wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein mL51 (39S ribosomal protein L51, mitochondrial) (L51mt) (MRP-L51) (bMRP-64) (bMRP64) (Q9CPY1)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q4U2R6}.
Interaction partners:
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein mL48
- Small ribosomal subunit protein bS18m
- Large ribosomal subunit protein mL45
- Large ribosomal subunit protein mL50
- Large ribosomal subunit protein mL55
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein uL29m
Sequence:
MAGSVPWAASRRLWGWVPSACRSFSLGVPRLAFVRLTLPPPKVVDRWNEKRALFGVYDNIGILGNFEKHPKELIKGPVWLRGWRGNELQRCVRKKKFVGNRMFIEDLHNLNKRISYLYKHFNRHGKYR
Protein: T. brucei spp.-specific protein (Q4GZ43)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVWLHWTTEQIMERKGHARVKFVCFPNFILLILFPFLLLVFTLLGDLFFLFYCYVQSLTPSPLIFNFFSRFFFFLLFDKLFHSPQRDIFLYPLTVFFSLFFSFVEVAVCLPHICFFFFTLVDCEEQMRQFIFYLPHFSSITFLSLK
Protein: Bromodomain containing 8 (H0YA84)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
GSKAPSIDGKEELDLAEKMDIAVSYTGEELDFETVGDIIAIIEDKASPESMLSPSHGSNPIEDPLEAETQHKFEMSDSLKEESGTIFGSQIKDAPGEDEEEDGVSEAASLEEPKEEDQGEGYLSEMDNEPPVSESDDGFSIHNATLQSHTLADSIPSSPASSQFSVCSEDQEAIQAQKIWKKAIMLVWRAAANHR
Protein: Ammonium transporter 1 (Q9C0V1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transporter for ammonium to use as a nitrogen source. Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal growth.
Subcellular location: Membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSSTTDATPTPSGVNGGDSMTVNLNQFYNNGDVAWILTSTALVFIMIPGVGFFYSGLARRRSAISMLFLSMMSVAIVAFQWFFWGYSLTFSHEGGPYIGSLANFGLRQTLGRPSSGASSVPDILFCVFQGMFAAITPALAIGAAADRGRMFPCMVFMFLWTSIVYDPIAFWTWNPNGWLNKLGSYDFAGGSPVHISSGMAALAYSIVIGKRCDHGTTKYRPHNVPHVVLGTVFLWFGWFGFNGGSSAAANMRGVMAVVVTHLAASVGGIVWCVIDFAKNRHWSVVGFCEGAVAGLVAITPGSGFVPPWAAVVIGALGAVFCYAATYLKKIIRVDDALDIFAEHGVGGMVGNILTALFAADYIEALDGSGTAYTGGWITHHYIQLGYQLADTVSCAAYSFAVSCALLFVMNYIPGLSLRVSREDEVLGLDKIELGESAYYYKDSTDEPPPITTSGVQYTSPTVSDSASNEKEQEHRAQNEAQKEEEYRAESEAQAPAI
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (A0A2U3TZV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSYWNLEKRNCVQYRRHFLVDNSVFHVERCMSVMQSGTQMIKLKRGTKGLVRLFYLDEHRTRLRWRPSRKSEKAKILIDSIYKVTEGRQSEIFHRQAEGNFDPSCCFTIYHGNHMESLDLITSNPEEARTWITGLKYLMAGISDEDSLAKRQRTHDQWVKQTFEEADKNGDGLLNIEEIHQLMHKLNVNLPRRKVRQMFQEADTDENQGTLTFEEFCVFYKMMSLRRDLYLLLLSYSDKKDHLTVEELAQFLKVEQKMNNVTTDYCLDIIKKFEVSEENKVKNVLGIEGFTNFMRSPACDIFNPLHHEVYQDMDQPLCNYYIASSHNTYLTGDQLLSQSKVDMYARVLQEGCRCVEVDCWDGPDGEPVVHHGYTLTSKILFRDVVETINKHAFVKNEFPVILSIENHCSIQQQRKIAQYLKGIFGDKLDLSSVDTGECKQLPSPQSLKGKILVKGKKLPYHLGDDAEEGEVSDEDSADEIEDECKFKLHYSNGTTEHQVESFIRKKLESLLKESQIRDKEDPDSFTVRALLKATHEGLNAHLKQSPDVKESGKKSHGRSLMTNFGKHKKTTKSRSKSYSTDDEEDTQQSTGKEGGQLYRLGRRRKTMKLCRELSDLVVYTNSVAAQDIVDDGTTGNVLSFSETRAHQVVQQKSEQFMIYNQKQLTRIYPSAYRIDSSNFNPLPYWNAGCQLVALNYQSEGRMMQLNRAKFKANGNCGYVLKPQQMCKGTFNPFSGDPLPANPKKQLILKVISGQQLPKPPDSMFGDRGEIIDPFVEVEIIGLPVDCCKDQTRVVDDNGFNPVWEETLTFTVHMPEIALVRFLVWDHDPIGRDFVGQRTVTFSSLVPGYRHVYLEGLTEASIFVHITINEIYGKNRQLQGLKGLFNKNPRHSSSENNSHYVRKRSIGDRILRRTASAPAKGRKKSKMGFQEMVEIKDSVSEATRDQDGVLRRTTRSLQARPVSMPVDRNLLGALSLPVSETAKDIEGKENSLAEDKDGRRKGKASIKDPHFLNFNKKLSSSSSALLHKDTSQGDTIVSTAHMSVTGEQLGMSSPRGGRTTSNATSNCQENPCPSKSLSPKQHLAPDPVVNPTQDLHGVKIKEKGNPEDFVEGKSILSGSVLSHSNLEIKNLEGNRGKGRAATSFSLSDVSMLCSDIPDLHSTAILQESVISHLIDNVTLTNENEPGSSISALIGQFDETNNQALTVVSHLHNTSVMSGHCPLPSLGLKMPIKHGFCKGKSKSSFLCSSPELIALSSSETTKHATNTVYETTCTPISKTKPDDDLSSKAKTAALESNLPGSPNTSRGWLPKSPTKGEDWETLKSCSPASSPDLTLEDVIADPTLCFNSGESSLVEIDGESENLSLTTCEYRREGTSQLASPLKLKYNQGVVEHFQRGLRNGYCKETLRPSVPEIFNNIQDVKTQSISYLAYQGAGFVHNHFSDSDAKMFQTCVPQQSSAQDMHVPVPKQLAHLPLPALKLPSPCKSKSLGDLTSEDIACNFESKYQCISKSFVTTGIRDKKGVTVKTKSLEPIDALTEQLRKLVSFDQEDNCQVLYSKQDANQLPRALVRKLSSRSQSRVRNIASRAKEKQEANKQKVPNPSNGAGVVLRNKPSAPTPAVNRHSTGSYIAGYLKNTKGGGLEGRGIPEGACTALHYGHVDQFCSDNSVLQTEPSSDDKPEIYFLLRL
Protein: (Lyso)-N-acylphosphatidylethanolamine lipase (EC 3.1.1.-) (Alpha/beta hydrolase domain-containing protein 4) (Abhydrolase domain-containing protein 4) (Alpha/beta-hydrolase 4) (Q8VD66)
Organism: Mus musculus (Mouse)
Function: Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine.
Interaction partners:
- Glycerophosphodiester phosphodiesterase 1
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Lysophosphatidylserine lipase ABHD12
- Monoacylglycerol lipase ABHD6
- Monoglyceride lipase
- Fatty-acid amide hydrolase 1
- N-acylethanolamine-hydrolyzing acid amidase
Sequence:
MADDLEQQPQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVTVSPEQKDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPTFPRDPEGAEDEFVASIETWRETMGIPTMILLGHSLGGFLATSYSIKYPERVKHLILVDPWGFPLRPTDPSEIRAPPTWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGANTWIDTSTGKKVKMQRPDSYVRDMEIEGASHHVYADQPHIFNAVVEEICNSVD
Protein: ADP-ribosylation factor-like protein 3 (Q1MTE5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Required for targeting proteins to the ciliary membrane by releasing myristoylated protein from unc119 cargo adapters into the cilium (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, cilium {ECO:0000250}. Note=Detected predominantly in the photoreceptor connecting cilium. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. Present on the mitotic spindle (By similarity). {ECO:0000250}.
Interaction partners:
- Protein XRP2
- Protein unc-119 homolog A
- Protein unc-119 homolog B
- Protein unc-119 homolog A
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Cilia- and flagella-associated protein 36
- Nephrocystin-3
- Protein unc-119 homolog B
- Intraflagellar transport protein 20 homolog
- small monomeric GTPase
Sequence:
MGLLSILRKLKSTPDQEVRILLLGLDNGGKTTLLKQLASEDITHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDSADRKRFEETGQELAELLDEEKLSGVPVLVFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKSVNAKRK
Protein: Dynein regulatory complex subunit 7 (Q17968)
Organism: Caenorhabditis elegans
Interaction partners:
- ANK_REP_REGION domain-containing protein
- Nuclear exosome regulator NRDE2
- Argonaute protein hrde-1
- Nuclear RNAi defective-3 protein
- SET domain-containing protein
- Chromo domain-containing protein.
- Histone-lysine N-methyltransferase set-25
- Piwi-like protein 1
Sequence:
MEIDWLNAIPDSEDSEEDEEERQERARLLKEKEEEREACKKRYLERIEREEAQRFGKQFKIDPLTFAERLERKLIPAEKKQRYREFIPCVVDHFGGTDVHFVKAMESIKTENQLLDFLTAAHKPLIEQTEDSVLHDWLAEFYKETVTSLLEMTSITDHDLKCFKVGNVFDEVRTNAIQKKVQKMEMENFAERVREAKIKEAEERKATAEATRDVLESLEGMTLSHVKHDELEDELNTIALEELHSTTRDTSPPRTRLSTRAQSQLNAMVKHLFVPAAPTTSTEVPMEMDKDDDEMDAYDDSDLKILFSSTTKESLKMEMGEENDECNFEPSQVSKYPSFQASSQFDETRRYDYDEEGDNKELARLRRPTWRKILNYEKRIGTNFHRFTNAENANLWRRNLYEDKRKKTSKVQFVDYDSPLNKMRLFVRPNEQFFNADDGPMTDRIDFSLSDGFNVLATRKIMSPLVCGSNYDCEFMARTREGPQYLVRKTQSWMHSYCGNILGRFWYLRDRHADKYPGVKDSNYDQKRRQNFGLLRYYTLEELIEVFGLLLPDVQIAMRRGVRRENMPVSTVVKLKEKDREAVESPVQGVLLLTDWRLVHLFDNTAIVNAIIHYFPTNLGGVFFEAMTEYLTELLLDNTIEFHTIIFAFGGTPTFKKQDFLAFWKKLIVRTTQSIDVFWMAQDWCDGLNSTQEEIDQLNEFNHYVEQMFTMMRKNGNINYNYCDIRKQYNIPSLDPSFNRPNDFLLLEPIYRAYINHFVDECNCYLKGPFVKCQPRVHNGYAQRNGTKLEFSK
Protein: Semaphorin-7A (CDw108) (JMH blood group antigen) (John-Milton-Hargen human blood group Ag) (Semaphorin-K1) (Sema K1) (Semaphorin-L) (Sema L) (CD antigen CD108) (O75326)
Organism: Homo sapiens (Human)
Function: Plays an important role in integrin-mediated signaling and functions both in regulating cell migration and immune responses. Promotes formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and MAPK3. Promotes production of pro-inflammatory cytokines by monocytes and macrophages. Plays an important role in modulating inflammation and T-cell-mediated immune responses. Promotes axon growth in the embryonic olfactory bulb. Promotes attachment, spreading and dendrite outgrowth in melanocytes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Extracellular side {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}. Note=Detected in a punctate pattern on the cell membrane of basal and supra-basal skin keratinocytes.
Interaction partners:
- Plexin-C1
- Integrin beta-1
- Integrin alpha-1
- Plexin-A1
- Plexin-B1
- Neuropilin-1
- Plexin-A4
- Plexin-A3
Sequence:
MTPPPPGRAAPSAPRARVPGPPARLGLPLRLRLLLLLWAAAASAQGHLRSGPRIFAVWKGHVGQDRVDFGQTEPHTVLFHEPGSSSVWVGGRGKVYLFDFPEGKNASVRTVNIGSTKGSCLDKRDCENYITLLERRSEGLLACGTNARHPSCWNLVNGTVVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNGKIPRFRRIRGESELYTSDTVMQNPQFIKATIVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSGQWRDTRVYGVFSNPWNYSAVCVYSLGDIDKVFRTSSLKGYHSSLPNPRPGKCLPDQQPIPTETFQVADRHPEVAQRVEPMGPLKTPLFHSKYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGEQEHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPLDLCEVYGGGCHGCLMSRDPYCGWDQGRCISIYSSERSVLQSINPAEPHKECPNPKPDKAPLQKVSLAPNSRYYLSCPMESRHATYSWRHKENVEQSCEPGHQSPNCILFIENLTAQQYGHYFCEAQEGSYFREAQHWQLLPEDGIMAEHLLGHACALAASLWLGVLPTLTLGLLVH
Protein: Patulin synthase (EC 1.1.-.-) (Dehydrogenase patE) (Patulin biosynthesis cluster protein E) (A0A075TRK9)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: Patulin synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatE catalyzes the last step of the pathway which is the conversion of E-ascladiol to patulin. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:30680886}. Vacuole {ECO:0000269|PubMed:30680886}. Secreted {ECO:0000269|PubMed:30680886}. Secreted, cell wall {ECO:0000269|PubMed:30680886}.
Interaction partners:
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphoesterase
- aldehyde dehydrogenase
- CDP-alcohol phosphatidyltransferase
Sequence:
MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARKEIVLSAGAFQSPQLLMVSGVGPAATLKAHNIPLVADRPGVGQNMQDHIIYAPSYRVNVITQSALLNEEFEAQANRDYNERAAGIYANPTSDILAWEKIPEPKRSAWFSNHTRQVLAEYPDDWPEVEFLTMGGYFGYQRNYIRDNPSDGYNYASLAVSLCTPRSRGNVTITSPDAGVPPVINPNWLTDPVDVELAVAAFKRTRDFFNTTAIKPILIGPEYFPGSQVATDAEILDHVRKSFDTIFHASCTCAMGLANDTQAVVDSKARVIGVEALRVVDASALPFLPPGHPQSTLYALAEKIACEISGNC
Protein: Probable U2 small nuclear ribonucleoprotein A' (U2 snRNP A') (Q9V4Q8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in pre-mRNA splicing as component of the spliceosome (By similarity). Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA (By similarity). In the germ line, has a role in oogenesis, by regulating spermatogenesis and nurse cell nuclei chromatin decondensation and dispersal, probably by regulating the splicing of proteins necessary for germline differentiation such as the meiotic protein mei-P26.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein Sm D3
- Splicing factor 3B subunit 1
- Probable small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein Sm D1
- Splicing factor 3B subunit 3
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein-associated protein B
- Splicing factor 3A subunit 1
Sequence:
MVKLTPELINQSMQYINPCRERELDLRGYKIPQIENLGATLDQFDTIDLSDNDLRKLDNLPHLPRLKCLLLNNNRILRISEGLEEAVPNLGSIILTGNNLQELSDLEPLVGFTKLETICLLINPVSTKPNYREYMAYKFPQLRLLDFRKIKQKDRQAAQEFFRTKQGKDVLKEISRKSKMSAAAAIAAEAGNGKGRGSEGGRLANPQDMQRIREAIKRASSLAEVERLSQILQSGQLPDKFQHEMEAVAQNGAGHNGSGAVAMEY
Protein: Sushi domain-containing protein 2 (Q9UGT4)
Organism: Homo sapiens (Human)
Function: May be a cytokine receptor for GPR15LG. May be a tumor suppressor; together with GPR15LG has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest. May play a role in breast tumorigenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23131994, ECO:0000269|PubMed:25351403}; Single-pass type I membrane protein {ECO:0000305}. Note=SUSD2 and LGALS1 co-localized in very specific, punctate regions along the cell membrane of breast cancer cells. {ECO:0000269|PubMed:23131994}.
Interaction partners:
- Protein GPR15LG
Sequence:
MKPALLPWALLLLATALGPGPGPTADAQESCSMRCGALDGPCSCHPTCSGLGTCCLDFRDFCLEILPYSGSMMGGKDFVVRHFKMSSPTDASVICRFKDSIQTLGHVDSSGQVHCVSPLLYESGRIPFTVSLDNGHSFPRAGTWLAVHPNKVSMMEKSELVNETRWQYYGTANTSGNLSLTWHVKSLPTQTITIELWGYEETGMPYSQEWTAKWSYLYPLATHIPNSGSFTFTPKPAPPSYQRWRVGALRIIDSKNYAGQKDVQALWTNDHALAWHLSDDFREDPVAWARTQCQAWEELEDQLPNFLEELPDCPCTLTQARADSGRFFTDYGCDMEQGSVCTYHPGAVHCVRSVQASLRYGSGQQCCYTADGTQLLTADSSGGSTPDRGHDWGAPPFRTPPRVPSMSHWLYDVLSFYYCCLWAPDCPRYMQRRPSNDCRNYRPPRLASAFGDPHFVTFDGTNFTFNGRGEYVLLEAALTDLRVQARAQPGTMSNGTETRGTGLTAVAVQEGNSDVVEVRLANRTGGLEVLLNQEVLSFTEQSWMDLKGMFLSVAAGDRVSIMLASGAGLEVSVQGPFLSVSVLLPEKFLTHTHGLLGTLNNDPTDDFTLHSGRVLPPGTSPQELFLFGANWTVHNASSLLTYDSWFLVHNFLYQPKHDPTFEPLFPSETTLNPSLAQEAAKLCGDDHFCNFDVAATGSLSTGTATRVAHQLHQRRMQSLQPVVSCGWLAPPPNGQKEGNRYLAGSTIYFHCDNGYSLAGAETSTCQADGTWSSPTPKCQPGRSYAVLLGIIFGGLAVVAAVALVYVLLRRRKGNTHVWGAQP
Protein: FI21256p1 (Neuromusculin, isoform F) (M9NEJ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGNMALRQSAKDVAKSNCVAVRSSISLSLVLVLCLALVDSSTAQVDTTISQQESQSVVLPCPVDAEKCGKLHSLNWFKGDDRIAAMLLGDSNVTSVNKEFDERVTVEQNPYRLVIKDLKIADEDIYLCDTTFFIPEETCDNFNGYRIELRVLVPPTEVVILDAKGDRIKNGSVVGPMQERQSLKATCTVRNTRPQPEVSWFRGTKRLTTYSPTHDLVDGLYTSTLELDWTLSREDLAQDIECRVKSAAIQNVTVTKFSVDLQVRPTSIDINGVKHHTVQGSKVVLTCDIHGARPAVNLTWYNTTTIISSGENEITEVRSKSLEKSDGTFHTQSELIFNATRFENDRVFRCEAENIVLQINREKPISSALTLEVLYPPVVKVSPSAITANTSEIVLLNCEYFANPASLTQVEWYRNDILVNVNDTTHYKGGNSENVALVIKSTEKEDIGNYSCQLSNNIGKGTSDQKINLDVQYAPTVEILMIPEGPVKESDESNVTLFCNVLDANPSVLTKVRWYANSTLLKELPDCEETREDLCHIDPSKLLLESIGRGFFYNYSCEGFNAAGWGPRSEDKELLVHYEPGPAALSHFPLVAVKKKSVTFSCSVDDPGFPESNRFRWLRGGRGPLQDIVTKDWTVEPVGLDSRTNYSCYAYNEGGKGVMATVNLEVHAPPFFIKNLPPYTGILHSSPNATLTCRIECVPRCDISWQKDGVPIERNDSRYFIKEKYMDASPATGDFESMLSVLHFNMPNWPDSKFNIEADNANYSCVSTGNIVGGSIRSRTYFGIEYAPENTTVSENIVYVQEDTIPGRVICKSRANPEPSYKWIFKNETIANGNALIINTAMNRNDDGTYTCLAYNKHGSSIAKTVIKVQFKPRCEIERQEIDDQDTLICTAYGNPIEADFSWSIKTENETDENLGSGKKENSVEKSFYILQTDYAISRTYRCVANNTVGYGPFCEIEVAAASSLLVWWQEQLAWWQLWEKNTLIILVAAILGLLLTVIVICCIIICICRRRRRQDKLHDKSSSLREPLTEPGEYENLPFHGLQTAPNKPINAQIFDDEFIYADLESQHYGPINYKAASLYSQVKKNKESGALDDLK
Protein: Cellular tumor antigen p53 (A0A8I6ADJ7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.
Interaction partners:
Sequence:
MLYVGDPMRHLATAQFNLLSSAMDQMGSRAAPASPYTPEHAASAPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDIVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILVIITLETRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESTTKNGAASKRAFKQSPPAIPALGTNVKKRRHGDEDMFYMHVRGRENFEILMKVKESLELMELVPQPLVDSYRQQQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGVNKLPSVNQLVGQPPPHSSAAGPNLGSMGSGILNSHSHSMPANGEMNGGHSSQTMVSGSHCTPPPPYHADPSLVRTLGP
Protein: Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit [Includes: Biotin carboxylase (BC) (EC 6.3.4.14); Biotin carboxyl carrier protein (BCCP)] (P9WPQ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, resulting in the formation of carboxyl biotin. When associated with the beta1 subunit AccD1, is involved in branched amino-acid catabolism with methylcrotonyl coenzyme A as the substrate.
Interaction partners:
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase beta1 subunit
- Probable biotin-dependent acyl-coenzyme A carboxylase beta3 subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit
- Probable fatty acid synthase Fas
- Citrate lyase subunit beta-like protein
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex
- Biotinylated protein TB7.3
- Possible acyl-CoA dehydrogenase FadE19
- Biotin--[acetyl-CoA-carboxylase] ligase
Sequence:
MFDTVLVANRGEIAVRVIRTLRRLGIRSVAVYSDPDVDARHVLEADAAVRLGPAPARESYLDIGKVLDAAARTGAQAIHPGYGFLAENADFAAACERARVVFLGPPARAIEVMGDKIAAKNAVAAFDVPVVPGVARAGLTDDALVTAAAEVGYPVLIKPSAGGGGKGMRLVQDPARLPEALVSARREAMSSFGDDTLFLERFVLRPRHIEVQVLADAHGNVVHLGERECSLQRRHQKVIEEAPSPLLDPQTRERIGVAACNTARCVDYVGAGTVEFIVSAQRPDEFFFMEMNTRLQVEHPVTEAITGLDLVEWQLRVGAGEKLGFAQNDIELRGHAIEARVYAEDPAREFLPTGGRVLAVFEPAGPGVRVDSSLLGGTVVGSDYDPLLTKVIAHGADREEALDRLDQALARTAVLGVQTNVEFLRFLLADERVRVGDLDTAVLDERSADFTARPAPDDVLAAGGLYRQWALARRAQGDLWAAPSGWRGGGHMAPVRTAMRTPLRSETVSVWGPPESAQVQVGDGEIDCASVQVTREQMSVTISGLRRDYRWAEADRHLWIADERGTWHLREAEEHKIHRAVGARPAEVVSPMPGSVIAVQVESGSQISAGDVVVVVEAMKMEHSLEAPVSGRVQVLVSVGDQVKVEQVLARIKD
Protein: H.sapiens ras-related Hrab6 protein (RAB6A, member RAS oncogene family, isoform CRA_a) (A0A024R5J5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIIMLVGNKTDLADKRQVSIEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMESTQDRSREDMIDIKLEKPQEQPVSEGGCSC
Protein: F-box protein At1g30790 (Q9SY20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Integral membrane HRF1 family protein
- F-box/LRR-repeat protein At1g67190
- F-box/kelch-repeat protein At3g24760
- F-box protein At5g52880
- F-box/kelch-repeat protein At2g24250
- F-box/FBD/LRR-repeat protein At5g53840
- F-box protein At2g20380
- Putative F-box/kelch-repeat protein At1g60570
- FBD-associated F-box protein At4g10400
- Putative F-box/kelch-repeat protein At4g02310
Sequence:
MKRQEIDHIPFDLTVEILTRLPAKSLMKFKCVSKLWSSIIHNQSFIDSFYSISSTRPRFIVAFSNGSFPSDKEKRLFIFSSSHEGHESSSSVITNLDTTIPSLTVSNNLASRCISVNGFIACSLYTRFTICNPSTRQVIVLPILPSGRAPDMRSTCIGYDPVDDQFKALALISSCIPNKDSTVEHLVLTLKGDKKNYSWRQIQGNNNIPPYSPVTMRVCINGVVYYGAWTPRQSMNAVIVCFDVRSEKITFIKTPKDVVRWCNDSILMEYKGKLASIVRNRYSRFDTFDLWVLEDIEKQEWSKQTCEIPLSVWDSVENFNMSFPGINKFGEIILAPTCLSGYHLRSFYIFYYHVETKKIRRVRLEGIADDENFRRCYGIGSGQCNVFISPEHVETIRFL
Protein: Fez family zinc finger protein erm (Earmuff) (Q9VQ56)
Organism: Drosophila melanogaster (Fruit fly)
Function: Zinc-finger transcriptional repressor. In larval brain, involved in the maintenance of cell fate of intermediate neural progenitors (INPs) that derive from type II neuroblasts. Restricts INP developmental potential and dedifferentiation by interacting with HDAC3 and the chromatin remodeling Brahma-associated protein (BAP) complex. Restricts INP proliferation by regulating neuroblast specific factors such as prospero, pnt and grh, and by antagonizing the function of self-renewal factors, such as klu, dpn and E(spl)mgamma-HLH. In the optic lobe, essential for coordinating the innervation/ targeting of the L3 and R8 axons to the M3 layer of the medulla. Early in medulla development, functions in parallel to CadN and Sema1a pathways to promote targeting of the L3 growth cones to the proximal domain of the outer medulla possibly by controlling the expression of various cell surface genes such as dpr1 and dpr17 which function in L3 growth cone targeting. Then once L3 growth cones segregate into the developing M3 layer, it activates the expression of netrins NetA and NetB which act locally to promote the attachment of R8 growth cones within the M3 layer.
Subcellular location: Nucleus {ECO:0000269|PubMed:24550111, ECO:0000269|PubMed:27151950, ECO:0000269|PubMed:27510969, ECO:0000269|PubMed:28245922, ECO:0000269|PubMed:28899667}.
Interaction partners:
- Protein deadpan
- Achaete-scute complex protein T8
- Protein numb
- Enhancer of split mgamma protein
Sequence:
MVYFSPRGMQPCSPAGEIAMMPPSKSPVMESAASEQNPAQQSQQQDEQSAKRACPLKFSIAKIMEPDHRPSQVPPPQPAPVSFATNDDDEDEDPEIDADSERSCSPIEVISLDQSPSTVNYDSAFKKYVPGPCSGATSSVASPPSTAAVQQFVSSRHQELLSQYPLLYYAPNQLMCAAAAAQYAALTAQQQSLASAAHLSSFTASLNASLHHSQSLRRNLGHPLAAAAAVAAVAQSQAVPNLQHTLEKSPVAQRTAQSSGLQANLKRKRSPQDQGEVTPPPASTATSATGARSRSPSPQGSIEDSSPGSASGGKPKTFSCLECGKVFNAHYNLTRHMPVHTGARPFVCKVCGKGFRQASTLCRHKIIHTSEKPHKCQTCGKAFNRSSTLNTHSRIHAGYKPFVCEYCGKGFHQKGNYKNHKLTHSGEKAYKCNICNKAFHQVYNLTFHMHTHNDKKPYTCRVCAKGFCRNFDLKKHMRKLHEIGGDLDDLDMPPTYDRRREYTRREPLASGYGQASGQLTPDSSSGSMSPPINVTTPPLSSGETSNPAWPRSAVSQYPPGGFHHQLGVAPPHDYPSGSAFLQLQPQQPHPQSQQHHQQQQRLSETFIAKVF