wanglab/gogpt-training-data huggingface dataset:
Protein: Tensin 2 (F7FBH3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}.
Interaction partners:
Sequence:
MLALSSARRSASEVGATPYPILLLLVPRAQCSSSQESPTLSRSTSKNPVHPSVMGMRSQAVEEGVPPSVPRWTSFCIVKPRKAEPHSFREKVFRKKAPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCQALPPAELRRNTAPVRRIEHLGSTKSLNHSKQRSTLPRSFSLDPLMERRWDLDLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVHDFGWPELHAPPLDKLCSICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKAAMELQPSQHRYVGYFSGLLSGSIRMNSSPLFLHYVFVPVLPAFEPNTGFQPFLKIYQSMQLVYTSGVYHITGPGPRQICISLEPALLLKGDVMVTCYHKGGQGTDRTLVFRVQFHTCTIHGPRLNFPKDQLDEAWADERFPFQASVEFVFSSSPEKVKGNTPRNDPSVSVDYNMTEPAVRWDSYENFNQHHEDSVDGSLAHTRGPLDGSPYAQVQRVPRQTPPAPSPELPPPPMLSVSSDSGHSSTLTTEHTAESPGRPPPTAAERQELDRLLGGCGVASAGRGAGRETAILDDEEQPSVGGGLHLGMYPGHRPGLSRRCSCRQGLREPCGVPNGGYYRPEGTLERRRPPYGGYEGHPQGYTEASVEKRRLCRSLSEGPYPYAPELGKPANGDFGYRPAGYREVVILEDPGVPALCSCPACEEKMALPTAALYGLRLEREAGEGWSSEVGKPLLHPVRPGHPLPLLVPACGHHHAPVPDYGCLKSPKVGEEGHEGCSYAVCPEGRYGHPGYPALVTYGYGGAVPSYCPAYGRAPHSCGSPSEGRGYPSPGAHSPQAGSVSPGSPPYLQSRKLGYEAPAEDGRDKYSLPGPLASAGPLASTESPEPSWRDGSSGHSTLPRSPRDAQCSASSELSGPSTPLHTSSPVQGKESTRRQDTTRSPSLAPTQRLSPGEALPSVVQGVTEKTPELLASSRPEPLDPSPFSQTSTPSSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPQGPSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYETNGPTQPPLPEKRHLPGSGQQSSPPARGTNQHVTFASPLPDVTQPPEHPLQENQSSVKFVQDTSKFWYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQPWKGDPSEQLVRHFLIETGPKGVKIKGCPTEPYFGSLSALVSQHSISPISLPCCLRIPSKDPLEETSEAPVPTNMSTAADLLRQGAACSVLYLTSVETESLTGPQAVARASSAALSCSPVPVPAIVHFKVSAQGITLTDNQRKVFFRRHYPVNSITFSSTDPQDRRWTNPDGTTSKIFGFVAKKPGSPWENVCHLFAELDPDQPASAIVTFITKVLLGQRK
Protein: T-box transcription factor T (Brachyury protein) (Protein T) (A0A8I6AEA5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MSSPGTESAGKSLQYRVDHLLSAVESELQAGSEKGDPTERELRVGLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWNKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERNDHKDVMEEPGDCQQPGYSQSGGWLVPGAGTLCPPASSHPQFGGSLSLPSTHGCERYPTLRNHRSSPYPSPYAHRNNSPTYADNSSACLSMLQSHDNWSSLGVPAHTSMLPVSHNASPPTGSSQYPSLWSVSNGTITPGSQTAGVSNGLGAQFFRGSPAHYAPLTHTVSAATSSSSGSPMYEGAATVTDISDSQYDTAQSLLIASWTPVSPPSL
Protein: Nucleoporin nup120 (Nuclear pore protein nup120) (O43044)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope.
Subcellular location: Nucleus {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:15226438, ECO:0000269|PubMed:16823372}. Note=Nuclear rim.
Interaction partners:
- Nucleoporin seh1
- Nucleoporin nup85
- Nucleoporin nup107
- Protein transport protein sec13
- Nucleoporin nup189
- Nucleoporin nup131
- Nucleoporin nup132
- Uncharacterized WD repeat-containing protein C4F10.18
- Nucleoporin nup184
- Nucleoporin nup44
Sequence:
MNELKHAVVPIDLQSFCLEGTLALWVPALENDSEDDSEAIETADDNEKLFKKECVAYDAGVYTSNKSKGSQTLRWSIFQNRTLTIFDVSLNSKKEPLSKFNVKIHFPSNVMKDGVAFSFSEHSDTTIIYAITHARVLYYIRLSKTWFQLPDARLDDDWCLCYRPISFLNQKPDLMAAISTSEICVSFFNGGLTKIILNPKDASHYEQHIDDSSYLFSLKKYLSLQAFKADYRSPNTIISMIFLSTYNVLVMLSLDYKLKVLDLSTNQCVETIELSQTILPLQSFPYLTSDHTTNSFIALYYPDNSHGSFSIYKLNANAHSFKLNVVIEKGIIPPSLPDDEFIPWMLSDFQLISSEGSQSKFLLIIAWKSNLNTVIQKCNLSLDQDESFSCVWSHSLDSFSLIEKTFFDVPTNMSSGDISEIWLQHIFAHNTSIESIQVALLSFQNSSSQVSKNKLDKFGALTISELKNAVLSSIVSTIQIEPNSDLTGYDYYEYKRLLYNEWERFAKLVAYLDHFGDEILSINFDPSNAVTYINYANKVAFIRDPYLIESFDEEPLTKLISSLETDDPSLIEGYQILDLGRSLHSCMSFSTLSEIRYSLRELVQDLPSYSLFDTLWVFYDKHIYPNVDPDYISTLIDTLVSLENPMRDIDSLIQRLRSFDIYNHSAQSPSLFLCASVARVLDSILKKFQVSIEGFIFLLSLITSQQDYELQSKFAGCDKLFLSLLEDWRLVSFLLENSALLLEKFEEEDVDSTNCNLNTMEALASVNTALQFFSALNYSECFSESQISPLHATVISSLSAIFIRDDTENDLVTELVEKLFLFKQYNACMQLIGWLNSDPIAVYLKALIYLKSKEAVKAVRCFKTTSLVLYSHTSQFAVLREFQEIAEKYHHQNLLSCYYLHLSKKLFEESAYIDALEFSLLADASKETDDEDLSIAITHETLKTACAAGKFDAAHVALMVLSTTPLKKSCLLDFVNQLTKQGKINQLLNYSMPTLRQDVDNLLERKAFQMINVESQPCWYNILFSWRYKHQNYRDAAAIIYEKLSRYISTTELIGKKERTFIIEHYLIVLNTLELLPKEDTWILVTDMSVDKEPDPNFLPQKLLTLDAIVAEYHLQLKDVAVQVTAEMSSAMNIDL
Protein: Conserved oligomeric Golgi complex subunit 5 (COG complex subunit 5) (13S Golgi transport complex 90 kDa subunit) (GTC-90) (Component of oligomeric Golgi complex 5) (Golgi transport complex 1) (Q9UP83)
Organism: Homo sapiens (Human)
Function: Required for normal Golgi function.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9792665}. Golgi apparatus membrane {ECO:0000269|PubMed:9792665}; Peripheral membrane protein {ECO:0000269|PubMed:9792665}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 7
- Syntaxin-5
- Golgi SNAP receptor complex member 2
- Vacuolar protein sorting-associated protein 53 homolog
Sequence:
MGWVGGRRRDSASPPGRSRSAADDINPAPANMEGGGGSVAVAGLGARGSGAAAATVRELLQDGCYSDFLNEDFDVKTYTSQSIHQAVIAEQLAKLAQGISQLDRELHLQVVARHEDLLAQATGIESLEGVLQMMQTRIGALQGAVDRIKAKIVEPYNKIVARTAQLARLQVACDLLRRIIRILNLSKRLQGQLQGGSREITKAAQSLNELDYLSQGIDLSGIEVIENDLLFIARARLEVENQAKRLLEQGLETQNPTQVGTALQVFYNLGTLKDTITSVVDGYCATLEENINSALDIKVLTQPSQSAVRGGPGRSTMPTPGNTAALRASFWTNMEKLMDHIYAVCGQVQHLQKVLAKKRDPVSHICFIEEIVKDGQPEIFYTFWNSVTQALSSQFHMATNSSMFLKQAFEGEYPKLLRLYNDLWKRLQQYSQHIQGNFNASGTTDLYVDLQHMEDDAQDIFIPKKPDYDPEKALKDSLQPYEAAYLSKSLSRLFDPINLVFPPGGRNPPSSDELDGIIKTIASELNVAAVDTNLTLAVSKNVAKTIQLYSVKSEQLLSTQGDASQVIGPLTEGQRRNVAVVNSLYKLHQSVTKVVSSQSSFPLAAEQTIISALKAIHALMENAVQPLLTSVGDAIEAIIITMHQEDFSGSLSSSGKPDVPCSLYMKELQGFIARVMSDYFKHFECLDFVFDNTEAIAQRAVELFIRHASLIRPLGEGGKMRLAADFAQMELAVGPFCRRVSDLGKSYRMLRSFRPLLFQASEHVASSPALGDVIPFSIIIQFLFTRAPAELKSPFQRAEWSHTRFSQWLDDHPSEKDRLLLIRGALEAYVQSVRSREGKEFAPVYPIMVQLLQKAMSALQ
Protein: Immune-associated nucleotide-binding protein 3 (AtIAN3) (AIG1-like protein) (Q9C8U6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Hyperosmolality-gated Ca2+ permeable channel 1.7
- Gb|AAF32477.1
- Glutamate receptor 2.3
- F-box protein At3g61340
- Subtilisin-like protease SBT3.7
- MATH domain and coiled-coil domain-containing protein At3g58210
- Kinesin-like protein KIN-14O
- Uncharacterized protein
- Core-2/I-branching beta-1,6-n-acetylglucosaminyltransferase family protein
- GDSL esterase/lipase At1g06990
Sequence:
MNHSEQASAYKAVKNIVLVGRTGNGKSATGNSLIGKDVFVSEAKATGVTKTCQTYKAVTPGGSRINVIDTPGLFDLSVSAEFISKEIINCLRLAEGGLHVVVLVLSVRTRITQEEENTLSTLQVLFGNEILDYLIVLFTGGDELEANNQTLDDYFHQGCPYFLKTVLGLCDDRKVMFNNMTKDKHKKVEQVQQFLALVAKVEERNEGKPFRGKMYLEIKEETEWLKKQKKAVEASNLGEAELAKMKKELQMEHDTRMSQMEDMVKNMLKETSAAHERMVSMLNENLENAHRENIDLRKAHDHEQKKRMMIQLGLGVPGALGMIAPAALAMCSIL
Protein: Inositol/phosphatidylinositol phosphatase, putative (Q38EY7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}.
Interaction partners:
- Pre-mRNA-processing factor 19
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- Phosphatidylinositol 4-phosphate 5-kinase alpha, putative
- Phosphoinositide phospholipase C
- Endonuclease/exonuclease/phosphatase, putative
- Activated protein kinase C receptor homolog
- Clathrin heavy chain
- BTB domain-containing protein
Sequence:
MVNGLPPAFQQTHYSSDDIFAFLRTASPVQSSCEILFPEEVWVQQELQFYEDSYTEQQDLRTCIVTFNVASKKPPQNLASLIALTMPGAGGEPVDLIMVSLQEVDMSASAMLKDETDASVVWVSALQAVIGADSQAAGESPYFAFPPKQLVGLLLCVFIRRSLLPHAQKMAITTVATGALGTMGNKGAVGLHLGLCRSNLCFINMHLAAGQKNVVKRNNDVSKIFMGMDFNTTKRPISLETRGGNSAQSELQFQYPEFLPHNNDVIVVAGDLNYRVNLTYRESLQLAMKKDYATLLKHDEFVKELANTHSPWMGFVELTPTYPPTYRYDIGTNNYDTSEKQRVPSYTDRIAIWTRRRDHQSSIRLERLQALTDVMSSDHKPVQACLCLPISREVLEKKISVTQSLRDSVKREGLDRIRKAKISVNSQSLNFGVRQFGDCGSRQPLKITNEGDCVAVIKAFRQQDGDPSKGAWLRVFPLIIFIPPRKEKEVMIECQLDRNSTEWVRNWRPFEGRGEVEITSTLVLCVRNGDIHFVECRCTVRPSVFGNTLDNISLLRNEVCAAAYTLWGTPERRSGGCMPQIPKELWYLCEAIYERGAQQPNLFTENPSTEVCDAIMKHLNTQCRPLPSEYNVQCISACLIYFLQSLQEPVVPYELYEKALAVLKSKSGNPFQFVQQQLPPLHANVWIYVCSLMNFLLRPVNTCGNGLTTKFLARVLSDVMLVRPEALTQMPPSVGTCTHQEVASNAPPKGGTALQAFRQQLQQEREDALRFVECFLVPPPAVIL
Protein: Transcription termination factor 2 (EC 3.6.4.-) (Lodestar homolog) (RNA polymerase II termination factor) (Transcription release factor 2) (F2) (HuF2) (Q9UNY4)
Organism: Homo sapiens (Human)
Function: DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15125840}. Nucleus {ECO:0000269|PubMed:15125840}. Note=Cytoplasmic during interphase. Relocates to the nucleus as cells enter mitosis.
Interaction partners:
- Meiotic recombination protein REC114
- Bifunctional polynucleotide phosphatase/kinase
- Protein kinase C gamma type
- cAMP-dependent protein kinase catalytic subunit gamma
- Protein kinase C alpha type
- cAMP-dependent protein kinase catalytic subunit alpha
- Protein kinase C beta type
- cAMP-dependent protein kinase catalytic subunit beta
- Inositol monophosphatase 1
- Inositol monophosphatase 2
Sequence:
MEEVRCPEHGTFCFLKTGVRDGPNKGKSFYVCRADTCSFVRATDIPVSHCLLHEDFVVELQGLLLPQDKKEYRLFFRCIRSKAEGKRWCGSIPWQDPDSKEHSVSNKSQHASETFHHSSNWLRNPFKVLDKNQEPALWKQLIKGEGEEKKADKKQREKGDQLFDQKKEQKPEMMEKDLSSGLVPKKKQSVVQEKKQEEGAEIQCEAETGGTHKRDFSEIKSQQCQGNELTRPSASSQEKSSGKSQDVQRESEPLREKVTQLLPQNVHSHNSISKPQKGGPLNKEYTNWEAKETKAKDGPSIQATQKSLPQGHFQERPETHSVPAPGGPAAQAAPAAPGLSLGEGREAATSSDDEEEDDVVFVSSKPGSPLLFDSTLDLETKENLQFPDRSVQRKVSPASGVSKKVEPSDPVARRVYLTTQLKQKKSTLASVNIQALPDKGQKLIKQIQELEEVLSGLTLSPEQGTNEKSNSQVPQQSHFTKTTTGPPHLVPPQPLPRRGTQPVGSLELKSACQVTAGGSSQCYRGHTNQDHVHAVWKITSEAIGQLHRSLESCPGETVVAEDPAGLKVPLLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKKEEKEKSTALTWLSKDDSCDFTSHGTLIICPASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEAEIPGANLNVEGTSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGGERLSILTKSLLLRRTKDQLDSTGRPLVILPQRKFQLHHLKLSEDEETVYNVFFARSRSALQSYLKRHESRGNQSGRSPNNPFSRVALEFGSEEPRHSEAADSPRSSTVHILSQLLRLRQCCCHLSLLKSALDPMELKGEGLVLSLEEQLSALTLSELRDSEPSSTVSLNGTFFKMELFEGMRESTKISSLLAELEAIQRNSASQKSVIVSQWTNMLKVVALHLKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVVIHRFVCEGTVEEKILQLQEKKKDLAKQVLSGSGESVTKLTLADLRVLFGI
Protein: Coiled-coil domain containing 62 (A0A024RBT8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLEHALRDAKMAETCIVKEKQDYKQKLKALKIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELLFTVEREKRKDELLNIAKSKQERTNSELHNLRQIYVKQQSDLQFLNFNVENSQELIQMYDSKMEESKALDSSRDMCLSDLENNHPKVDIKREKNQKSLFKDQKFEAMLVQQNRSDKSSCDECKEKKQQIDTVFGEKSVITLSSIFTKDLVEKHNLPWSLGGKTQIEPENKITLCKIHTKSPKCHGTGVQNEGKQPSETPTLSDEKQWHDVSVYLGLTNCPSSKHPEKLDVECQDQMERSEISCCQKNEACLGESGMCDSKCCHPSNFIIEAPGHMSDVEWMSIFKPSKMQRIVRLKSGCTCSESICGTQHDSPASELIAIQDSHSLGSSKSALREDETESSSNKKNSPTSLLIYKDAPAFNEKASIVLPSQDDFSPTSKLQRLLAESRQMVTDLELSTLLPISHENLTGSATNISHLCGRQKADTNTE
Protein: Ribosome biogenesis protein BOP1 (Block of proliferation 1 protein) (Q14137)
Organism: Homo sapiens (Human)
Function: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:12429849}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:12429849}.
Interaction partners:
- Ribosome biogenesis protein WDR12
- WD repeat-containing protein 74
- ATP-dependent RNA helicase DDX18
- Pescadillo homolog
- Nucleolar complex protein 2 homolog
- Glutamate-rich WD repeat-containing protein 1
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Ribosomal L1 domain-containing protein 1
- mRNA turnover protein 4 homolog
- GTP-binding protein 4
Sequence:
MAGSRGAGRTAAPSVRPEKRRSEPELEPEPEPEPPLLCTSPLSHSTGSDSGVSDSEESVFSGLEDSGSDSSEDDDEGDEEGEDGALDDEGHSGIKKTTEEQVQASTPCPRTEMASARIGDEYAEDSSDEEDIRNTVGNVPLEWYDDFPHVGYDLDGRRIYKPLRTRDELDQFLDKMDDPDYWRTVQDPMTGRDLRLTDEQVALVRRLQSGQFGDVGFNPYEPAVDFFSGDVMIHPVTNRPADKRSFIPSLVEKEKVSRMVHAIKMGWIQPRRPRDPTPSFYDLWAQEDPNAVLGRHKMHVPAPKLALPGHAESYNPPPEYLLSEEERLAWEQQEPGERKLSFLPRKFPSLRAVPAYGRFIQERFERCLDLYLCPRQRKMRVNVDPEDLIPKLPRPRDLQPFPTCQALVYRGHSDLVRCLSVSPGGQWLVSGSDDGSLRLWEVATARCVRTVPVGGVVKSVAWNPSPAVCLVAAAVEDSVLLLNPALGDRLVAGSTDQLLSAFVPPEEPPLQPARWLEASEEERQVGLRLRICHGKPVTQVTWHGRGDYLAVVLATQGHTQVLIHQLSRRRSQSPFRRSHGQVQRVAFHPARPFLLVASQRSVRLYHLLRQELTKKLMPNCKWVSSLAVHPAGDNVICGSYDSKLVWFDLDLSTKPYRMLRHHKKALRAVAFHPRYPLFASGSDDGSVIVCHGMVYNDLLQNPLLVPVKVLKGHVLTRDLGVLDVIFHPTQPWVFSSGADGTVRLFT
Protein: Extraocular myosin heavy chain EO-MYHC (Q8VHZ3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
HIFSISDNAYQFMLTDRDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNM
Protein: Arginine kinase (EC 2.7.3.3) (Q38EV2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Arginase, putative
- Arginine kinase
- Arginine kinase
Sequence:
MGFGSSKPKNKPSKADSKNSPSDPTGAGNNDLEKAFAKLQAAKDCHSLLKKHLTSDVFKKLKDKKTKLGATLLDVIQSGVQNLDSGVGLYAPDAEAYTVFADLFDPVIEDYHNGFKVTDKQPPKDFGDLNTLVDVDPEGKYVISTRVRCGRSLAGYPFNPCLTKEQYEEMESRVREQLSTMTDDLQGTYYPLSGMTKETQQQLIDDHFLFKEGDRFLQAARACEYWPTGRGIYHNNDKTFLVWVNEEDHLRIISMQKGGNLKEVFGRLVKAVNTIEEKVEFSRDDRLGFLTFCPSNLGTTIRASVHIKLPKLGADRAKLEEVAAKYNLQVRGTAGEHSDSPDGIYDISNKRRLGLSEYEAVKEMQDGILELIKLEQSDDAEGNGGADAAGPDDGVDGVATNENE
Protein: Prenylcysteine oxidase 1 (EC 1.8.3.5) (Prenylcysteine lyase) (Q9CQF9)
Organism: Mus musculus (Mouse)
Function: Prenylcysteine oxidase that cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine. Only active against free prenylcysteines and not prenylcysteine residues within prenylated proteins or peptides (By similarity). Involved in the final step in the degradation of prenylated proteins, by degrading prenylcysteines after the protein has been degraded.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q9UHG3}.
Interaction partners:
- Serum paraoxonase/arylesterase 1
- Apolipoprotein E
- Apolipoprotein C-IV
- Apolipoprotein B-100
- Apolipoprotein A-II
- Apolipoprotein C-III
- Phospholipid transfer protein
- Apolipoprotein A-I
- Platelet-activating factor acetylhydrolase
- Clusterin
Sequence:
MGRFAAALVGSLFWLGLLLCGLGSLASAEPRAPPNRIAIVGAGIGGTSSAYYLRKKFGKDVKIDVFEREEVGGRLATLKVQGHDYEAGGSVIHPLNLHMKRFVKELGLSSVPASGGLVGVYNGKSLVFEESSWFVINVIKLVWRYGFQSLRMHMWVEDLLDKFMRIYRYQSHDYAFSSVEKLMHAIGGDDYVRLLNQTLRENLKKAGFSETFLNEMIAPVMKVNYGQSTDINAFVGAVSLTAADSNLWAVEGGNKIVCSGLLQASSSNLISGSVMSIEEKTRTKQTGNPTKMYEVVYKTGSETHSDFYDIVLVAAPLNRKMSNITFRNFDPPIEEFNDPYQQLVTTFIKGELNSTLFSSRPKDQFGLSAILVTDDSDMFINSLSIVASVRQKEGPPPAVDGMHVWKTFSRDILTKEQISKLFLSYDYAVRKPWLSYPHYEPPQKCPSIILHDRLYYLNGIEFAASCMEMSAIAGYNAALLAYHRWNGNEDMIDQDDLYERLKTEL
Protein: Platelet-activating factor acetylhydrolase (EC 3.1.1.47) (A0A8I5Y241)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MSGPDAQEVSGLQIMFHKLQSVMSAVSAGRCKIPKGNGSYPVGCTDMMFGYGNESIFLRLYYPAQDQGPHDTVWVPNIEYFWGLSKFLGTPTFVGNILRLLYGSLTAPASWNFPLRTGEKYPLIIFSHGLGAFRTIYSAIGAALASYGFIVATVEHRDGSASATYYFEDQAAAKMENRSWFYLKKIKQEESERARKEQVRQRAKECSKALSAILDIEHGNPKENVLGLPFDMKQLKDSIDETKIAVMGHSFGGATVFQALSEDQRFRCGIALDPWMFPVSEELYSRVPQPLFFINSAEFQTPKDIAKMKNFYQPDKERKMITIKGSVHQNFADGTFVTGKIIGNKLSLKGDIDSRVAIDLTNKASLAFLQKHLGLHKDFDQWDCLVEGENENLIPGSPFDVVTQSPALQSSPGSHNQN
Protein: Menage a trois, isoform C (B7YZF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLEAVMASDINWDPALSKLISTLKESENLSNDQEIDFLKALLESKELNALVNVHTKVAKVGRDDRLAPVLSTSAQVLYEVLEQLSQHCHLNDDCKEAFHLLQDSHLQHLLFAHDAIAQKDFYPHLPEAPVEMDEDEETIKIVQLVKSNEPLGATIKTDEESGKIIIARIMHGGAADRSGLIHVGDEVIEVNNINVEGKTPGDVLTILQNSEGTITFKLVPADNKGAQRESKVRVRAHFDYNPDVDPYIPCKEAGLAFQRGDVLHIVAQDDAYWWQARKEHERSARAGLIPSRALQERRILHDRTQKNGTDLDSKPGSCASLCTTPPGSPRLPASSSTSSCRQPKTKKIMYDLTENDDFDREQIATYEEVAKLYPRPGVFRPIVLIGAPGVGRNELRRRLIARDPEKFRSPVPYTTRPMRTGEVAGREYIFVAREKMDADIEAGKFVEHGEYKGHLYGTSAESVKSIVNAGCVCVLSPHYQAIKTLRTAQLKPFLIHVKPPELDILKATRTEARAKSTFDEANARSFTDEEFEDMIKSAERIDFLYGHFFDVELVNGELVNAFEQLVQNVQRLENEPVWAPSMWVQ
Protein: EB domain-containing protein (O45828)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKQLPIFLVFMVATAFCDNIGFFKSPTEKRCDKDYECSGTDLCGHYVCTPLSEFRKCPEDKRCGFEYSCMSGVCRYMSDFDAERRFSNFGPDMKCKDSRVCPIGLHCSNGNCV
Protein: Endoribonuclease YicC (EC 3.1.26.-) (P23839)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Guanylate kinase
- DNA-directed RNA polymerase subunit omega
- Glutamate synthase large chain
Sequence:
MIRSMTAYARREIKGEWGSATWEMRSVNQRYLETYFRLPEQFRSLEPVVRERIRSRLTRGKVECTLRYEPDVSAQGELILNEKLAKQLVTAANWVKMQSDEGEINPVDILRWPGVMAAQEQDLDAIAAEILAALDGTLDDFIVARETEGQALKALIEQRLEGVTAEVVKVRSHMPEILQWQRERLVAKLEDAQVQLENNRLEQELVLLAQRIDVAEELDRLEAHVKETYNILKKKEAVGRRLDFMMQEFNRESNTLASKSINAEVTNSAIELKVLIEQMREQIQNIE
Protein: Lmo0485 protein (Q8Y9P0)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Interaction partners:
- Heme-degrading monooxygenase
- Uroporphyrinogen-III C-methyltransferase
Sequence:
MIEKTIMERRSIKKANDEPISRETVNTILEQAAYAPFHSKVEPWNVYVLHTLAEKERYIEKIIEFNEREQGVSFSEAEIADLKAGYAKKIITPPYLLIVTTNIIGHGKKDFESIGATSAFIQNIQLLGWEAGIGMIWRSNRFIFDAKFADDLGIPAEQKIVGTLHLTSLAEVPEAKPRRPLNEWVKNLADL
Protein: Long-chain-alcohol oxidase FAO1 (EC 1.1.3.20) (Long-chain fatty alcohol oxidase 1) (B5WWZ8)
Organism: Lotus japonicus (Lotus corniculatus var. japonicus)
Function: Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRKECHPLLRGGRKDNKFRQGFSSSEMESLASICEVILPPLPMDALKIKKHDDVSIEDVEFFWNTSASHYPIPHEVAEILSKRSLIEAVILIRVVLWLLATRLGTFLLCGLLCFSEKWPFINNFSSMSLKKRERVMQWWLKNRFITPIRLAFAYLKVLCLFAYFTWVDENGDNPAWKAIGYEVSADEKLPNSSNGRLLEKGIVETMHETNSTLQQSLTEKGLNVTLDSRNNILKVKCDAIVVGSGCGGGVAASVLSGAGHKVVVLEKGNYFAPRDYSSLEGPSMDQLYETGGILASVDSRILLLAGSTVGGGSAVNWSACIKTPHEVLKEWSENHNLSLFSTSEYLSAMETVCERIGVTESCTHEGFQNQVLRKGCQNLGLKVDYVPRNSSGNHFCGSCGYGCPKGEKQGTQDTWLVDAVENGAVIITGCKAERFLLENNRNGSGRKKKCLGVLAKALSSRVTMKLQIEAKVTISAGGALLTPPLMISSGLKNKNIGKNLHLHPVLMTWGYFPESTSELKGKIFEGGIITSVHKVPSRDSNSYSDTRAIIETPSLGPGSFASLCPWESGLDFKERMLNYPRTAHLITIIRDKACGQVTTEGRVSYKLSAFDKENMKCGLQQALRILKAAGAVEVGTHRSDGQRVKCGEVSENEMAEFIDSVCPMEGALSPGENWNIYTSAHQMGSCRMGMNEKEGAVDENGESWEAQGLFVCDASLLPTAVGVNPMITIQSTAYCISNRVVDYLKRDQI
Protein: Protein W (P0C1C7)
Organism: Nipah virus
Function: Prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta). Interacts with host STAT1 protein in the nucleus, blocking it's phosphorylation by IFN-alpha/beta. Also blocks antiviral state induced by Toll-like receptor 3/TLR3 binding to dsRNA.
Subcellular location: Host nucleus {ECO:0000269|PubMed:15857993}.
Interaction partners:
Sequence:
MDKLELVNDGLNIIDFIQKNQKEIQKTYGRSSIQQPSIKDQTKAWEDFLQCTSGESEQVEGGMSKDDGDVERRNLEDLSSTSPTDGTIGKRVSNTRDWAEGSDDIQLDPVVTDVVYHDHGGECTGYGFTSSPERGWSDYTSGANNGNVCLVSDAKMLSYAPEIAVSKEDRETDLVHLENKLSTTGLNPTAVPFTLRNLSDPAKDSPVIAEHYYGLGVKEQNVGPQTSRNVNLDSIKLYTSDDEEADQLEFEDEFAGSSSEVIVGISPEDEEPSSVGGKPNESIGRTIEGQSIRDNLQAKDNKSTDVPGAGPKDSAVKEEPPQKRLPMLAEEFECSGSEDPIIRELLKENSLINCQQGKDAQPPYHWSIERSISPDKTEIVNGAVQTADRQRPGTPMPKSRGIPIKKGAQTRNIHLLGRKTCLGRRVVQPGMFEDHPPTKKARVSMRRMSN
Protein: Gonad-stimulating substance (Relaxin-like gonad-stimulating peptide) [Cleaved into: Gonad-stimulating substance B chain; Gonad-stimulating substance A chain] (C9K4X8)
Organism: Patiria pectinifera (Starfish) (Asterina pectinifera)
Function: Induces oocyte maturation and ovulation in vitro in ovarian fragments and induces spawning behavior and gamete release in vivo. Probably mediates its effects by binding to a G-protein coupled receptor located in follicle cell membranes. Following receptor binding, stimulates GTP-dependent adenylyl cyclase activity in follicle cell membranes of fully grown ovaries at stage V but not in young ovaries at stage IV, leading to the production of cAMP. This stimulates the production of the maturation-inducing hormone, 1-methyladenine, in stage V but not stage IV ovaries. The lack of activity in stage IV ovaries may be due to the very low levels of the G-protein alpha s subunit which is not expressed at high levels in follicle cells until stage V.
Subcellular location: Secreted {ECO:0000269|PubMed:23829221}.
Interaction partners:
Sequence:
MTSNNRHLFQATCLVLLLLHAAFHGGALGEKYCDDDFHMAVFRTCAVSKRSQPGMSLSDVLTMNRFRGHNIKRSIDSTLEDNAFFMSGLEKRSEYSGIASYCCLHGCTPSELSVVC
Protein: B-cell CLL/lymphoma 7 protein family member C (Q8WUZ0)
Organism: Homo sapiens (Human)
Function: May play an anti-apoptotic role.
Interaction partners:
- Protein SSXT
- AT-rich interactive domain-containing protein 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF complex subunit SMARCC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
- Bromodomain-containing protein 9
- B-cell CLL/lymphoma 7 protein family member B
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
Sequence:
MAGRTVRAETRSRAKDDIKKVMATIEKVRRWEKRWVTVGDTSLRIFKWVPVVDPQEEERRRAGGGAERSRGRERRGRGASPRGGGPLILLDLNDENSNQSFHSEGSLQKGTEPSPGGTPQPSRPVSPAGPPEGVPEEAQPPRLGQERDPGGITAGSTDEPPMLTKEEPVPELLEAEAPEAYPVFEPVPPVPEAAQGDTEDSEGAPPLKRICPNAPDP
Protein: Cystatin-like protein (CbCystatin) (M1GL27)
Organism: Clarias batrachus (Walking catfish) (Silurus batrachus)
Function: Involved in hypoxia tolerance.
Interaction partners:
Sequence:
MDVALKLLLLAALTLLASAQTPIDYKDLSTTLQEHIDKALEEGNRKFGGRHHVALDSFVTPAVTRQSILNVNVFLKVTTCMKTRSYKHRPECNTQKRSTPKINCLVCKMKNGTELVHCARKIDILHGEHKEIRDNCDVTRIGVSSLMAQTMPDDYRKQVGCLGCI
Protein: Cx9C motif-containing protein 4, mitochondrial (A6ZMQ6)
Organism: Saccharomyces cerevisiae (strain YJM789) (Baker's yeast)
Subcellular location: Mitochondrion intermembrane space {ECO:0000250}. Note=Imported into the mitochondria via the mitochondrial disulfide relay system. {ECO:0000250}.
Interaction partners:
Sequence:
MSNPCQKEACAIQDCLLSHQYDDAKCAKVIDQLYICCSKFYKDNGKDSRSPCCPLPSLLELKMKQRKLTPGDS
Protein: SH3 domain-containing protein 1 (Q9C865)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipid binding protein bound strongly to phosphatidic acid, phosphatidylinositol-4-phosphate and phosphatidylinositol-4,5-bisphosphate. Binds actin in vitro. Involved in trafficking and modification of clathrin-coated vesicles.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:11701884}. Cell membrane {ECO:0000269|PubMed:11701884}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11701884}. Endoplasmic reticulum {ECO:0000269|PubMed:11701884}. Cytoplasmic vesicle {ECO:0000269|PubMed:11701884}.
Interaction partners:
- Auxilin-related protein 1
- Probable inactive poly [ADP-ribose] polymerase SRO2
- Poly
- Zinc finger CCCH domain-containing protein 47
- Dynamin-2A
Sequence:
MEAIRKQAAKLREQVARQQQAVLKHLGHVNADAVVVDEEELHCHQKLQDLYSSTKAAKRLQRNIVRGLEGFIATGTKVVEIGLKFAEDFKKYGDENPDANTPLSRVAHHFGTSYKSVEGERETLLGVLSEQVCEPIRTMIYSAPLEDARHLVNHYDRLRQEVEAQATDVLRRRSKLKESDISEEAYIKLKNSESRLAELKSSMKTLGKEATKAMLEVDDQQQNVTSQRLRALVEAERSYHRNALDILDKLHSEMIAEEEAIGSSPKSLPLHIEDSASLPQQEPNSNSSGEIKSNPLGKIKASRREEIKSNPQEVTKPSPKDEMKSSPQEETKSNHQKEIKSSPQEEIKKSNGSDDHHNHQLLSQNDSYFLAKVVHPFDAQAPGELSLAVDDYVIVRQVAGTGWSEGEYKGKAGWFPSAYVEKQEKAPASKIVESNSKQQ