wanglab/gogpt-training-data huggingface dataset:
Protein: Sex-determining transformer protein 1 (Cbr-tra-1) (Q17308)
Organism: Caenorhabditis briggsae
Function: Plays a major role in controlling sexual phenotype. Terminal global regulator in a well-characterized cascade of sex-determining genes (By similarity). Promotes female development (By similarity). Interacts with tra-2 to promote spermatogenesis. Promotes spermatogenesis through the Tip60 HAT complex and by regulating the expression of genes, such as fog-3, required for male development. Association with chromatin and at the fog-3 promoter requires wdr-5.1, and may also require wdr-5.2 (By similarity). With trr-1, activates the fog-3 gene to determine sperm/oocyte cell fate. In hermaphrodites, binds to an intronic regulatory site in the ceh-30 gene, preventing ceh-30 transcription and thereby preventing survival of the CEM (cephalic male) sensory neurons (By similarity). Represses the expression of the transcription factor dmd-3 in hermaphrodites to govern the timing and extent of male tail tip morphogenesis (By similarity). Plays a role in controlling the sex-specific differentiation of PHC sensory neurons and represses the development of male-specific morphological features (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P34708}. Cytoplasm {ECO:0000250|UniProtKB:P34708}. Note=Localization with chromatin in the nucleus in part depends on normal function of wdr-5.1. {ECO:0000250|UniProtKB:P34708}.
Interaction partners:
- Sex-determining transformer protein 2
- Sex-determination protein fem-3
- Protein CBR-DMD-3
- Protein CBR-HER-1
- Protein CBR-MAB-3.1
- Protein CBR-MAB-3.2
- XO lethal protein 1 homolog
- FOG-3
Sequence:
MMAPSTEDPETVVEAQRRGSFSKKNGNGWTKPGLANGSESKHMEPVTGTNALMAAIDADDQETKLKDPLEKEASTYKSATDRFFQSSHPPSHQTVENPIKLEPPTSSGVTQNGSPVTNSLVPEAAQPLQTVAESSEPTAASAEPTDASSAESSTITVTPVVPVVKFTNQTTPNGSTVATSVGQNVRLTINGKRVGRPPGTFKRPPNNPTTNTSHGEETDSEASTDLICRWKDCMLKFANLKGLVEHVQEKHVQSTEQEHHAWRCEWEGCDRNETFKALYMLIVHVRRHTGEKPNKCEYPGCGKEYSRLENLKTHRRTHTGEKPYKCEFSDCEKAFSNASDRAKHQNRTHSNLKPYSCQIGGCQKSYTDPSSLRKHIKAVHGDEEYEKAKKSRPPNYSNRRRPDHRMPPPTSAMSHPYLAPPHVLPPVAAPGVHQQNFINLALAQHHHNQRAQFIANNAALMDPNGSGAAQAAAAAQAAQAQQAQMYQAQAMQQHQFAAQMQQQAVMQVHMQQAALQQAQVAIIQNNLLSTQGIMNQFPMMSPLLTPRAPGNVMSLLQQQQVTPPTPTMMQLTPHTPITPITPITPLTPMGATTGPMFSMPNIMMTTPVRMDIPTSVPAAVPVAPVAPVAPVAPAAPVAPPASSLAEATEPRFRLLRQHMEGAEVAPVLAPQQPLEEDDDMTDDEESGNVAPAVIRNGDGPDDRNSGTGSSSPRSSASSGSGTLEVAGSVAQNGNRSSSTGERGMRSFLIADILQMAHDFQNGRIITDALHKAIFDTSDVTAMFHIYRTFECVCEYLQFTFSAGERLPTWPEVRTIHEYYHSDYDRTRFHASETVRRRDNLFWRFVNYCNSDLPIGGRPILSVSYDEGFEESIDQGSNFGTIPQQLISRMAAEAFDDEDDGFDDAFDIPGLRLGGVEVLIQQQRHRVRRAALKQAQIDYPTAEEDLGYVGGGFGQEDDDHHSYAIYEQQKTVAFVDLSEKPKVEVLTDEDFMEQFKAAEARCQARLAIEPMVKVARTVINGKVVEYTESQLFSPPVSRRTIYSMLKQFPEHQENLLKFITLHVDKCELENVIPSREYMSDMESSFFAHHRIVRAALRARGEITEAEEAEYQQSSNLMYNQDFAALMFPELDESHDDFLNDLPISSRRRSSDSDSKEAPSMKKPRSF
Protein: Chemotaxis protein methyltransferase (EC 2.1.1.80) (P07364)
Organism: Escherichia coli (strain K12)
Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Interaction partners:
- Chemotaxis protein CheW
- Methyl-accepting chemotaxis protein II
- Chemotaxis protein CheY
- Chemotaxis protein CheA
- Methyl-accepting chemotaxis protein I
- Protein phosphatase CheZ
- Methyl-accepting chemotaxis protein IV
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Aerotaxis receptor
- Flagellar motor switch protein FliN
Sequence:
MTSSLPCGQTSLLLQMTERLALSDAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHSGEWQAFINSLTTNLTAFFREAHHFPLLADHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRHEELKNLTPQQLQRYFMRGTGPHEGLVRVRQELANYVDFAPLNLLAKQYTVPGPFDAIFCRNVMIYFDQTTQQEILRRFVPLLKPDGLLFAGHSENFSHLERRFTLRGQTVYALSKD
Protein: Guanine nucleotide-binding protein subunit gamma (Q3KRE3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU004973}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU004973}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU004973}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- G protein subunit alpha transducin 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MSSGASVSALQRLVEQLKLEAGVERIKVSQAAAELQQYCIQNACKDALLLGVPAGSNPFREPRSCALL
Protein: Zinc-binding protein (Q50888)
Organism: Myxococcus xanthus
Interaction partners:
Sequence:
MIRVVTLDPFDDKQLAKFNRTLYTAFGVGSEHSDSVEVPAGMSEPLDAEKLIDEVKGIRSYKDDKVLLLTTRKLKDRELPSGVAPTAGFARQGKDRAILTIAPHKDLESAFKAVSRHALHQLGHLWELHHCLDPRCSMYPPWTPSFAQGEAIFCTFCREKSEQKIRLAKS
Protein: Acidic leucine-rich nuclear phosphoprotein 32 family member A (Acidic nuclear phosphoprotein pp32) (pp32) (Leucine-rich acidic nuclear protein) (LANP) (Mapmodulin) (Potent heat-stable protein phosphatase 2A inhibitor I1PP2A) (Putative HLA-DR-associated protein I) (PHAPI) (P39687)
Organism: Homo sapiens (Human)
Function: Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription. Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation. In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone-acetyltranferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking. Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition. Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A.
Subcellular location: Nucleus {ECO:0000269|PubMed:11830591, ECO:0000269|PubMed:18180367}. Cytoplasm {ECO:0000269|PubMed:18180367}. Endoplasmic reticulum. Note=Translocates to the cytoplasm during the process of neuritogenesis (By similarity). Shuttles between nucleus and cytoplasm. {ECO:0000250, ECO:0000269|PubMed:18180367}.
Interaction partners:
- Protein SET
- DNA repair nuclease/redox regulator APEX1
- Nucleoside diphosphate kinase A
- Exportin-1
- ELAV-like protein 1
- Prothymosin alpha
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Nuclear pore complex protein Nup214
- Granzyme A
- Ataxin-1
Sequence:
MEMGRRIHLELRNRTPSDVKELVLDNSRSNEGKLEGLTDEFEELEFLSTINVGLTSIANLPKLNKLKKLELSDNRVSGGLEVLAEKCPNLTHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLDGYDRDDKEAPDSDAEGYVEGLDDEEEDEDEEEYDEDAQVVEDEEDEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEELGEEERGQKRKREPEDEGEDDD
Protein: Initiation-specific alpha-1,6-mannosyltransferase (EC 2.4.1.232) (Outer chain elongation protein 1) (P31755)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). Adds the first alpha-1,6-mannose to the Man(8)GlcNAc(2) and Man(9)GlcNAc(2), but not Man(5)GlcNAc(2), endoplasmic reticulum intermediates. Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins. Has also the potential to transfer a second alpha-1,6-mannose to the Man(8)GlcNAc(2) core oligosaccharide.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14676282, ECO:0000269|PubMed:1628616}; Single-pass type II membrane protein {ECO:0000269|PubMed:8601597, ECO:0000303|PubMed:1628616}. Golgi apparatus membrane {ECO:0000269|PubMed:14676282, ECO:0000269|PubMed:15229219, ECO:0000269|PubMed:1628616}; Single-pass type II membrane protein {ECO:0000303|PubMed:1628616}. Note=Is recycled between the trans-Golgi network and a late compartment of the endoplasmic reticulum. {ECO:0000269|PubMed:14676282}.
Interaction partners:
- Mannan polymerase complexes subunit MNN9
- Mannan polymerase I complex VAN1 subunit
- Alpha-1,3-mannosyltransferase MNN1
- Osmosensing histidine protein kinase SLN1
- Probable alpha-1,6-mannosyltransferase MNN10
- Putative endoplasmic reticulum mannosidase MNL2
- Probable alpha-1,6-mannosyltransferase MNN11
- Mannan polymerase II complex ANP1 subunit
- Alpha-1,2-mannosyltransferase MNN2
- Transcription factor SKN7
Sequence:
MSRKLSHLIATRKSKTIVVTVLLIYSLLTFHLSNKRLLSQFYPSKDDFKQTLLPTTSHSQDINLKKQITVNKKKNQLHNLRDQLSFAFPYDSQAPIPQRVWQTWKVGADDKNFPSSFRTYQKTWSGSYSPDYQYSLISDDSIIPFLENLYAPVPIVIQAFKLMPGNILKADFLRYLLLFARGGIYSDMDTMLLKPIDSWPSQNKSWLNNIIDLNKPIPYKNSKPSLLSSDEISHQPGLVIGIEADPDRDDWSEWYARRIQFCQWTIQAKPGHPILRELILNITATTLASVQNPGVPVSEMIDPRFEEDYNVNYRHKRRHDETYKHSELKNNKNVDGSDIMNWTGPGIFSDIIFEYMNNVLRYNSDILLINPNLNKNDEEGSESATTPAKDVDNDTLSKSTRKFYKKISESLQSSNSMPWEFFSFLKEPVIVDDVMVLPITSFSPDVGQMGAQSSDDKMAFVKHMFSGSWKEDADKNAGHK
Protein: FAD:protein FMN transferase (EC 2.7.1.180) (Flavin transferase) (P0AB85)
Organism: Escherichia coli (strain K12)
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein such as NqrB and NqrC, two subunits of the NQR complex.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:P41780}.
Interaction partners:
- Ion-translocating oxidoreductase complex subunit D
- Ion-translocating oxidoreductase complex subunit G
- Ion-translocating oxidoreductase complex subunit C
- Ion-translocating oxidoreductase complex subunit E
- Ion-translocating oxidoreductase complex subunit B
- Ion-translocating oxidoreductase complex subunit A
Sequence:
MEISFTRVALLAAALFFVGCDQKPQPAKTHATEVTVLEGKTMGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEQQPVQIPSQEQIDAMKAKTGLQHLTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADAWDTGLMVLGPEKAKEVVRREGLAVYMITKEGDSFKTWMSPQFKSFLVSEKN
Protein: Raf homolog serine/threonine-protein kinase Raf (D-Raf) (dRAF-1) (EC 2.7.11.1) (Protein pole-hole) (P11346)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine/threonine kinase required in the early embryo for the formation of terminal structure. Also required during the proliferation of imaginal cells. May act downstream of Ras85D in the tor signal transduction pathway. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis.
Interaction partners:
- Ras-like protein 1
- Dual specificity mitogen-activated protein kinase kinase dSOR1
- 14-3-3 protein zeta
- Mitogen-activated protein kinase ERK-A
- Connector enhancer of KSR protein CNK
- Ras-related protein Rap1
- Tyrosine-protein kinase Src42A
- AT08303p
- Inosine-5'-monophosphate dehydrogenase
- Tyrosine-protein kinase Src64B
Sequence:
MSSESSTEGDSDLYDPLAEELHNVQLVKHVTRENIDALNAKFANLQEPPAMYLIEYQELTSKLHELEAKEQELMERLNSQDQQEDSSLVERFKEQPHYQNQTQILQQQRQLARVHHGNDLTDSLGSQPGSQCGTLTRQPKILLRAHLPNQQRTSVEVISGVRLCDALMKALKLRQLTPDMCEVSTTHSGRHIIPWHTDIGTLHVEEIFVRLLDKFPIRTHIKHQIIRKTFFSLVFCEGCRRLLFTGFYCSQCNFRFHQRCANRVPMLCQPFPMDSYYQLLLAENPDNGVGFPGRGTAVRFNMSSRSRSRRCSSSGSSSSSKPPSSSSGNHRQGRPPRISQDDRSNSAPNVCINNIRSVTSEVQRSLIMQARPPLPHPCTDHSNSTQASPTSTLKHNRPRARSADESNKNLLLRDAKSSEENWNILAEEILIGPRIGSGSFGTVYRAHWHGPVAVKTLNVKTPSPAQLQAFKNEVAMLKKTRHCNILLFMGCVSKPSLAIVTQWCEGSSLYKHVHVSETKFKLNTLIDIGRQVAQGMDYLHAKNIIHRDLKSNNIFLHEDLSVKIGDFGLATAKTRWSGEKQANQPTGSILWMAPEVIRMQELNPYSFQSDVYAFGIVMYELLAECLPYGHISNKDQILFMVGRGLLRPDMSQVRSDAPQALKRLAEDCIKYTPKDRPLFRPLLNMLENMLRTLPKIHRSASEPNLTQSQLQNDEFLYLPSPKTPVNFNNFQFFGSAGNI
Protein: Uncharacterized protein (Q9VLB4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform B
- Cytochrome c oxidase subunit 7C, mitochondrial
- Accessory gland protein Acp36DE
- Fe2OG dioxygenase domain-containing protein
- LD38634p
- Serpin 28F
- Putative ferric-chelate reductase 1 homolog
- Acyl-CoA binding protein 3, isoform A
- FI02892p
- Accessory gland-specific peptide 26Aa
Sequence:
MAIEPISAVPSLLSDYLRTPSCPPNLQWDPTVKICLPNLDYNQYVPKGLLNNPSLPGSPWNSPVATPGRKPGGSSGGGTKETLERKPVQRPVAKPSVSSGGGSGGSTEEKPGGSAGGGSGGSPKDKPVESSGASPGEKPAGSPESKPEGSSGGAAEVGAAGEKPVDIPQQKPEDSSGGGSGGSPQNKPVESSKGNPEVKPAGIPENKPVESSKGNPEVKPAGIPESKPGGSSVGAAAESADKKPIESPDKKPIESPDKKPIEIPKGKPGGDSDGSTGRPEEKPIVSPGEKPTGSSGGNAKGNVGEKPAGSAGGTTNTNINTIKIQHKR
Protein: Kinesin light chain 2 (KLC 2) (O88448)
Organism: Mus musculus (Mouse)
Function: Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9H0B6}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H0B6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H0B6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H0B6}.
Interaction partners:
- Kinesin-1 heavy chain
- Kinesin heavy chain isoform 5A
- Kinesin heavy chain isoform 5C
- Calsyntenin-1
- C-Jun-amino-terminal kinase-interacting protein 3
- Kinesin light chain 1
- Kinesin light chain 3
- Kinesin light chain 4
- Huntingtin-associated protein 1
- Glycogen synthase kinase-3 beta
Sequence:
MATMVLPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLASHEAGEAEPGSQERCLLLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEMLPQEEKGDVPKDSLDDLFPNEDEQSPAPSPGGGDVAAQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGENKPIWMHAEEREESKDKRRDRRPMEYGSWYKACKVDSPTVNTTLRTLGALYRPEGKLEAAHTLEDCASRSRKQGLDPASQTKVVELLKDGSGRGHRRGSRDVAGPQSESDLEESGPAAEWSGDGSGSLRRSGSFGKLRDALRRSSEMLVRKLQGGGPQEPNSRMKRASSLNFLNKSVEEPVQPGGRVFLTAAL
Protein: At1g30260/F12P21_9 (Galactosyltransferase family protein) (Q9C754)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At3g14395
- LOB domain-containing protein 3
- NAC domain-containing protein 101
- Expansin-A15
Sequence:
MATSRLARFITEVAPPQFVTVMRRRTAKVLDTIKEEEREVGTDSIFPSSFNSKKISSPFTSPYSSSVSSASASASCTSGLNKFPVTENRGSFPVFKN
Protein: PML nuclear body scaffold (F1M589)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Retinoic acid receptor, alpha
- Small ubiquitin-related modifier 1
- SUMO-conjugating enzyme UBC9
- Runt-related transcription factor 1
- Transcription factor PU.1
- Death domain-associated protein 6
- Cellular tumor antigen p53
- E3 ubiquitin-protein ligase RNF4
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MPPPEEPSEDHEHSQSPAEQAIKEEFQFLRCPGCQTQAKCPKLLPCLHTLCSGCLEAPGLQCPICQAPGSANANAEALDNVFFESLQRRLAVFRQIVDAQAACTRCKELADFWCFECEQLMCGKCFDAHQWYLKHEARPLAELRDNSVREFLDSTRKSNIFCSNTNHRTPAQTNIYCRGCAKPLCCECALLDRNHSHLQCEIGKEIQQLHEELGTMTQALEEQGRTFDSAHAQMHSAIGQLDDARSDTEKQIRARVRQVIEHVQAQERELLEAVNVRYQRDYQEIAGQLGHLEAVLQRIRTGGALVKRMKLYASEQEVLDMHGFLRKALCRLRQEEPQNHKVQLRTSGFEEFKLCLQDLVSFITQRTDVAVAGRASPEAASTHPEAASAQPEAASTHPEAASAQPEAASAHPESASTPGNSTDLEQPKEVQRAQAQAMELSKTQPVAMVKSVPGAHPVPVYAFSMQGPTYREEASQTVSPMKRKCCHIDCCRKIIKMESTDENEDRLSTSSPEQPRPSTSKAISPPHPDGTSSTESTIPEKETPLPNNNHVASDAGETEERIVVISSSEDSDAENLPSHELDDSSSESSSIQLEGPNSLKALDESLAEPHLEDRTLVFFDLKIDNETQKISQLAAVNRESKFRVLIQPEAFSVYSKAVSLESGLQHFLSFLNSMHRPLLACPRLWGPGLPIFFQALNDINKLWEFQDAISGFLAVLPLIQERIPSASSFKLRNLAKTYLARNMSERSALAAVLAMRDLCCLLEVSPGLQLAQHIYSFSSLQCFASLQPLIQAQVLPQPEARLLALHNVSFLELLTAYRSNRQEGLKKYVHYLSLQTTPSSASTQIAQFLQALSAYMDGQLEGHIPAGAEGTALSLSGRAENKGCLA
Protein: Coiled-coil domain-containing protein 3 (Fat/vessel-derived secretory protein) (Favine) (Q9BQI4)
Organism: Homo sapiens (Human)
Function: Negatively regulates TNF-alpha-induced pro-inflammatory response in endothelial cells (ECs) via inhibition of TNF-alpha-induced NF-kappaB activation in ECs. Positively regulates lipid accumulation in adipose cells (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9D6Y1}.
Interaction partners:
Sequence:
MLRQLLLAALCLAGPPAPARACQLPSEWRPLSEGCRAELAETIVYARVLALHPEAPGLYNHLPWQYHAGQGGLFYSAEVEMLCDQAWGSMLEVPAGSRLNLTGLGYFSCHSHTVVQDYSYFFFLRMDENYNLLPHGVNFQDAIFPDTQENRRMFSSLFQFSNCSQGQQLATFSSDWEIQEDSRLMCSSVQKALFEEEDHVKKLQQKVATLEKRNRQLRERVKKVKRSLRQARKKGRHLELANQKLSEKLAAGALPHINARGPVRPPYLRG
Protein: Fatty acid binding protein, isoform C (Q8INK3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein ultraspiracle
- Ecdysone-induced protein 75B, isoform B
Sequence:
MSFVGKKYKLDKSENFDEYMKELGVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGDKPTTIVREFTDNELITLIPHLTPSQHGSLRLRVPCQPVPPTSVDDGARSGGCGQRPGGP
Protein: Uncharacterized protein C1604.03c (O94369)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MGAILSTPKTPIEVRRKRIVPLFRANHTRFRPVDEKNRINAVPLLLLGCLYGKYKDDDFVDFFDKAIPLLVPQTHKGLDTYEIDVSTYKTHIGHPKFIEPFVLFYGDRLVHDARYNLHELVWQTLSRNPEYIKGLCYDSCTPLANLAVGLSLNIQEVLIDCFATAACFTTEDTSINPIPTLPSVFCTIVDDEGISLKELLYIIEESLLKNAIPDPFSVSTYTLKSAFEHLVKKDFLKYYTAYLASSAVDYIDAYFTESFGSFFISRLASQFLVSFQTLPSFFSFPLVTDNWQHLAALPFNSTYETFRAFDHPSTNGPAIGPLYNAAPAPR
Protein: Hydrazine dehydrogenase (HDH) (EC 1.7.2.8) (Octaheme c-type cytochrome kustc0694) (Q1PW30)
Organism: Kuenenia stuttgartiensis
Function: Catalyzes the four-electron oxidation of hydrazine to N2. The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane. Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans. Cannot oxidize hydroxylamine to NO.
Subcellular location: Anammoxosome {ECO:0000269|PubMed:25962914}.
Interaction partners:
Sequence:
MRKFLKVTLASALIGCGVIGTVSSLMVKEAKAVEIITHWVPHEVYGMPGEPDNSGKVFFSGLKAKYMGYPKDAQRSPYPGKYSKFWKTLPAYRYYIPDYMYNRDEVRPSNPIKGTFKLEQCVACHSVMTPGIVRDYNKSAHSKAEPAPTGCDTCHGNNHQKLTMPSSKACGTAECHETQYNEQGQGGIGSHASCSSFAQVECAWSIERPPGDTAGCTFCHTSPEERCSTCHQRHQFDPAVARRSEQCKTCHWGKDHRDWEAYDIGLHGTVYQVNKWDTEQFDFSKKLSDADYVGPTCQYCHMRGGHHNVQRASIVYTSMGMSMADRGAPLWKEKRDRWVSICDDCHSPRFARENLQAMDESVKDASLKYRETFKVAEDLLIDGVLDPMPKDLCPDWSGQHIWSLKIGAYHDGEAYGGTTGESGEFRMSNCTDVERLCFESVGYFQTYIYKGMAHGSWNDATYSDGSFGMDRWLVNVKQNASRARRLAALEKKVGISWQPEQFWKTGEWLDQLTGPYIVKNHPGKTIFDLCPDPGWLDTHHAPAEEVEYIERKLKELGITAGSHSAHHHESGHDPAARSMKEH
Protein: Protein scabrous (P21520)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in regulation of neurogenesis. May encode a lateral inhibitor of R8 differentiation. In conjunction with Gp150, promotes Notch activation in response to Delta by regulating acquisition of insensitivity to Delta in a subset of cells.
Subcellular location: Late endosome {ECO:0000269|PubMed:12756167, ECO:0000269|PubMed:2175046}. Note=Colocalizes in late endosomes with Gp150.
Interaction partners:
- Neurogenic locus Notch protein
Sequence:
MRDWQTFPDLQKKKVSRDHLNCPATMAGSNVLWPILLAVVLLQISVAFVSGAASGGVVLSDVNNMLRDAKVVTSEKPVVHSKQETEAPESSVELLRFVDDDEDSEDISSIERQDGRTMESKKMADQVRLLTKQLNALMLRRREDYEMLEHNLRKSLRLTTNANSVDADMRSELNQLREELAALRSSQSGNKERLTVEWLQQTISEIRKQLVDLQRTASNVAQDVQQRSSTFEDLATIRSDYQQLKLDLAAQRERQQQTEVYVQELREEMLQQEQDFQHALVKLQQRTRKDGSSASVEEESGSQEANQEQTGLETTADHKRRHCRFQSEQIHQLQLAQRNLRRQVNGLRFHHIDERVRSIEVEQHRIANANFNLSSQIASLDKLHTSMLELLEDVEGLQTKMDKSIPELRHEISKLEFANAQITSEQSLIREEGTNAARSLQAMAVSVSVLQEEREGMRKLSANVDQLRTNVDRLQSLVNDEMKNKLTHLNKPHKRPHHQNVQAQMPQDDSPIDSVLAETLVSELENVETQYEAIINKLPHDCSEVHTQTDGLHLIAPAGQRHPLMTHCTADGWTTVQRRFDGSADFNRSWADYAQGFGAPGGEFWIGNEQLHHLTLDNCSRLQVQMQDIYDNVWVAEYKRFYISSRADGYRLHIAEYSGNASDALNYQQGMQFSAIDDDRDISQTHCAANYEGGWWFSHCQHANLNGRYNLGLTWFDAARNEWIAVKSSRMLVKRLPAVECQANASASGAFVSVSGSAADAAPSSGATTTTTTATAAPATVTTPKTNNSVVQFVAAGQA
Protein: Regulator of G-protein signaling 20 (RGS20) (Regulator of G-protein signaling Z1) (Q9QZB1)
Organism: Mus musculus (Mouse)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins.
Subcellular location: Membrane; Lipid-anchor. Nucleus. Cytoplasm. Note=Shuttles between the cytoplasm/cell membrane and the nucleus Anchored to the membrane through palmitoylation. {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MRTANGGPRARASPSASPADPGLPEGSERTEMRMRQMCGGSETQGPAPSQQGGRGSNACCFCWCCCCTCSCLTVRNQEDQRPQRASHEIRTDIPACEESPTPTLEEVCAWAQSFDNLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKREANKSTIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVDPSQHIFDDAQLQIYTLMHRDSYPRFMNSTVYKDLLTSLAEKTVEA
Protein: Rap guanine nucleotide exchange factor (GEF) 1 (Q3UHC1)
Organism: Mus musculus (Mouse)
Interaction partners:
- Crk-like protein
- Adapter molecule crk
- E3 ubiquitin-protein ligase CBL
- Breast cancer anti-estrogen resistance protein 1
- Growth factor receptor-bound protein 2
- Ras-related protein Rap-1A
- Fibroblast growth factor receptor substrate 2
- GTPase HRas
- Rho-related GTP-binding protein RhoQ
- GTPase KRas
Sequence:
MSSGLGLRRSPEMSGKIEKADSQRSHLSSFTMKLMDKFHSPKIKRTPSKKGKPAEVSKIPEKPVSKEARDRFLPEGYPIPLDLEQQAVEFMSTSAVASRSQRQKNLCWLEEKEKEVVSALRYFKTIVDKMAIDKKVLEMLPGSASKVLEAILPLVQTDPRIQHSSALSSCYSRVYQSLANLIRWSDQVMLEGVNSEDKEMVTTVKGVIKAVLDGVKELVRLTIEKQGRPSPTSPVKPSSPASKPDGQPELPLTDREMEILNKTTSVSPSAELLPDSTSEEVAPPKPPLPGIRVVDNSPPALPPKKRQSAPSPTRVAVVAPMSRATSGSSLPVGINRQDFDVECYTQRRLSGGSRSCGGESPRLSPCSSTGKLSRSDEQLSSLDRDSGQCSRNTSCETLDHYDPDYEFLQQDLSNADQIPPQAACNLSPLPESLGESGPPFLGHPFQLPLGSCLQQEGQQTDTPPALPEKKRRSAVSQTTDSSGCRVSYERHPSQYDNISEGDLQNPVPVQPVPYPPFAAVLPFQQGASSASAEFVGDFSVPELAGDTEKPPPLPEKKNKHMLAYMQLLEDYSEPQPSMFYQTPQSEHIYQQKNKMLMEVYGFSESFCGSDSTQELAPPPALPPKQRQLQASYAASSFSVSYCVQQTKVAFTPEDGSAAQGLSVSVSNSFLNRHGSLPVPSYKSVFRSYSQDFMPHHQASVQPFLPPTSSSSPHFPPVHTSQSSDLAVPTVSSPPPSTVDGPLSSSQDSSFHGNPVRLPSETSFTDSEPPSGKDGHPRDPSVSSASGKDSRENGERSPKSLDGLESAQSEEEVDELSLIDHNEIMARLTLKQEGDDGPDVRGGSGDILLVHATETDRKDLVLYCEAFLTTYRTFISPEELIKKLQYRYEKFSPFADTFKKRVSKNTFFVLVRVVDELCLVELTEEILKLLMELVFRLVCSGELSLARVLRKNILDKVDQKKLLRCAHSDQPLAARGVAARPGTLHDFHSHEIAEQLTLLDAELFYKIEIPEVLLWAKEQNEEKSPNLTQFTEHFNNMSYWVRSIIMLQEKAQDRERLLLKFIKIMKHLRKLNNFNSYLAILSALDSAPIRRLEWQRQTSEGLAEYCTLIDSSSSFRAYRAALSEVEPPCIPYLGLILQDLTFVHLGNPDYIDGKVNFSKRWQQFNILDSMRCFQQAHYEIRRNDDIINFFNDFSDHLAEEALWELSLKIKPRNITRRKTDREEKT
Protein: INSM transcriptional repressor 1 (A0A8I6GJX9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRGFLVKRSKKSTPVSYRVRGGEDCDRALLLSPGCGGARAEPPVPSPGPLPPPPPPALAERAHAALAAALACAPGPPPPPPGPRAAHFGNPEAAHPAPLYSPTRPVSREHEKHKYFERSFNLGSPVSAESFPTPAALLAGGGGGANGAGGGGGGTCGGDALLFAPAELKMGTAFSAGAEAARGPGPGPPLSPAAALRPPGKRPAAPAAVAAEPPAKAAKAPSAKKPKAIRKLHFEDEVTTSPVLGLKIKEGPVEAPRGRAGGATRPLGEFICQLCKEEYADPFALAQHKCSRIVRVEYRCPECAKVFSCPANLASHRRWHKPRPAPAAARAPEPEAATRAEAREAAGGGGSSDRDTPSPGGVSESGSEDGLYECHHCAKKFRRQAYLRKHLLAHHQALQAKGAPPPPPPPPPPPAEDILAFYAGPDEKAPQEASGDGEAVGVLGLSAATECHLCPVCGETFPSKGAQERHLRLLHAAQVFPCKYCPATFYSSPGLTRHINKCHPSENRQVILLQVPVRPAC