA
Protein: Mitogen-activated protein kinase kinase kinase (EC 2.7.11.25) (A0A0G2JUN9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MESSRSLLGCLASAAAAPPGEDATGAGAEEEEDEEEAAAELGSHATLPYWTAVFEYEAAGEDELTLRLGDVVEVLSKDSQVSGDEGWWTGQLNQRVGIFPSNYVTPRSAFSSRCQPGTEDPSCYPPIQLLEIDFAELTLEEIIGIGGFGKVYRAFWVGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRVPPDILVNWAVQIARGMNYLHDEAIVPVIHRDLKSSNILILQKVENGDLSNKTLKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTCPEPFAKLMEDCWNPDPHSRPSFSSILDQLTTIEESGFFEMPKDSFHCLQDDWKHEIQEMFDQLRAKEKELRTWEEELTRAALQQKNQEELLRRREQELAEREIDILERELNIIIHQLCQEKPRVKKRKGKFRKSRLKLKDGNRISLPSADFQHKFTVQASPTMDKRKSLISNRSSPPASPTIIPRLRAIQLTPGESSKTWGRSSVVPKEEGEEEEKRAPKKKGRTWGPGTLGQKELTSGDEGLKSLVDGYKQWSSSAPNLGKGPRSSPALPGFTSLMEIEDEDSEGPGSGENHLQHSPNQSYLCIPFPRGEDGDGPSSDGIHEEPTPVNSATSTPQLTPTNSLKRSGTHHRRCEVALLGCGAVLAATGLGFDLLEAGKCQLLPPEEPEPPAREEKKRREGLFQRASRPRRSTSPPSRKLFKKEEPMTLLGDPSASLTLLSLSSISECNSTRSLLRSDSDEIVVYEMPVSPVEAPPLTQCTQNPLVNVRVERFKRDPNQSLTPTHVTLTAPTQPSGHRRTPSDGALKPASVPPALGSRSPSSNGVSPGPGAGMLKTPSPSRDPGEFPRLPDPNVVFPPTPRRWNTQRDSTLERPKTLEFLPRPRPSANRQRLDPWWFVSPSHARSASPANSSSTETPSNLDSCFASSSSTVEERPGLPALLPLQAGPLPPAERTLLDLDAEGQSQDSTVPLCRAELNAHGPSPYEIQQEFWS
Protein: Jupiter microtubule associated homolog 2 (H3BMV3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFQVPDSEGGRAGSRAMKPPGGESSNLFGSPEEATPSSRPNRMASNIFGPTEEPQNIPKRTNPPGGKGSGIFDESTPVQTRQHLNPPGGKTSDIFGSPVTATSRLAHPNKPKDHVFLCEGEEPKSDLKAARSIPAGAEPEKSQLFRYTKEEEELWRPPSTKLYRTSGSNSQTSFQKRLETLGQEMKEFSS
Protein: Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 (Ankyrin-like protein 1) (Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein) (Q8WWH4)
Organism: Homo sapiens (Human)
Function: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with pi-bodies suggests a participation in the primary piRNAs metabolic process. Required prior to the pachytene stage to facilitate the production of multiple types of piRNAs, including those associated with repeats involved in the regulation of retrotransposons. May act by mediating protein-protein interactions during germ cell maturation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to pi-bodies, a subset of the nuage which contains primary piRNAs (By similarity). {ECO:0000250}.
Interaction partners:
- Piwi-like protein 2
- RNA helicase Mov10l1
- Tudor domain-containing protein 1
- Spliceosome-associated protein CWC15 homolog
- Probable ATP-dependent RNA helicase DDX4
- Putative ATP-dependent RNA helicase TDRD12
- ATP-dependent RNA helicase TDRD9
- Tumor susceptibility gene 101 protein
- Tudor and KH domain-containing protein
- Protein maelstrom homolog
Sequence:
MAASALRGLPVAGGGESSESEDDGWEIGYLDRTSQKLKRLLPIEEKKEKFKKAMTIGDVSLVQELLDSGISVDSNFQYGWTPLMYAASVANAELVRVLLDRGANASFEKDKQSILITACSAHGSEEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLLSFTLNPLEGKLQQLTKEDTICKILTTDSDREKDHIFSSYTAFGDLEVFLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITSKDQQKILAALKELQVEEIQFGELSEETKLEISGDEFLNFLLKLNKQCGHLITAVQNVITELPVNSQKITLEWASPQNFTSVCEELVNNVEDLSEKVCKLKDLIQKLQNERENDPTHIQLREEVSTWNSRILKRTAITICGFGFLLFICKLTFQRK
Protein: Family with sequence similarity 184, member A (Q6P9G8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDYSQEMHLKLSKKIAQLTKVIYALNTKNDEHESAIQALKDAHEEEIQQILAETREKILQYKSKVTEELDLRRKIQVLESSLEDHIKMKQQALTEFEAYKHRVEDMQLCAEAQHVQRIVTMSREVEEIRRKFEEKLRSFGQLQVQFEKDKRLALEDLQAAHRQEIQELLKSQQDHSASVNKGQEKAEELHRMEVESLNKMLEELRLERKKLIEDYEGKLNKAQSFYERELDTLKRSQLFTAESLQASKEKEADLRKEFQGQEAILRKTIGKLKTELQMVQDEAGSLLDKCQKLQTALAIAENNVQVLQKQLDDAKEGEMALLSKHKEVESELAAARERLQQQASDLVLKASHIGMLQATQMTQEVTIKDLESEKSRVNERLSQLEEERAFLRSKTQSLDEEQKQQILELEKKVNEAKRTQQEYYERELKNLQSRLEEEVTQLNEAHSKTLEELAWKHHMAIEAVHSNAIRDKKKLQMDLEEQHNKDKLNLEEDKNQLQQELENLKEVLEDKLNTANQEIGHLQDMVRKSEQGLGSAEGLIASLQDSQERLQNELDLTKDSLKETKDALLNVEGELEQERQQHEETIAAMKEEEKLKVDKMAHDLEIKWTENLRQECSKLREELRLQHEEDKKSAMSQLLQLKDREKNAARDSWQKKVEDLLNQISLLKQNLEIQLSQSQTSLQQLQAQFTQERQRLTQELEELEEQHQQRHKSLKEAHVLAFQTMEEEKEKEQRALENHLQQKHSAELQSLKDAHRESMEGFRIEMEQELQTLRFELEDEGKAMLASLRSELNHQHAAAIDLLRHNHHQELAAAKMELERSIDISRRQSKEHICRITDLQEELRHREHHISELDKEVQHLHENISALTKELEFKGKEILRIRSESNQQIRLHEQDLNKRLEKELDVMTADHLREKNIMRADFNKTNELLKEINAALQVSLEEMEEKYLMRESKPEDIQMITELKAMLTERDQIIKKLIEDNKFYQLELVNRETNFNKVFNSSPTVGVINPLAKQKKKNDKSPTNRFVSVPNLSALESGGVGNGHPNRLDPIPNSPVHDIEFNSSKPLPQPVPPKGPKTFLSPAQSEASPVASPDPQRQEWFARYFTF
Protein: Cell division cycle 45 (CDC45), putative (Q386N9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication complex GINS protein SLD5
- Uncharacterized protein
- DNA helicase
- GINS subunit domain-containing protein
- DNA replication licensing factor MCM3
- GINS subunit domain-containing protein
- Uncharacterized protein
- BRCT domain-containing protein
Sequence:
MADTLSPWDRINRFYHITRKPIHLFVAYHADAAAASLTLTSLLKACFIPFNLHPIAEYAEARDIIQRTSLAQDAELQVGDAAPVDELFLLIGLGASVALFSFFDLQRHIVLVLDSYRPFLLENLRACDSDRLVIWGQEKIHEEVDDFFRTQREQEKARRRRRRRRQMHRRRVRQHAEGDVEEDEVSDEASSSDDDDDDENDDEYGDDDEMTPSQSQERLDWLREDVPAHLERLYYAAECAGKSCALEMYDLAILLNRVKEPVLWHAALGVCDLFKRRLVDYGTYITDMRRIHNEVKLRKGIRHGLLDDLTNDTVNRYHKQVSSSNTMQLSSLEEDQLFLLRHLSLWNAMWLHPVVAGLLSLHRVEEGLGTLRQLLARCGVSAKVAQQPWRELPDDVKKDSCQLVRNELKQLLRTRGSFIKNPIQIQCVARTTGYSVEVSTFDICTLFTALLSAAPPSTIYTTSKDETTMKEKLREFRREQFWRAHDIIDADPNSPAFGAAVKEAQALHESVATATSALMQPGMMQSTKGIHYTQPADPTNTSTALETFGCPFRLGVLVERLLYTLTVERGLGKYTRDVRPVLLSCYIPRFTAAPEQQQQQQQHQQQQQQAEHSFIVVFAHEGPITAGLTPLIPVVRWNDCVTDTEEFLVPPLRDFVRRDAVVVEGRESTAHLAEMLHLHSLAGGR
Protein: Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase) (Q2LAM0)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydroxylation of free fatty acids at the C-2 position to produce 2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis (Probable). FA2H is stereospecific for the production of (R)-2-hydroxy fatty acids (By similarity). Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath. Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies critical for skin permeability barrier (By similarity). Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis. Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7L5A8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7L5A8}. Microsome membrane {ECO:0000250|UniProtKB:Q7L5A8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7L5A8}.
Interaction partners:
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Bifunctional coenzyme A synthase
- Methylsterol monooxygenase 1
- Fatty acid hydroxylase domain containing 2
- Cholesterol 25-hydroxylase
- DDB1- and CUL4-associated factor 17
Sequence:
MAPAPPPAASFTSAEVQRRLAAGACWVRRGASLYDLTGFVRHHPGGEQLLLARAGQDISADLDGPPHKHSDNARRWLEQYYVGELRADPQDPTENGAGAPAETQKTDAAIEPQFKVVDWDKDLVDWQKPLLWQVGHLGEKYDEWVHQPVARPIRLFHSDLIEAFSKTVWYSVPIIWVPLVLYLSWSYYRTLTQDNIRLFASFTRDYSLVVPESVFIGLFVLGMLIWTLVEYLIHRFLFHMKPPSNSHYLIMLHFVMHGQHHKAPFDGSRLVFPPVPASVVVAFFYVFLRLILPEAVAGILFAGGLLGYVLYDMTHYYLHFGSPHKGSYLYNMKAHHVKHHFEYQKSGFGISTKLWDYFFHTLIPEEADPKMQ