wanglab/gogpt-training-data huggingface dataset:
Protein: Sperm protamine P1 (Q3MN80)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000650}.
Interaction partners:
Sequence:
MARYRCCRSQSRSRYYRQRQRSRRRRRRSCQTRRRAMRCCRPRYRPRCRRH
Protein: Cadherin 11 (Cadherin-11 isoform X1) (F1RFU7)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
Interaction partners:
- Catenin beta 1.
- Junction plakoglobin
- Cadherin-2
- IQ motif containing M
- Catenin delta 1
- Catenin alpha-1
- Cadherin-1
Sequence:
MKENYCLQAALVCLGMLCHSQAFATERRSHLRPSFHGHHEKGKEGQVLQRSKRGWVWNQFFVIEEYTGPDPVLVGRLHSDIDSGDGNIKYILSGEGAGTIFVIDDKSGNIHATKTLDREERAQYTLMAQAVDRDTNRPLEPPSEFIVKVQDINDNPPEFLQETYHANVPERSNVGTSVIQVTASDADDPTYGNSAKLVYSILEGQPYFSVEAQTGIIRTALPNMDREAKEEYHVVIQAKDMGGHMGGLSGTTKVTITLTDVNDNPPKFPQSVYQMSVSEAAVPGEEVGRVKAKDPDIGENGLVTYNIVDGDGMELFEITTDYETQEGVVKLKKPVDFETKRAYSLKVEAANVHIDPKFISNGPFKDTVTVKIAVEDADEPPMFLAPSYIHEVQENAAAGTVVGRVHAKDPDAANSPIRYSIDRHTDLDRFFTINPEDGFIKTTKPLDREETAWLNITVFAAEIHNRHQEAKVPVAIRVLDVNDNAPKFAAPYEGFICESDQTKPLSNQPIVTISADDKDDTANGPRFIFSLPPEIIHNPNFTVRDNRDNTAGVYARRGGFSRQKQDLYLLPIVISDSGIPPMSSTNTLTIKVCGCDVNGALLSCNAEAYILNAGLSTGALIAILACIVILLVIVVLFVTLRRQKKEPLIVFEEEDVRENIITYDDEGGGEEDTEAFDIATLQNPDGINGFIPRKDIKPEYQYMPRPGLRPAPNSVDVDDFINTRIQEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESATTDSDLDYDYLQNWGPRFKKLADLYGSKDTFDDDS
Protein: Serologically defined colon cancer antigen 8 homolog (B8JK76)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in the establishment of cell polarity and epithelial lumen formation. Also plays an essential role in ciliogenesis and subsequent Hedgehog signaling pathway that requires the presence of intact primary cilia for pathway activation. Mechanistically, interacts with and mediates RABEP2 centrosomal localization which is critical for ciliogenesis (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q86SQ7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q86SQ7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q86SQ7}. Cell junction {ECO:0000250|UniProtKB:Q86SQ7}. Note=Located at the distal ends of both centrioles and colocalizes to centrosomes throughout the cell cycle. {ECO:0000250|UniProtKB:Q86SQ7}.
Interaction partners:
- Serine/threonine-protein kinase PLK
- Centrosomal protein of 290 kDa
- Bardet-Biedl syndrome 1.
- Nephrocystin-3
- Si:dkey-202c5.1 protein.
- Bardet-Biedl syndrome 12
- Abelson helper integration site 1.
- Centriole and centriolar satellite protein ofd1
- Nephronophthisis 1.
- IQ calmodulin-binding motif-containing protein 1
Sequence:
MKPSLESDEEEELGALQKTLRERANRSIQHLSSMLAGHSSDSETSEPNQQELLSSVQQNPCSPVQQSEAVSQLRSLLQMKTKDANIQSLSPSRRKLAAKRATDDGSSSQPGVHNLVPIINNQSEYIQHLEAEVKFCKEELLEMKQRVRVVIVENEKLHHELKAKTIEDTLKEYTFVDSTLNMEHTAENTLKERLGSVNQAEDHKWRKEMEQLKCLYQAQTETLEAQVVSLKKDLACIQKEYEESKERLRHKEAMAVAAGTGQRVSGLCLKCAQHEAVLAETHTNVHVQSIERLTKERDELMTVLCSLRASQTDAQQREWGAYQQVKQAVEMAEEANLEKTRALVQCEHFHNELTRQRERLERELASEQDKISQAREAARSESKKEREELMQTLSSLSQKVAELQGLLDRGERDRNSLNSQLEEAYKKLTVQETDSSKMCAELRFLLSQAQLKKEEAERDVRDISSKLGRQLELAEQEVQKLGVELSGYRQRLEEAQRAEGRARAEAAGLAEGLSRAQRQLHLTRQEKEASERCCGEDMAALTFQAQRRERELTQTLQQMEAQHEKSVRETDALLSAQNSLIRKLKEECHTLGAKLEELAQSSRAEMEQLSLEREHLQESAEKLRGRCEEMEEQCVQHGRMHQRMKQRLQQLDQHCQASSQQVLQLLSRQKQLMQERQQLTEDLHSLKSQVHAGKRMDRLAV
Protein: Muscleblind-like protein 2 (Muscleblind-like protein 1) (Muscleblind-like protein-like) (Muscleblind-like protein-like 39) (Q5VZF2)
Organism: Homo sapiens (Human)
Function: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. RNA-binding protein that binds to 5'ACACCC-3' core sequence, termed zipcode, within the 3'UTR of ITGA3. Binds to CUG triplet repeat expansion in myotonic dystrophy muscle cells by sequestering the target RNAs. Seems to regulate expression and localization of ITGA3 by transporting it from the nucleus to cytoplasm at adhesion plaques. May play a role in myotonic dystrophy pathophysiology (DM).
Subcellular location: Nucleus {ECO:0000269|PubMed:11929853}. Cytoplasm {ECO:0000269|PubMed:16273094}. Note=Greater concentration in the nucleus. Expressed in or near large cytoplasmic adhesion plaques (PubMed:16273094). Location in the cytoplasm is microtubule-dependent (PubMed:16273094). In both DM1 and DM2 patients, colocalizes with nuclear foci of retained expanded-repeat transcripts (PubMed:11929853).
Interaction partners:
- CCHC-type zinc finger nucleic acid binding protein
- CUGBP Elav-like family member 1
- KH domain-containing RNA-binding protein QKI
- Chloride channel protein 1
- Myotonin-protein kinase
- Muscleblind-like protein 1
Sequence:
MALNVAPVRDTKWLTLEVCRQFQRGTCSRSDEECKFAHPPKSCQVENGRVIACFDSLKGRCSRENCKYLHPPTHLKTQLEINGRNNLIQQKTAAAMLAQQMQFMFPGTPLHPVPTFPVGPAIGTNTAISFAPYLAPVTPGVGLVPTEILPTTPVIVPGSPPVTVPGSTATQKLLRTDKLEVCREFQRGNCARGETDCRFAHPADSTMIDTSDNTVTVCMDYIKGRCMREKCKYFHPPAHLQAKIKAAQHQANQAAVAAQAAAAAATVMAFPPGALHPLPKRQALEKSNGTSAVFNPSVLHYQQALTSAQLQQHAAFIPTGSVLCMTPATSIDNSEIISRNGMECQESALRITKHCYCTYYPVSSSIELPQTAC
Protein: AT-rich interaction domain 1B (A0A1B0GWJ2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPPQPPGSQSESSSHPALSQSPMPQERGNYSRPPAYSGVPSASYSGPGPGMGISANNQMHGQGPSQPCGAVPLGRMPSAGMQNRPFPGNMSSMTPSSPGMSQQGGPGMGPPMPTVNRKAQEAAAAVMQAAANSAQSRQGSFPGMNQSGLMASSSPYSQPMNNSSSLMNTQAPPYSMAPAMVNSSAASVGLADMMSPGESKLPLPLKADGKEEGTPQPESKSKDSYSSQGISQPPTPGNLPVPSPMSPSSASISSFHGDESDSISSPGWPKTPSSPKSSSSTTTGEKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFECKIERGEEPPPEVFSTGDTKKQPKLQPPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQGGRSSTISVHDPFSDVSDSSFPKRNSMTPNAPYQQGMSMPDVMGRMPYEPNKDPFGGMRKVPGSSEPFMTQGQMPNSSMQDMYNQSPSGAMSNLGMGQRQQFPYGASYDRRHEPYGQQYPGQGPPSGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGDMYNMQYSSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQTHGIPPQMMGGPLQSSSSEGPQQNMWAARNDMPYPYQNRQGPGGPTQAPPYPGMNRTDDMMVPDQRINHESQWPSHVSQRQPYMSSSASMQPITRPPQPSYQTPPSLPNHISRAPSPASFQRSLENRMSPSKSPFLPSMKMQKVMPTVPTSQVTGPPPQPPPIRREITFPPGSVEASQPVLKQRRKITSKDIVTPEAWRVMMSLKSGLLAESTWALDTINILLYDDSTVATFNLSQLSGFLELLVEYFRKCLIDIFGILMEYEVGDPSQKALDHNAARKDDSQSLADDSGKEEEDAECIDDDEEDEEDEEEDSEKTESDEKSSIALTAPDAAADPKEKPKQASKFDKLPIKIVKKNNLFVVDRSDKLGRVQEFNSGLLHWQLGGGDTTEHIQTHFESKMEIPPRRRPPPPLSSAGRKKEQEGKGDSEEQQEKSIIATIDDVLSARPGALPEDANPGPQTESSKFPFGIQQAKSHRNIKLLEDEPRSRDETPLCTIAHWQDSLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEVLRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLILATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDALAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNLMHMQPPPLEPPSVDMMCRAAKALLAMARVDENRSEFLLHEGRLLDISISAVLNSLVASVICDVLFQIGQL
Protein: 50S ribosomal protein L13, putative (Q580D5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 50S ribosomal protein L17, putative
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- Uncharacterized protein
- Large ribosomal subunit protein uL3m
- 30S Ribosomal protein S17, putative
- Ribosomal protein L11, putative
- 40S ribosomal protein S5, putative
- Large ribosomal subunit protein bL21m
- 50S ribosomal protein L2, putative
- KOW domain-containing protein
Sequence:
MQRSTRIVMAPFKSVLRRHKHHPEGLPLYNDMSKQWLCREGERWWLLDARGEQLPRVAAVAAQYITGQHRPDFTPGMITGDHVVIVNIKDVVMVGDQWIRVPITWQTAYPGGKYRIRLTDMYERDPCMLMWWFLKDEVNRHFVRKLKTRIAPLEKAWLYEDSIHPHADKNPRPLCWTDPEVKGWKYRDPQFIRRWKPNEFMH
Protein: P2X receptor A (DdP2X) (P2XA) (Q86JM7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: P2X receptors are ATP-gated ion channels that play a role in intracellular calcium signaling. Not required for the purinergic response to extracellular nucleotides. Inward currents evoked by intracellular ATP and ATP analogs. Exclusively selective for ATP over other nucleotides. Insensitive to P2 receptor antagonists PPADS, suramin and 2',3'-O-(2,4,6-trinitrophenyl)-ATP but inhibited by nanomolar concentrations of copper and sodium ion. More permeable to ammonium than either sodium or potassium ions and less permeable to choline. It has been reported that p2xA is not essential for osmoregulation, however this information is in contradiction with another source which indicates that p2xA is required for osmoregulation. Found to be permeable to chloride ions. Inhibited by copper and sodium ions.
Subcellular location: Contractile vacuole membrane {ECO:0000269|PubMed:17625565, ECO:0000269|PubMed:19833731}. Note=Ligand binding domain within the lumen of the vacuole.
Interaction partners:
Sequence:
MGFSFDWDDIFQYSTVKIVRIRDRRLGILHLSFLVGIVAYIVVYSAIIKKGYLFTEVPIGSVRTSLKGPNTFASNLTYCSNQQHNGSTYPFTPLECNYWDEQLALFPVGQDSTFTCTTRVRLSKQEANCNFTDPTCKFVDEPGSAKNIYIADIESFTILIDHTMYASSSGSQFNAVDLHGYILNQDGDEVQIDANGTSIGVSGKPDIMTIGQLLSFGGVSLDQASPVDSNVSIRYDGVVLFVFITYSNTYTYSTSDFKYVYSVQQIANTIYDVPETIILESIHSRLLYKRHGIRVIFIQTGTIGSFHFQTLLLTLVSGLGLLAVATTVVDQLAIRLLPQRKSYSSLKFQVTESMSNPMKKRITTDEGEDVLYTRIEGL
Protein: Scm polycomb group protein like 2 (B1AVB3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGQTANEDHFDWDKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLNTSSWPMFLLRVLTGSELAPAVFFKEEPPRPLQNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPPGKIVEKRPRRKRRTRLWRLRTALLGNEEEAPAAEEPGTSVLTFGDENRTLKDCRGEAAEEPGTSAFTFGDENRTLKDCQGGWKKPKGRGFIKPGKDETRPGKHDQGAPAGKKPRGRGFTQPLEDEARPGRDVQVAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKRKGKTVTTPWTEDPRLFADQGAAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKRKGKTVTTPWTEDPRLFADQGAAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKPKGKRVTKSRKDQAQFLADEEAMPALFSALSVSSTERTPPSSSEQPKSSTSGKTKSTSRGAQTSRKSPRKTSVVQPVPKTSKKAGKSKSTGNTSSPKKGITIKIVLPKKKGGKSGKKEKSIPVISSTSSASLSTLMKSSSSNKTSAGPSKIVMSTVCVYINKHGDCGPFLDPQKVQQLPNHFGPGPVNVILQRTVQACVNCAFQAKDVFLFLKTDNRGGEMITAFFDGKVHTVQLPPVNSASFALRFLENFCQSLQCDNFLSSQPFRREAQVPTPDTGTDQSKPENGEPKEKRSLKRLSLHPHRSAPVSSKVPRKSGQASKASSYITVPDPSVLKQGFCKDPSTWSVDEVIQFMKHTDPQISGPLADLFRQHVTYLLIRFSCCPNASK
Protein: ALX homeobox protein 1 (Cartilage homeoprotein 1) (CART-1) (Q1LVQ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Sequence-specific DNA-binding transcription factor that binds palindromic sequences within promoters and may activate or repress the transcription of a subset of genes. Most probably regulates the expression of genes involved in the development of mesenchyme-derived craniofacial structures (By similarity). Required for proper neural crest cell migration into the frontonasal primordia during development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15699}.
Interaction partners:
Sequence:
MEYLSDKFSLKSPAIKGSDYYMDQVMDTLDNVQYYNKASPKCVQAFPMQSNDQHSSMDRSSPCDNQSSVTYCAPKSEESSLHAMENCCSLRVSPATSGPDKTDLDELGEKCDSNVSSSKKRRHRTTFTSAQLEELEKVFQKTHYPDVYVREQLAMRTELTEARVQVWFQNRRAKWRKRERYGQIQQAKSHFAATYDISMLPRTDSYSQISNNLWTGPSAGSSVVSSCMIPRGSPPCVTSPYPHSPRAAEHGYVGFPNHQQNQFGVNHVSLNNFFADSLLASSANSHAAFETKPEFERRSSSIAVLRMKAKEHTANISWAM
Protein: Annexin D1 (AnnAt1) (Annexin A1) (Q9SYT0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a peroxidase activity. May act in counteracting oxidative stress. May also mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development.
Subcellular location: Cytoplasm, cytosol. Membrane. Note=translocate from cytosol to membrane upon salt treatment; this translocation is calcium dependent.
Interaction partners:
- Protein NDL1
- Thioredoxin superfamily protein
- DEAD-box ATP-dependent RNA helicase 37
- DEAD-box ATP-dependent RNA helicase 11
- Probable cyclic nucleotide-gated ion channel 6
Sequence:
MATLKVSDSVPAPSDDAEQLRTAFEGWGTNEDLIISILAHRSAEQRKVIRQAYHETYGEDLLKTLDKELSNDFERAILLWTLEPGERDALLANEATKRWTSSNQVLMEVACTRTSTQLLHARQAYHARYKKSLEEDVAHHTTGDFRKLLVSLVTSYRYEGDEVNMTLAKQEAKLVHEKIKDKHYNDEDVIRILSTRSKAQINATFNRYQDDHGEEILKSLEEGDDDDKFLALLRSTIQCLTRPELYFVDVLRSAINKTGTDEGALTRIVTTRAEIDLKVIGEEYQRRNSIPLEKAITKDTRGDYEKMLVALLGEDDA
Protein: Ribosome biogenesis ATPase RIX7 (Q07844)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in ribosome biogenesis. Seems to be required for restructuring nucleoplasmic 60S pre-ribosomal particles to make them competent for nuclear export.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11447111}.
Interaction partners:
- Ribosome biogenesis protein NSA1
- Ribosome biogenesis protein YTM1
- Nucleolar GTP-binding protein 2
- Ribosome biogenesis protein ERB1
- Nucleolar complex-associated protein 3
- Ribosome biogenesis protein 15
- Nucleolar GTP-binding protein 1
- Nucleolar complex protein 2
- Probable metalloprotease ARX1
- rRNA-processing protein EBP2
Sequence:
MVKVKSKKNSLTSSLDNKIVDLIYRLLEEKTLDRKRSLRQESQGEEGENNEGEEDEDIFESMFFAKDLTAGEIFTFCLTKDLSLQRVKKVVLQKTIDRMLKDVIESELEEFGSYPGYNNEEEEKPSLEEELAKKNMMIERDTNEMNKRITSTWSKSGSVSESITETDDPKTEEVKKSKKRSKEGTCKVKRQKIKEDRSPPNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDELTMEKTNGKPVIIIGATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKRIFQTYANIKSTPTTATDSSEDNMEIDETANGDESSLKNTANMIDPLPLSVVQQFIRNYPEPLSGEQLSLLSIKYEDFLKALPTIQPTAKREGFATVPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKSHGTPLSSDVDFEEIIRNEKCNNFSGADLAALVRESSVLALKRKFFQSEEIQSVLDNDLDKEFEDLSVGVSGEEIIVTMSDFRSALRKIKPSVSDKDRLKYDRLNKKMGLTEEMKDAEEMKQ
Protein: Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (GMP-PDE gamma) (EC 3.1.4.35) (P18545)
Organism: Homo sapiens (Human)
Function: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.
Interaction partners:
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- cGMP-specific 3',5'-cyclic phosphodiesterase
- Guanylate kinase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
Sequence:
MNLEPPKAEFRSATRVAGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII
Protein: Ngs1p (A0A1D8PRM0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Beta-hexosaminidase
- Rep1p
- Chitinase 2
- Chitinase 3
- Chitinase 1
- Chitinase 4
- NDT80 domain-containing protein
Sequence:
MSTFYAGQLLCGGFQGTTVTPQAYHLIVEHHVSAMILSRKNAFNVEQMTKLIKDLQYIAMTEGRYKYPIMFAIDEEGGMMNSLFDPDFLTQYPGAMALAATGDPQLVYEISRAIAIEIKKIGFSIILGPVLDVVTKLSHQLVGVRSFGTTIEDVVKYGRMCAQGLQDGGLFTVGKHFPGIGNATVDSLLELPMMGDSLEQLRHFNVVPFEMLINEGLLDGISAAGCGVPNISPDETHACLSPVVINQLLRQELNFDGFVISECLEMEALYHSVGLGQGVILAINAGCDLVMVCHDMELQNEAIDSIKTAVVNGNLDEETVLKSLKRINKLQTRLPSWTQLFPEGEVSAKLPPTLFRNECPVVWEQHQKLSSLAYKKSITLIRDFDGTLPIPKHLSARGSDQIDSILLLTPLLNPIYPCKQTGSSQRLFTGEEVFQKFGDFLSNHPINKTKSYNVLHTTYTANGLTPLHESLIEQSKIVIFLTSEAGRNMYQIGIVKYVSILCGVNPLTLTKGLGPVQPRKPLIIVATSSPYDFFYNKSIGSAYLCCYDYTNNALENLASLLMGDFEAQGCVPGEKKFSTKHKKSAVEGRNENNHLSAKSVHKPKRRWLVDEFSMERDWQGLTKLLKTNSDQLTNDGFYKRLEGLLSSTAKHQKHFVVRNSSLNILYGIVLTWVNESNCGHLVYILVEKSKRLQSIGKNLHLRAIRYLIKERKCNEIVLGSSFPLISLGGNNNKPFFKGVGWNTQVSTEKSVMLLQNLDSWSVPQNILQEIMIVGVRFDICSDTSKLMKMMERCLSSEAYDAREYKNVKSLYSEAQKYLKINSPYEVKIILALEPTTQNVIGSIVIFTSNSQLSKFYPFIDVFGEENDSPGNRSIIGAIAGPVIDPSYSNLTEIFKYGLICSAITFLKTSLSEDNIKSCIMTDMGTEDKAMRGVKEIGFNVWKPYHDNYGYNSVNSNVESKFGL
Protein: All-trans-retinol 13,14-reductase (EC 1.3.99.23) (All-trans-13,14-dihydroretinol saturase A) (RetSat A) (All-trans-retinol 7,8-reductase) (Q5BLE8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol. In addition, saturates the 7-8 double bond of all-trans-retinol to produce all-trans-7,8-dihydroretinol. Can also use vitamin A2 (all-trans-3,4-didehydroretinol) as a substrate, to produce all-trans-13,14-dihydro-3,4-didehydroretinol or all-trans-7,8-dihydro-3,4-didehydroretinol. May play a role in vitamin A metabolism.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q64FW2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64FW2}.
Interaction partners:
- Lecithin retinol acyltransferase b, tandem duplicate 1.
- Cytochrome P450 27C1
- Cytochrome P450 26A1
- Dehydrogenase/reductase
- Lecithin retinol acyltransferase b, tandem duplicate 2.
- Short chain dehydrogenase/reductase family 16C, member 5a
- Epidermal retinol dehydrogenase 2
- Short-chain dehydrogenase/reductase 3
- Dehydrogenase/reductase
- Si:dkey-221h15.4
Sequence:
MWFAVVAIFLALVAFLYRYVVGSGPNPFAIDTREPLKPMVFDRKLKNKVLKQGFLASRVPEDLDAVVVGSGIGGLAIAVLLAKVGKKVLVLEQHDRAGGCCHTFKEQGFEFDVGIHYIGELSNHKPLRCIIDQMTNGQLQWDPLENPFDNVVIGPPENRRIYQIYSGRKRYMDELKKCFPGEEKAIDEYVRLCKEVGQGVWVMVLLKFLPTPIANFLVRTGLANRLTSFSRYASRSLTDVVNELTQNKDLRAVLSYIFGTYGKIPKEASFSMHSLIVNHYMNGAWYPKGGATEIAYHMIPIIEKAGGAVLVRAPVNRILLNDAKEAIGVSVLKGQEEVHVRAPIVISDAGIFNTYEYLLPKDVQTMPAIQKQLSMLQHGDSGLSIFIGLDGTKEELGLKADNYFIYPENNIDELLEDYRSGNREESAKKNPLIFVASPSAKDSTWPERTPGKSTLTVVSFANYEWFEEWKDDKVKNRSTDYKQLKELFINYILEAVTEIYPKIKDRIEYVDAGTPITNQHYIAAPRGEIYGADHGIPRFSAELNATIRAQTPIKNLYLTGQDLMLCGFAGALTGALTCGSVILNRNLHLEAFSLAKRVQNGNNKKKT
Protein: Phosphatidylinositol transfer protein PDR17 (PITP) (Phosphatidylserine transport B pathway protein 2) (Pleiotropic drug resistance protein 17) (SEC14 homolog 3) (P53844)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Contributes to efficient phospholipase D1 activation and phospholipase B1 inhibition in the regulation of phospholipid turnover. Forms a complex with phosphatidylserine decarboxylase PSD2 that seems essential for maintenance of vacuolar phosphatidylethanolamine (PE) levels.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12869188, ECO:0000269|PubMed:14562095}. Microsome {ECO:0000269|PubMed:12869188}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme 2
- Phosphatidylinositol transfer protein SFH5
- PSTB2-interacting protein 1
- SEC14 cytosolic factor
- Phosphatidylinositol 4-kinase STT4
- Oxysterol-binding protein homolog 4
- Phosphatidylinositol-3-phosphatase SAC1
Sequence:
MGLFSRKRDHTPAVPKEKLIPCDKIFLDPPAKYGNAPLLEPISEDQNEKYRAVLRHFQDDDLKLPENLNDLDNGTHANDRPLSDWEKFWLSRECFLRYLRANKWNTANAIKGLTKTLVWRREIGLTHGKEDKDPLTADKVAVENETGKQVILGFDNAKRPLYYMKNGRQNTESSFRQVQELVYMMETATTVAPQGVEKITVLVDFKSYKEPGIITDKAPPISIARMCLNVMQDHYPERLAKCVLINIPWFAWAFLKMMYPFLDPATKAKAIFDEPFENHIEPSQLDALYNGLLDFKYKHEVYWPDMVKKVDDLRLKRFDRFLKFGGIVGLSEYDTKGQHDELKYPVDMVI
Protein: Calmodulin-binding transcription activator, isoform B (B7YZU5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENVPDISTSASSSSTSNSTSTLKLQSQITSKNVLIRSQSSGKLSSNEAKSAKPAATTSTTTTLRAAKLKIGAMQQQKQQHQQQHQATSGGNIILLRGTRNENGQIIIQNKQDILSLLSEQQQQQQQEKSHSSTAITLNQLPTATTVARKTIVQGSSGAGSSSSSSSSTISIVANSNNKEASSNTILLQTPINASQLESVLKAQERSKQANATQTKMVERPFMLKHATRSLSSESNCDSKSPFVLQTLKRLEKSQSILVIRNSTASTAATNTSMATSPPNGNSLATSSILSVTRTTKAAKGVAGALHKLKAAAATTATSGGASSAGATSSTATTILRLGKSATTVAINGASKLEATTSTTTAVPVPATATTSNKLSNAVTSEQQQQQQQQSTTTQTNVPLGNDGEPIKLPDNLESLPRADSFPSQRHRWNTNEEIAAILISFDKHGEWQSKEVRTRPKSGSLLLYSRKKVRYRRDGYCWKKRKDGKTTREDHMKLKVQGTECIYGCYVHSAILPTFHRRCYWLLQNPDIVLVHYLNVPYPDDNKMAVIAPSITLWGDKKEWTKEELVSQLKPMLSTINSDDDSDSGNDIEISTAETVESIVCQLMEKQRLSRQAALVKQLDCGCGDGGCVDGKTCTHPVMRRSAAMLKSSVQEKRLGEPFNGNTPNVVVASKLYSRWAERPRQHVDNHGQFHNVTQQLPQESAIKFQIIPPQQQQQQDGNYQQQQYRGGSQMLAARSNLVMQQQQQHQQQQQYHQQQQQQQQQQQQHQQQQQHLSLQRFVASQGQNSVHLNQQHRLQIANTTITATASDPATTLAAAAAVAAASGATPVALNIMDTELIENQNHMTANKITNSGSSNSSSSNASKQLAGQTNNKLNVVNNNDPGNNNFMYNQQQQLNASSNSNNSSQQQQQQQQQHYYKLQQTTATPTSGQPPPLAQVQPHSLAQPPVEAMCMSPEHRSSSQPTPATSSAGSIPSSVSVSISVSTSTPTPAPTSISTPTSGTSSTSSSLQSIIDGNQQQQITTTSTAATCDNLMSANALSEQDSHTVNNQATEAPNRSQLQSQSQSLSLNQNGCATYSASSDNSSQISDESSSFGGNNQNSSNSSTSEEEPQVEALSFFNETLDLSQEDIQRTLIANMPYNTTAAGATAPSTTITTGNTKLELSQQETKEKPAMGTETATEIEDDETDDVFANLDAFDMLVEFPELDLDDKQALNNTALEQSSFLGESAPSQPRKVHNICDFSPEWSYTEGGVKVLVAGPWTSSNGGAYTVLFDAQPVPTQLVQEGVLRCYCPAHEAGFVTLQVACGGFLVSNSVMFEYKLSLLADAPFDATSSNDCLYKFTLLNRLSTIDEKLQVKTEHELTTDNTALYLEPNFEEKLVAYCHKLIKHAWSMPSTAASWTVGLRGMTLLHLAAALGYAKLVGAMLNWRSENPHIILETELDALSQDVYGFTPLAWACVRGHVECSLLLYKWNHNALKIKTQAQQTPLDLASMRGHKVLLAQMYRLEKERCRKPQLRGGLANLSMNMGVEAEAEEQHQSFSAFDLELQRKHDGVFLRPVAVHSNQSPPNGSSRYSKRSSIDSGINMDIRSKSGKPLARLHSNFESHDSYALGVDSPLDSLTGTNCLLSPLRKMDFALWDSDAKVLTLAEHIIAAMPERIKNEADEMMVLGSPLTEPLTSESSALTDSFMDPLLDSLPNTHFDSDFSFDFHDHSYRYHDVSTPCSSLSPASSGPLQSPASYSILGTDPSVSSPSPPPSTKQLTEFLHASSISSYPFEADFSKLTLTDTEQRELYEAAKCIQKAYRSYKGRQKLEEQNKERSAATVIQNYYRRYKQYAYYRQMTNAALVIQHGYRSYRRNKRFKKSGLCLSSSSDHGSVSSNSQCLSSFYDHYKQDQQQLHELGSQPSTPKETSPSGPLKRTYSQSTQNQAARKIQQFMRQSRIKLQKERAEKEKLVHQRRAEYLQNLQFQGQQEMLVYHENNISAPSSGNTNASNNNNLHQIQSNQ
Protein: Synaptotagmin-4 (Synaptotagmin IV) (SytIV) (Q9H2B2)
Organism: Homo sapiens (Human)
Function: Synaptotagmin family member which does not bind Ca(2+) (By similarity). Involved in neuronal dense core vesicles (DCVs) mobility through its interaction with KIF1A. Upon increased neuronal activity, phosphorylation by MAPK8/JNK1 destabilizes the interaction with KIF1A and captures DCVs to synapses (By similarity). Plays a role in dendrite formation by melanocytes.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000250|UniProtKB:P50232}; Single-pass membrane protein {ECO:0000250|UniProtKB:P50232}.
Interaction partners:
- Synaptosomal-associated protein 25
- Complexin-1
- Kinesin-like protein KIF1A
Sequence:
MAPITTSREEFDEIPTVVGIFSAFGLVFTVSLFAWICCQRKSSKSNKTPPYKFVHVLKGVDIYPENLNSKKKFGADDKNEVKNKPAVPKNSLHLDLEKRDLNGNFPKTNLKPGSPSDLENATPKLFLEGEKESVSPESLKSSTSLTSEEKQEKLGTLFFSLEYNFERKAFVVNIKEARGLPAMDEQSMTSDPYIKMTILPEKKHKVKTRVLRKTLDPAFDETFTFYGIPYTQIQELALHFTILSFDRFSRDDIIGEVLIPLSGIELSEGKMLMNREIIKRNVRKSSGRGELLISLCYQSTTNTLTVVVLKARHLPKSDVSGLSDPYVKVNLYHAKKRISKKKTHVKKCTPNAVFNELFVFDIPCEGLEDISVEFLVLDSERGSRNEVIGQLVLGAAAEGTGGEHWKEICDYPRRQIAKWHVLCDG
Protein: Protein IDA (Protein INFLORESCENCE DEFICIENT IN ABSCISSION) (Q8LAD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in an ethylene-independent separation step of floral abscission. Promotes abscission zone (AZ) cells rounding. May act with RLK5 and HSL2 as ligand-receptor pairs.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:12972671}.
Interaction partners:
- Receptor-like protein kinase 5
- Receptor-like protein kinase HSL1
- Somatic embryogenesis receptor kinase 1
- LRR receptor-like serine/threonine-protein kinase HSL2
- At2g23270
- PAMP-induced secreted peptide 2
- Protein IDA-LIKE 4
- At4g37295
- Transmembrane protein
- Protein IDA-LIKE 2
Sequence:
MAPCRTMMVLLCFVLFLAASSSCVAAARIGATMEMKKNIKRLTFKNSHIFGYLPKGVPIPPSAPSKRHNSFVNSLPH
Protein: Serine (Or cysteine) peptidase inhibitor, clade F, member 1 (Q80ZA3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Low-density lipoprotein receptor-related protein
- LDL receptor related protein 5
- Plasminogen
- Tissue-type plasminogen activator
Sequence:
MQTLVLLLWTGALLGHGSSQNVPDSSQDSPAPDSTGEPVVEEDDPFFKAPVNKLAAAVSNFGYDLYRLRSGAVSTGNILLSPLSVATALSALSLGAEQRTESVIHRALYYDLINNPDIHSTYKELLASVTAPEKNFKSASRIVFERKLRVKSSFVAPLEKSYGTRPRILTGNPRIDLQEINNWVQAQMKGKIARSTREMPSALSILLLGVAYFKGQWATKFDSRKTTLQDFHLDEDRTVRVPMMSDPKAILRYGLDSDLNCKIAQLPLTGSMSIIFFLPLTVTQNLTMIEESLTSEFVHDIDRELKTIQAVLTVPKLKLSYEGDVTNSLQDMKLQSLFESPDFSKITGKPVKLTQVEHRAAFEWNEEGAGTSSNPDLQPVRLTFPLDYHLNRPFIFVLRDTDTGALLFIGRILDPSST