wanglab/gogpt-training-data huggingface dataset:
Protein: 7-dehydrocholesterol reductase (7-DHC reductase) (EC 1.3.1.21) (Protein DWARF 5) (Sterol Delta(7)-reductase) (Q9LDU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC). Lesions in the gene coding for the enzyme cause dwarfism.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Delta
- Delta
- Putative Delta
- Sterol 14-demethylase
- Probable 3-beta-hydroxysteroid-Delta
- Methylsterol monooxygenase 2-2
- Ergosterol biosynthetic protein 28
- Methylsterol monooxygenase 2-1
- Methylsterol monooxygenase 1-1
- Cycloartenol-C-24-methyltransferase
Sequence:
MAETVHSPIVTYASMLSLLAFCPPFVILLWYTMVHQDGSVTQTFGFFWENGVQGLINIWPRPTLIAWKIIFCYGAFEAILQLLLPGKRVEGPISPAGNRPVYKANGLAAYFVTLATYLGLWWFGIFNPAIVYDHLGEIFSALIFGSFIFCVLLYIKGHVAPSSSDSGSCGNLIIDFYWGMELYPRIGKSFDIKVFTNCRFGMMSWAVLAVTYCIKQYEINGKVSDSMLVNTILMLVYVTKFFWWEAGYWNTMDIAHDRAGFYICWGCLVWVPSVYTSPGMYLVNHPVELGTQLAIYILVAGILCIYINYDCDRQRQEFRRTNGKCLVWGRAPSKIVASYTTTSGETKTSLLLTSGWWGLARHFHYVPEILSAFFWTVPALFDNFLAYFYVIFLTLLLFDRAKRDDDRCRSKYGKYWKLYCEKVKYRIIPGIY
Protein: GmrSD restriction endonucleases C-terminal domain-containing protein (C8V6E2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MPRLLPVLLAAASLQVARVGATPPGIPSTSVAETQLEALTVKEAGASSDYDRDLFPHWISQGDSCNTRDRVLIRDGTNVETGSGCSITGSWTSPYDGETWTATSDVDIDHVVPLSNAWNSGASEWTTDEREAFANDLSIPQLLAVTDSVNQQKSDSGPEEWLPPLESYHCTYGKMWTNVKYTYGLSVTSAEKSALEDLLAKC
Protein: 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31) (P85971)
Organism: Rattus norvegicus (Rat)
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19343716}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- GDH/6PGL endoplasmic bifunctional protein
- Probable gluconokinase
- N-acetylglucosamine-6-phosphate deacetylase
- Transaldolase
- RNA-binding protein 45
- ribulose-phosphate 3-epimerase
- Ribose-5-phosphate isomerase
- Glucose-6-phosphate isomerase
- Transketolase
Sequence:
MAAPAPGLISVFSSPQELGASLAQLVAQRAASCLEGNRGRFALGLSGGSLVSMLARDLPAATAPAGPASFARWTLGFCDERLVPFDHAESTYGLYRTHLLSKLPIPDSQVLTIDPALPVEDAAEDYARKLRQAFQGDTVPVFDLLILGVGPDGHTCSLFPGHPLLQEREKIVAPIGDSPKPPPQRVTLTLPVLNAAQSVIFVATGEGKAAVLKRILEDQESALPAAMVQPRTGALCWFLDEAAARLLSVPFEKHSTL
Protein: Metal tolerance protein 1 (OsMTP1) (Q688R1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in sequestration of excess zinc in the cytoplasm into vacuoles to maintain zinc homeostasis.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Tonoplast.
Interaction partners:
- Metal tolerance protein 7
- Cadmium/zinc-transporting ATPase HMA2
- Metal tolerance protein 6
Sequence:
MDSHNSAPPQIAEVRMDISSSTSVAAGNKVCRGAACDFSDSSNSSKDARERMASMRKLIIAVILCIIFMAVEVVGGIKANSLAILTDAAHLLSDVAAFAISLFSLWAAGWEATPQQSYGFFRIEILGALVSIQLIWLLAGILVYEAIVRLINESGEVQGSLMFAVSAFGLFVNIIMAVLLGHDHGHGHGHGHGHGHSHDHDHGGSDHDHHHHEDQEHGHVHHHEDGHGNSITVNLHHHPGTGHHHHDAEEPLLKSDAGCDSTQSGAKDAKKARRNINVHSAYLHVLGDSIQSIGVMIGGAIIWYKPEWKIIDLICTLIFSVIVLFTTIKMLRNILEVLMESTPREIDATSLENGLRDMDGVVAVHELHIWAITVGKVLLACHVTITQDADADQMLDKVIGYIKSEYNISHVTIQIERE
Protein: Secretogranin-3 (Secretogranin III) (SgIII) (Q8WXD2)
Organism: Homo sapiens (Human)
Function: Member of the granin protein family that regulates the biogenesis of secretory granules. Acts as a sorting receptor for intragranular proteins including chromogranin A/CHGA (By similarity). May also play a role in angiogenesis. Promotes endothelial proliferation, migration and tube formation through MEK/ERK signaling pathway.
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P47868}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P47868}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:12098761, ECO:0000269|PubMed:25326458}. Note=Associated with the secretory granule membrane through direct binding to cholesterol-enriched lipid rafts. {ECO:0000250|UniProtKB:P47868}.
Interaction partners:
- Chromogranin-A
- Secretogranin-1
- Neuroendocrine protein 7B2
- Secretogranin-2
- Transient receptor potential cation channel subfamily A member 1
- Carboxypeptidase E
- Pro-MCH
- Pro-opiomelanocortin
Sequence:
MGFLGTGTWILVLVLPIQAFPKPGGSQDKSLHNRELSAERPLNEQIAEAEEDKIKKTYPPENKPGQSNYSFVDNLNLLKAITEKEKIEKERQSIRSSPLDNKLNVEDVDSTKNRKLIDDYDSTKSGLDHKFQDDPDGLHQLDGTPLTAEDIVHKIAARIYEENDRAVFDKIVSKLLNLGLITESQAHTLEDEVAEVLQKLISKEANNYEEDPNKPTSWTENQAGKIPEKVTPMAAIQDGLAKGENDETVSNTLTLTNGLERRTKTYSEDNFEELQYFPNFYALLKSIDSEKEAKEKETLITIMKTLIDFVKMMVKYGTISPEEGVSYLENLDEMIALQTKNKLEKNATDNISKLFPAPSEKSHEETDSTKEEAAKMEKEYGSLKDSTKDDNSNPGGKTDEPKGKTEAYLEAIRKNIEWLKKHDKKGNKEDYDLSKMRDFINKQADAYVEKGILDKEEAEAIKRIYSSL
Protein: Transmembrane channel-like protein (A4FU59)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}.
Interaction partners:
Sequence:
VEWSGECLRSCRREVQIKVEEKEDETEESSSEEEEEVEDKLPRRESLRPKRKRTRDVINEDDPEPEPEDEETRKAREKERRRRLKRGAEAKKFVSENEGALGKGKGKRWFAFKMMMAKKWAKFLRDFENFKAACVPWENKIKAIESQFGSSVASYFLFLRWMYGVNMVLFILTFSLIMLPEYLWGLPYGSLPRKTVPRAEEASAANFGVLYDFNGLAQYSVLFYGYYDNKRTIGWMNFRLPLSYFLVGIMCIGYSFLVVLKAMTKNIGDDGGGDDNTFNFSWKVFTSWDYLIGNPETADNKFNSITMNFKEAITEEKAAQVEENVHLIRFLRFLANFFVFLTLGGSGYLIFWAVKRSQEFAQQDPDTLGWWEKNEMNMVMSLLGMFCPTLFDLFAELEDYHPLIALKWLLGRIFALLLGNLYVFILALMDEINNKIEEEKLVKANITLWEANMIKAYNASFSENSTGPPFFVHPADVPRGPCWETMVGQEFVRLTVSDVLTTYVTILIGDFLRACFVRFCNYCWCWDLEYGYPSYTEFDISGNVLALIFNQGMI
Protein: Pre-mRNA-splicing factor 38 (Q9VYE9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367025}.
Interaction partners:
- Pre-mRNA-splicing factor 38
- Ubiquitin carboxyl-terminal hydrolase
- Pinin, isoform B
- BcDNA.LD23634
- LD29830p
- RH42690p
Sequence:
MDEDYSASSSAGGGKKAGKQHNTLPFWGNESSMNLNALILANIQSSSYFKVHLFKLKTYHEVVDEIYYQVKHMEPWERGSRKTSGQTGMCGGVRGVGAGGIVSTAYCLLYKLYTLRLTRKQINGLLNHTDSAYIRALGFMYLRYTQPPGDLYDWYEDYLQDEEEIDVKAGGGQVLTIGQMVYQFMTKLDWFSTLFPRIPVPIQKQIEKRIEQYCREQGVTVHQLSTGRSTAGTGGGPGAAGQDADYQDYPEGGVERGSGGRGGGQAGSRSNAYPQPNNYRNDYDERDYYAAASGSSYGRGRGGYEDYPPAPLPPQMPYGERERERDRDRDKNKDYDRHRSKHKKKHNHRQSSRSRSRSRSRSRHRSERHERKRDGGGYERSSKSRHNEHYEERERRHR
Protein: Ornithine carbamoyltransferase (EC 2.1.3.3) (Ornithine transcarbamylase) (OTCase) (P05150)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Argininosuccinate synthase
- Protein ARG5,6
- Arginine biosynthesis bifunctional protein ArgJ, mitochondrial
- Arginase
- Acetylornithine aminotransferase, mitochondrial
- Carbamoyl phosphate synthase arginine-specific large chain
- Carbamoyl phosphate synthase arginine-specific small chain
- Argininosuccinate lyase
- Ornithine aminotransferase
- 1,4-alpha-glucan-branching enzyme
Sequence:
MSTTASTPSSLRHLISIKDLSDEEFRILVQRAQHFKNVFKANKTNDFQSNHLKLLGRTIALIFTKRSTRTRISTEGAATFFGAQPMFLGKEDIQLGVNESFYDTTKVVSSMVSCIFARVNKHEDILAFCKDSSVPIINSLCDKFHPLQAICDLLTIIENFNISLDEVNKGINSKLKMAWIGDANNVINDMCIACLKFGISVSISTPPGIEMDSDIVDEAKKVAERNGATFELTHDSLKASTNANILVTDTFVSMGEEFAKQAKLKQFKGFQINQELVSVADPNYKFMHCLPRHQEEVSDDVFYGEHSIVFEEAENRLYAAMSAIDIFVNNKGNFKDLK
Protein: Fibronectin type 3 and ankyrin repeat domains protein 1 (Q8TC84)
Organism: Homo sapiens (Human)
Function: Through the activation of JUN and AP-1-mediated transcription, may regulate apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:27060496}. Cytoplasm, cytosol {ECO:0000269|PubMed:20978819}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9DAM9}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9DAM9}.
Interaction partners:
- Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32
Sequence:
MEPQKIMPPSKPHPPVVGKVTHHSIELYWDLEKKAKRQGPQEQWFRFSIEEEDPKMHTYGIIYTGYATKHVVEGLEPRTLYRFRLKVTSPSGECEYSPLVSVSTTREPISSEHLHRAVSVNDEDLLVRILQGGRVKVDVPNKFGFTALMVAAQKGYTRLVKILVSNGTDVNLKNGSGKDSLMLACYAGHLDVVKYLRRHGASWQARDLGGCTALHWAADGGHCSVIEWMIKDGCEVDVVDTGSGWTPLMRVSAVSGNQRVASLLIDAGANVNVKDRNGKTPLMVAVLNNHEELVQLLLDKGADASVKNEFGKGVLEMARVFDRQSVVSLLEERKKKQRPKKSCVC
Protein: Deacetylase sirtuin-type domain-containing protein (Q2U2P7)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Glutamine-dependent NAD
- Nicotinamide-nucleotide adenylyltransferase
- Sugar kinase
- Sugar kinase
- Inosine/uridine-preferring nucleoside hydrolase domain-containing protein
- NAD
- Uncharacterized protein
- COMPASS component cclA
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
Sequence:
MDDGFSDVSELSSPPASPTPPPGFYPSPPPSQEADESSGTRSQDRDDLPPAKKRRRVAAPKERRTQRLDLSSSAGLSYTEQQAQIDLLTKTIRRHRKIVVIAGAGISTSAGIPDFRSTDGLFKSLQKKHNLKASGKLLFDAAVYQDETLTASFQDMVRSLSEEAAKTSPTAFHHMLARISQENRLTRLYTQNIDGIETSMPPLATQIPLNVKAPWPRTIQLHGSLEKMVCQKCRHLGDFDGDMFDRPDAPECPECARNNQFRIETGQRSHGIGKMRPRIVLYNEHNPDEEAITSVMNADVRSRPDALIVVGTSLKIPGVRRLVKSLCSVIRSRRNGVTMWINNEPPAGKEFEDCWDLMVKGDCEEVARLAALKRWDDHSENVFDECNASEVERVKNEHGVSIVIETPKKRQKTQTGFLTPSSSHDEEASKVPKKGGSRSNPASRGRSLQEVLKASKTAESKKPAAKKSAPRRKIKKDEPAKNTRITTFSKVTKAQKVATDTEKAVKLEKEENKPMHPLPPGAARNNGPMIPQLAQKGEETPQRSSRWRQPDTISPKSVPKGMSQLLNQPAA
Protein: Leucine-rich repeat receptor protein kinase HPCA1 (EC 2.7.11.1) (Protein HYDROGEN-PEROXIDE-INDUCED CALCIUM INCREASES 1) (Q8GZ99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Leucine-rich repeat receptor protein kinase that acts as sensor of extracellular hydrogen peroxide. Required for intracellular calcium influx in response to extracellular hydrogen peroxide. Mediates hydrogen peroxide-induced activation of calcium channels in guard cells and is required for stomatal closure.
Subcellular location: Cell membrane {ECO:0000269|PubMed:32076270}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Serine/threonine-protein phosphatase BSL1
- Aminopeptidase P2
Sequence:
MSSRTGASLLLILFFFQICSVSALTNGLDASALNALKSEWTTPPDGWEGSDPCGTNWVGITCQNDRVVSISLGNLDLEGKLPADISFLSELRILDLSYNPKLSGPLPPNIGNLGKLRNLILVGCSFSGQIPESIGTLKELIYLSLNLNKFSGTIPPSIGLLSKLYWFDIADNQIEGELPVSNGTSAPGLDMLLQTKHFHFGKNKLSGNIPKELFSSNMSLIHVLFDGNQFTGEIPETLSLVKTLTVLRLDRNKLIGDIPSYLNNLTNLNELYLANNRFTGTLPNLTSLTSLYTLDVSNNTLDFSPIPSWISSLPSLSTLRMEGIQLNGPIPISFFSPPQLQTVILKRNSIVESLDFGTDVSSQLEFVDLQYNEITDYKPSANKVLQVILANNPVCLEAGNGPSYCSAIQHNTSFSTLPTNCSPCEPGMEASPTCRCAYPFMGTLYFRSPSFSGLFNSTNFSILQKAIADFFKKFNYPVDSVGVRNIRENPTDHQLLIDLLVFPLGRESFNQTGMSLVGFAFSNQTYKPPPIFGPYIFKADLYKQFSDVEVSSKSSNKSILIGAVVGVVVLLLLLTIAGIYALRQKKRAERATGQNNPFAKWDTSKSSIDAPQLMGAKAFTFEELKKCTDNFSEANDVGGGGYGKVYRGILPNGQLIAIKRAQQGSLQGGLEFKTEIELLSRVHHKNVVRLLGFCFDRNEQMLVYEYISNGSLKDSLSGKSGIRLDWTRRLKIALGSGKGLAYLHELADPPIIHRDIKSNNILLDENLTAKVADFGLSKLVGDPEKTHVTTQVKGTMGYLDPEYYMTNQLTEKSDVYGFGVVLLELLTGRSPIERGKYVVREVKTKMNKSRSLYDLQELLDTTIIASSGNLKGFEKYVDLALRCVEEEGVNRPSMGEVVKEIENIMQLAGLNPNSDSATSSRTYEDAIKGSGDPYGSESFQYSGNFPASKLEPQ
Protein: PtdIns3K complex I subunit atg38 (Meiotically up-regulated gene 167 protein) (O94427)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:31941401}. Cytoplasm, cytosol {ECO:0000269|PubMed:31941401}.
Interaction partners:
- Phosphatidylinositol 3-kinase pik3
- Serine/threonine-protein kinase vps15
- Vacuolar protein sorting-associated protein 38
- Vacuolar protein sorting-associated protein atg6
- Autophagy-related protein 14
- Autophagy protein 16
- Autophagy-related protein 18
- Probable cysteine protease atg4
- Serine/threonine-protein kinase atg1
- Autophagy-related protein 9
Sequence:
MVRYSLRKAHEYARDGENQEVLGEISQAIMYYGLAKSQFEKICQNTAQPLIKRCANNQIEELMVRIRELRESLPNKQTPISMSMSTRLSPMYTSSLTPRFTSNSMVLPGDHNTTVRLKPSFREALMEDSEDDLYQMYSKFEMQVKKLSTNYGLAVAFSIVPMDDDQPSPSIFSSDESFLIVEGDDFSLGNSVEEDANATSKEDPAYQNTNEQIQPLSNFDISQQEYLNNTRIPYENEDLHLQHITQGTTDDNNVSKFLIPSYNDAKELSEEEMGRSHKREESFKRAFGHASSSESSIGEITDSREDIQSNRLVNGSWENNDFTKEINNNFPDRSETPTLQTIEAPTKLMKYTRRKSLFRFPFFRSISGKKKEEPMESGTDSLESSTAQITVDSQLKIKQLETQIATLQKQLEQFQTSTLDQDLH
Protein: 4-coumarate--CoA ligase 5 (4CL 5) (Os4CL5) (EC 6.2.1.12) ((E)-ferulate--CoA ligase) (EC 6.2.1.34) (4-coumaroyl-CoA synthase 5) (Q6ZAC1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the phenylpropanoid metabolism by mediating the activation of a number of hydroxycinnamates for the biosynthesis of monolignols and other phenolic secondary metabolites. Catalyzes the formation of CoA esters of cinnamate, 4-coumarate, caffeate and ferulate. Is also able to convert sinapate to its corresponding CoA ester, a reaction that is rarely observed in 4CL catalysis. Is more efficient with substrates in the following order: ferulate > 4-coumarate > sinapate > caffeate > cinnamate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioesters (By similarity).
Interaction partners:
- Phenylalanine ammonia-lyase
- tricin synthase
- Phenylalanine ammonia-lyase
- Os06g0592400 protein
- Aldehyde dehydrogenase 1
- Hydroxycinnamoyltransferase 1
- Aldehyde dehydrogenase 1
- Phenylalanine ammonia-lyase
- Os08g0205000 protein
- Os02g0180700 protein
Sequence:
MGSLPEQFVFRSRLPDIAIPDHLPLHDYVFERLADRRDRACLIDGATGETLSFGDVDALSRRVAAGLSSIGVCHGSTVMLLLPNSVEFAVAFLASSRLGAVTTTANPLHTPPEIAKQVAASGATVVVTEPAFVAKVSGLAGVTVVATGGGAERCASFAGLAAADGSALPEVAIDVANDAVALPYSSGTTGLPKGVMLSHRGLVTSVAQLVDGENPNLHLREDDVVLCVLPMFHVYSLHSILLCGMRAGAAIVVMKRFDTVKMLQLVERHGVTIAPLVPPIVVEMAKSDALDRHDLSSIRMVISGAAPMGKELQDIVHAKLPNAVLGQGYGMTEAGPVLSMCMAFAKEPTPVKSGACGTVVRNAELKIVDPDTGLSLPRNQPGEICIRGKQIMKGYLNNPEATEKTIDKDGWLHTGDIGFVDDDDEIFIVDRLKELIKYKGFQVAPAELEAMLIAHAAVADAAVVPMKDDSCGEIPVAFVVARDGSGITDDEIKQYVAKQVVFYKRLHKIFFVDAIPKAPSGKILRKDLRAKLAAGIPAC
Protein: Phytoene synthase 2, chloroplastic (OsPSY2) (EC 2.5.1.32) (Q2QLV9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the conversion of geranylgeranyl diphosphate to phytoene. Mediates the first committed step in carotenoid biosynthesis.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:18326788}; Peripheral membrane protein {ECO:0000305}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:23023170, ECO:0000269|PubMed:28025520}.
Interaction partners:
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- aldehyde oxygenase
- Probable solanesyl-diphosphate synthase 3, chloroplastic
- Solanesyl-diphosphate synthase 2, chloroplastic
- Os07g0580900 protein
- prolycopene isomerase
- Os02g0668100 protein
- Geranylgeranyl diphosphate reductase, chloroplastic
- Phytoene synthase 1, chloroplastic
- Phytoene synthase 3, chloroplastic
Sequence:
MASSSSAAALWTAAPHPHGSCIRIHAIFHQRHQRRGRRPVVVASSVRPLQAASLAVATAPVAVASRRTAAEEAVYEVVLRQAALVEEATHRRGAGAPRWAEEDAVDWGLLLGDAYHRCGEVCAEYAKTFYLGTQLMTPERRKAVWAIYVWCRRTDELVDGPNSSYITPKALDRWEKRLEDLFEGRPYDMYDAALSDTVSKFPVDIQPFKDMIEGMRLDLWKSRYRSFDELYLYCYYVAGTVGLMTVPVMGIAPDSKASTESVYNAALALGIANQLTNILRDVGEDSRRGRIYLPLDELAEAGLTEEDIFRGKVTDKWRKFMKGQILRARLFFDEAEKGVAHLDSASRWPVLASLWLYRQILDAIEANDYNNFTKRAYVNKAKKLLSLPVAYARAAVAS
Protein: Scaffold attachment factor B2 (K7ERX3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEEEGTEDNGLEDDSRDGQEDMEASLENLQNMGMMDMSVLDETEVANSSAPDFGEDGTDGLLDSFCDSKEYVAAQLRQLPAQPPEHAVDGEGFKNTLETSSLNFKVTPDIEESLLEPGTDKRNT
Protein: C3/C5 convertase (F1R886)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Complement component c3a, duplicate 2.
- Peptidase S1 domain-containing protein
- C3/C5 convertase
- Complement 4B
- Complement C5
- Complement component c3a, duplicate 1.
- Complement component c3a, duplicate 4.
Sequence:
MTSMECGLRLKWLILALICPLIAGAPSREGSCPEENLDIAGGSFTLSNGYSDGSYLQYICPDNHYPSISSRRCQFGVWTPKASSRKKAECKKITCPNPRVLENGEVAPYQERYYINDVTTYSCSSDYKFRGSKVRVCQPNGKWNGSTPICGRDSDHCPDPGVPPGSSRTGSIFNIDDEVTYHCDSPLTLIGSKVRKCLDDGQWSGTEPQCYADFTYDTAMEAAEAFGNSLTTTLTVQQGFEDDQHGKKISLDRGGKLDIYIAVDASDSIDPKDFGKAKKIIKTLIEKISYYEVSPNYEILMFATDVDQIVKMRDFKTNEKARNISKIFEDLDNFNYDKKGDRTGTNIAKLYLKILDSMSLEQVQNKEDFLQTQHVIIVFTDGQANMGGNPKPKVDLIKNLVIKNNASRENKLDLYVFGVGKDVKKEDMNGLVSEKKDERHFFKLPDLDEVQNTFDLMLDDSTVVGLCGMQQNYDGSNKRSAYPWLAQLSIAQSQISDCMGSLVTSRYILTAAHCFKEGDTPDKITVYLEKNTDVKVEKVFIHPNYSLTAKQSIGIKEFYDFDVALLQLKTPVKMSVNLRPICLPCTKETNRALKLSDSQGTCEKHEQILLSNELVDAAFTSKMDMEKRSPRKIRRITVKLGKYLDACVEDAKKAKGIEVADATEAVTKNFLCSGGNQPQRDDVSCKGESGGATHVDKYGRLIQIGVVSWGVKNLCSKAKLDAVSVSDSRDYHINLLRPDIQSFLKKHLENDKLGHTLTFLP
Protein: DASH complex subunit HSK3 (Helper of ASK1 protein 3) (Outer kinetochore protein HSK3) (P69852)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.
Subcellular location: Nucleus {ECO:0000305|PubMed:25236177}. Cytoplasm, cytoskeleton, spindle {ECO:0000305|PubMed:25236177}. Chromosome, centromere, kinetochore {ECO:0000305|PubMed:25236177}. Note=Associates with the mitotic spindle and the kinetochore.
Interaction partners:
- DASH complex subunit SPC34
- DASH complex subunit DAD2
- DASH complex subunit ASK1
- DASH complex subunit DAD4
- DASH complex subunit SPC19
- DASH complex subunit DUO1
- DASH complex subunit DAD3
- DASH complex subunit DAM1
- DASH complex subunit DAD1
- Inner kinetochore subunit IML3
Sequence:
MNANKQRQYNQLAHELRELQTNLQETTKQLDIMSKQCNENLVGQLGKVHGSWLIGSYIYYMEQMLGKTQ
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (F4IBX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLMTLAATTSVSFNSKLLLFRIRCSDSNPKRGFGSKKEEKDPALQQRKSSSKQSVSVPRKAPGLNTQFEGKSGRSFDIDFDERLENIRRSALEQKKTEVVKEFGPIDYDAPVKSDQKTIGLGTKVGVGIAVVVFGLVFALGDFLPTGRCVKISWVGFRNFTFLSYQVIDSPTKNTTVVKNQISEEEKATLQQRLKEFETTLNGTPQDQAALEGAAVTLTELGDYSRAAAFLEKLAKERPTDPDVFRLLGEVNYELNNYEGSIAAYKISEKVSKGIDLEVTRGLMNAYLAAKKPDEAVKFLLDTRERLNTKKTSTTDSVTDETNLDPIQVELLLGKAYSDWGHISDAIAVYDQLISAHPEDFRGYLAKGIILRENGSRGDAERMFIQARFFAPNKAKALVDRYSKL
Protein: Exocyst complex component 3-like protein (Q8BI71)
Organism: Mus musculus (Mouse)
Function: As part of the exocyst, may play a role in regulated exocytosis of insulin granules.
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:18480549}. Note=Colocalizes with insulin granules.
Interaction partners:
- Exocyst complex component 2
- Exocyst complex component 4
- Exocyst complex component 5
- Exocyst complex component 1
- Exocyst complex component 8
- Rab effector MyRIP
- Exocyst complex component 6
- Exocyst complex component 7
- Exocyst complex component 6B
- Exocyst complex component 1-like
Sequence:
MDSKIQPTLRPGSSCPRPEWPEQERAEQLARGAALKWASGIFYRPEQLTRLGQYRSREIQRNYSLEARIKSVVQSYLEGVQTGVWQLTRALEAVQGTREALSQAHHLLKGLSRTSQTLEPLRECVVQHKQLQILTRLLPRLQAVPATVAHTQTLIDSERLLEAYVSLRELEQLKEETLAPLGGLELPIFQGLGLLAEALGQAVEAAAGAAGRLAREDPALLVAAIRVAEVETERTILGQAPRDWRQRCLRALQEGLERVHFASPVLPEPGALAGWLEALQVALPAELATAEALVAPCCPPSYRVVELWAHTLHSGLRRSVQQLLAGPELGAADTFALLHWALHVYTGKEMMGNLELGPEADVSQLEPLLTSENIEQLEAAFVAQVQVSVAQWLKKALDGEVAEWSGEQEPPTDPSGFYHSPMPAIVLQILAENIQVTNLISDSLHRRAHNMAVSELGAFLRSFSDALIRFSRDHLRGDAVAPHYVPYLLSAFNHQSALRSSVSVLLPDGEASGVLAPVEAALDDVQRRICRLVLEVLQVELQPLFSALPSRRWLLSSELLDGVCEQTSHFCQDFWRVRKPGVQLLLAEAERTVVLQYLRALMQGRLVCRGTDERSQAAERLRQDAAQLKELFLGLGLEESAHCAPVLLALRELLNLHDPTLLGLEVAGLRQQFPDVSEDHVSALLDLRGDVSREHRQAALSSLQAGPPPSPSTGRRALFSLVPTPTPSLSSCLPSGPCS
Protein: Paralemmin-2 (Q3UZT2)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
Sequence:
MEMAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTADGGKCTLPRLFSDAFLLVLGVVFIYTDSPGDRCEGTLPKGIPGKGQQPSWQRPKRSHCRLFCLCLLT
Protein: Uncharacterized protein (Q4GYK0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLIGMKYSAPKAIVISLHFPKSRSPYIGTHFHVVCYEGDGPWKHLLQPAECWCSKLLTGKKKCATTARHHGMPRTFEVPMSIMGIHNHKRILNRGIFIFVPNRIYFINNREFLLTRRTCVYFDTTANTFPKKKTYVRW
Protein: SET and MYND domain containing, arthropod-specific, member 9, isoform A (SET and MYND domain containing, arthropod-specific, member 9, isoform B) (Q9W373)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- SET and MYND domain containing, class 4, member 1, isoform B
- Seminal fluid protein 51E
- Seminal fluid protein 36F
Sequence:
MICPKRTSELLDLHLAPFKDKDPAWEIGVSKIAGRGVVATRSLKRGEIIFRDSPLLIGLAAHEEDSLNACSVCLKMLPDTRFMCRQGCGLPVCSLCAKKKQHKSDCDLFKSWGPNEPDVANSVIIRLLCVARAINLSKEQRDLIYCLQANLDNNHRTEVRNAAKCFKNFPTDKKLIEIMNRTVAVLRTNGFDKTTDRTNDNQEFNYRALYPLFGVVNHDCIPNAYYTFEEKTNNMIVRAAVDIPEGFEVTTTYTKLFTGNIARHLFLKMKKSFTCKCSRCSDPTEKGAFISGLYCRDTNCTGLVVPEITGLPHPNWNCLVCKQKSTHAQMMKSQDFASGAINAKVNSNSLRTLVQYLNEKSDSFIPSSNYVVIDAKMSVLQRLQQGREDCSEELAHNTRLRYSRDITQLMDKLGLGDSLLRTHLEELLRREEERRAKRLADEAEKQRKLAELQAKAAEADKLLEVLQKEQSEQSEQAEPAGTADPGTAPAAPPVATAELA
Protein: High-affinity nitrate transporter 2.2 (AtNRT2:2) (Q9LMZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in high-affinity nitrate transport.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nitrate reductase 2
- Nitrate reductase 1
- Ferredoxin--nitrite reductase, chloroplastic
- High-affinity nitrate transporter 3.1
- Protein NRT1/ PTR FAMILY 6.3
- Protein NRT1/ PTR FAMILY 4.6
- Transcription factor TGA4
- Protein NRT1/ PTR FAMILY 7.3
- Transcription factor TGA1
- Protein NRT1/ PTR FAMILY 2.12
Sequence:
MGSTDEPGSSMHGVTGREQSYAFSVDGSEPTNTKKKYNLPVDAEDKATVFKLFSFAKPHMRTFHLSWISFSTCFVSTFAAAPLIPIIRENLNLTKHDIGNAGVASVSGSIFSRLVMGAVCDLLGPRYGCAFLVMLSAPTVFSMSFVSDAAGFITVRFMIGFCLATFVSCQYWMSTMFNSQIIGLVNGTAAGWGNMGGGITQLLMPIVYEIIRRCGSTAFTAWRIAFFVPGWLHIIMGILVLTLGQDLPGGNRAAMEKAGEVAKDKFGKILWYAVTNYRTWIFVLLYGYSMGVELSTDNVIAEYFFDRFHLKLHTAGIIAACFGMANFFARPAGGWASDIAAKRFGMRGRLWTLWIIQTSGGLFCVWLGRANTLVTAVVSMVLFSLGAQAACGATFAIVPFVSRRALGIISGLTGAGGNFGSGLTQLVFFSTSRFTTEEGLTWMGVMIVACTLPVTLIHFPQWGSMFFPPSNDSVDATEHYYVGEYSKEEQQIGMHLKSKLFADGAKTEGGSSVHKGNATNNA