wanglab/gogpt-training-data huggingface dataset:
Protein: CRS2-associated factor 2, chloroplastic (Chloroplastic group IIA intron splicing facilitator CRS2-associated factor 2) (Q9LDA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein required for the splicing of group IIB introns in chloroplasts. Forms splicing particles with CRS2. Interacts with RNA and confers intron specificity of the splicing particles.
Subcellular location: Plastid, chloroplast stroma {ECO:0000305}.
Interaction partners:
- Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic
- Ribonuclease III domain-containing protein RNC1, chloroplastic
- Transcription termination factor MTERF4, chloroplastic
- Protein WHAT'S THIS FACTOR 1 homolog
- Protein THYLAKOID ASSEMBLY 8, chloroplastic
- CRM-domain containing factor CFM3A, chloroplastic/mitochondrial
- Pentatricopeptide repeat-containing protein At5g04810, chloroplastic
- CRM-domain containing factor CFM9, mitochondrial
- CRM-domain containing factor CFM3B, chloroplastic
- NAD
Sequence:
MAIVASLRDINLFSSLPSTPPMADSSSGTFRPAPPIPIPKYAPSNRNRNQKTNHQTDTNPKKPQSNPALKLPHHRTRYYKPVKEGVISSDGDRTILIGDSGVSYQLPGAPFEFQFSYSETPKVKPVGIREPAFMPFAPPTMPRPWTGKAPLKKSKKKIPLFDSFNPPPAGKSGVKYVEMPGPLPFGRYPKEGMNREEVLGEPLKRWEKGMLIKPHMHDNRQVNLGRDGFTHNMLELIHSHWKRRRVCKVRCKGVPTVDMNNVCRVLEEKTGGEIIHRVGGVVYLFRGRNYNYRTRPQYPLMLWKPAAPVYPKLIQEVPEGLTKEEAHEFRVKGKSLRPICKLSKNGVYVSLVKDVRDAFELSSLVKVDCPGLEPSDYKKIGAKLKELVPCVLLSFDDEQILMWRGREWKSRFVDNPLIPSLSETNTTNELDPSDKPSEEQTVANPSTTISSPKMISLWQRALESSKAVILEELDLGPDDLLKKVEELEGTSLAAEHTYTAMVLSNTDGAAEDYVDEKDRSEEYYSDIDDDFDDECSDDESLDPVGPVGSLPVDKIVRKLRERLK
Protein: Sodium- and chloride-dependent taurine transporter (Solute carrier family 6 member 6) (Q00589)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Mediates sodium- and chloride-dependent transport of taurine. Can also mediate transport of beta-alanine, hypotaurine and gamma-aminobutyric acid (GABA) (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P31641}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGGGLPVFFLEVIIGQYTSEGGITCWEKICPLFSGIGYASIVIVSLLNIYYVIILAWATYYLFQSFQSELPWAHCNHSWNTPQCMEDTMRKNKSLWITLSTKNFTSPVTEFWERNVLSLSSGIDDPGSLKWDLALCLLLVWLVCFFCIWKGVKSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDISRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQVTSLVDLYPSFLRKGFRREIFIAFMCSISYLLGLSMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGSDNLYDGIEDMIGYRPGPWMKYSWAVVTPVLCVGCFIFSLVKYVPLTYNKVYVYPTWAIGLGWSLALSSMMCVPLVMVIRLCQTEGPFLVRLKYLLTPREPNRWAVEREGATPYSSRLAVNGALMKPTHIIVETMM
Protein: BMP/retinoic acid-inducible neural-specific protein 3 (Q499E0)
Organism: Mus musculus (Mouse)
Function: Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition. Promotes pituitary gonadotrope cell proliferation, migration and invasion, when overexpressed. May play a role in cell pituitary tumor development.
Subcellular location: Secreted {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:17138656}.
Interaction partners:
Sequence:
MIWRRRAGAELSSLMALWEWIVLSLHCWVLAVAAVSDQHATSPFDWLLSDKGPFHRSQEYTDFVDRSRQGFSTRYKIYREFGRWKVNNLAVERRNFLGSPLPLAPEFFRNIRLLGRRPTLQQITENLIKKYGTHFLLSATLGGEESLTIFVDKRKLSKRSEGSETSTNSSSVTLETLHQLAASYFIDRDSTLRRLHHIQIASTAIKVTETRTGPLGCSNYDNLDSVSSVLVQSPENKIQLQGLQVLLPDYLQERFVQAALSYIACNSEGEFICKDNDCWCHCGPKFPECNCPSMDIQAMEENLLRITETWKAYNSDFEDSDEFKFFMKRLPMNYFLNTSTIMHLWTMDSNFQRRYEQLENSMKQLFLKAHRIVHKLFSLSKRCHKQPLISLPRQRTSTYWLTRIQSFLYCNENGLLGSFSEETHSCTCPNDQVVCTAFLPCTVGDASACLTCAPDNRTRCGTCNTGYMLSQGLCKPEVAESTDHYIGFETDLQDLEMKYLLQKTDRRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSSLVHMILGLSLQICLTKNSTLEPVLAVYVNPFGGSHSESWFMPVSESSFPDWERTKLDLPLQCYNWTLTLGNKWKTFFETVHIYLRSRIKANGPNSNESIYYEPLEFIDPSRNLGYMKINNIQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNKLSPPGQRRLDLFSCLLRHRLKLSTSEVVRIQSALQAFNAKLPNTVDYDTTKLCS
Protein: TGFB-induced factor homeobox 1 (A0A8I6ACG1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MKSKKGVVAAASGSDSEDEDSMDSPLDLSSSAASGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLSQQTHLSTLQVCNWFINARRRLLPDMLRKDGKDPNQFTISRRGAKISEASSIEAAMGIKNFMPTLEESPFHSCVVGPNPTLGRPVSPKPPSPGPILARPSVICHTTVTALKDGPFSLCQAVSVGHSTDVQQVAPSNFTDASLRYPEDTCKSGPSPNPQSGLFNTPPPTPPDLNQDFSGFQLLVDVALKQAAEMELQAKLTA
Protein: GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 1) (O-FucT-1) (Q91ZW2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6EV70}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 2
- Coagulation factor VII
- Protein O-glucosyltransferase 1
- EGF domain-specific O-linked N-acetylglucosamine transferase
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
- Beta-1,3-N-acetylglucosaminyltransferase manic fringe
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- Alpha-
- Xyloside xylosyltransferase 1
Sequence:
MGAAAWAPPHLLLRASFLLLLLLLPLRGRSAGSWDLAGYLLYCPCMGRFGNQADHFLGSLAFAKLLNRTLAVPPWIEYQHHKPPFTNLHVSYQKYFKLEPLQAYHRVVSLEDFMENLAPSHWPPEKRVAYCFEVAAQRSPDKKTCPMKEGNPFGPFWDQFHVSFNKSELFTGISFSASYKEQWTQRFPAKEHPVLALPGAPAQFPVLEEHRELQKYMVWSDEMVRTGEALISAHLVRPYVGIHLRIGSDWKNACAMLKDGTAGSHFMASPQCVGYSRSTATPLTMTMCLPDLKEIQRAVTLWVRALNARSVYIATDSESYVSEIQQLFKDKVRVVSLKPEVAQIDLYILGQADHFIGNCVSSFTAFVKRERDLHGRQSSFFGMDRPSQLRDEF
Protein: Vacuolar protein sorting-associated protein ist1 (O74490)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}. Endosome {ECO:0000250}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 46
- Uncharacterized protein C162.06c
- Vacuolar protein sorting-associated protein vts1
- Suppressor protein of bem1/bed5 double mutants
- ESCRT-III complex subunit did4
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein sorting-associated protein 24
- Vacuolar-sorting protein snf7
- Vacuolar protein-sorting protein bro1
- Mitochondrial import protein 2
Sequence:
MSRLQIQLKLAASRIEILRQKEEALAKQARRNVALGLKSYSPALAKARIEPLIMQDIYIELLELLQVDVEILANRCVVLEKRAFNDSMSFKSSLYHVMAAAPQLQIKELRFVHDFLVKLYGKEFARLSDPDLATNDTAFYQLLYPPIPKDELVEAYRKELIRTYFPNDYPKEANKDIPSSAEADTMLNLESSENREQPTSLKEENTQEDDEKVNGNLANISKRAEPQNNGSTNASSLQSSNYLPTNPTLTHSNKAPSFEELAARLDRLKHL
Protein: Thyroid hormone receptor beta (TR-beta) (TRb) (Nuclear receptor subfamily 1 group A member 2) (Thyroid hormone receptor beta-1) (TRbeta1) (Q9PVE4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for the thyroid gland hormone triiodothyronine (T3). Transactivating activity is ligand-dependent, and is repressed in the absence of T3.
Subcellular location: Nucleus.
Interaction partners:
- Iodothyronine deiodinase
- Iodothyronine deiodinase
- Monocarboxylate transporter 10
- UDP-glucuronosyltransferase
- Solute carrier organic anion transporter family member
- Transthyretin
- Thyroglobulin.
- Nuclear receptor corepressor 2
- Thyroid-stimulating hormone subunit beta a.
- Nuclear receptor corepressor 1.
Sequence:
MSEQADKCNSRWKDEAMQNGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLNPTYACKYEGKCVIDKVTRNQCQECRFKKCIAVGMATDLVLDDSKRLAKRKLIEENRERRRREELQKTVWDRPEPTQEEWEMIRVVTEAHMATNAQGNHWKQKRKFLSAVGVKEAKPEDIGSAPIVNAPEGNKVDIEAFSQFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGVSLSSFNLDDSEVALLQAVILLSSDRPGLTSVERIERCQEEFLLAFEHYINYRKHKVAHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
Protein: Actin-interacting protein 1-2 (Q9LV35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds actin. Enhances the F-actin depolymerization activity of actin-depolymerizing factor (ADF) proteins.
Interaction partners:
- Actin-7
- Actin-12
- F-actin-capping protein subunit beta
- Actin-3
- Actin-1
- Protein pleiotropic regulatory locus 1
- Guanine nucleotide-binding protein subunit beta
- Actin-8
- Cyclase-associated protein 1
- Ribosome biogenesis protein WDR12 homolog
Sequence:
MELSETYACVPSTERGRGILISGNSKSDTILYTNGRSVVTLDLNNPLKVSIYGEHAYPATVARYSPNGEWIASGDVSGTVRIWGAYNDHVLKNEFKVLAGRIDDLQWSADGMRIVASGDGKGKSLVRAFMWDSGSNVGEFDGHSRRVLSCAIKPTRPFRIVTCGEDFLVNFYEGPPFKFKLSSREHSNFVNCVRFAPDGSKFITVSSDKKGIIYDGKTCEILGELSSDDGHKGSIYAVSWSPDGKQVLTVSADKSAKIWDISDNGSGSLNTTLNCPGSSGGVDDMLVGCLWQNDHIVTVSLGGTISIFSASDLDKSPFQFSGHMKNVSSLAVLKGNADYILSGSYDGLICKWMLGRGFCGKLQRTQNSQIKCFAAHEEEIVTSGYDNKISRISYKDDQCTNEESIDIGNQPKDLSLAPLSPDLLLVTFESGVVFLRDGKVVSTINLGFIVTALAVTPDGTEAVIGGQDGKLHLYSINGDSLTEEAVLERHRGAISVIRYSPDLSMFASADLNREAVVWDRVSREMKLKNMLYHSARINCLAWSPNSTMVATGSLDTCVIVYEVDKPASSRMTIKGAHLGGVYGLGFADDSHVVSSGEDACIRVWSFTPQ
Protein: Methyltransferase-like protein 22 (EC 2.1.1.-) (Q9BUU2)
Organism: Homo sapiens (Human)
Function: Protein N-lysine methyltransferase. Trimethylates KIN at Lys-135 (in vitro).
Subcellular location: Nucleus {ECO:0000269|PubMed:23349634}.
Interaction partners:
- DNA/RNA-binding protein KIN17
- Protein N-lysine methyltransferase METTL21A
- Electron transfer flavoprotein beta subunit lysine methyltransferase
- Protein N-lysine methyltransferase METTL21D
- Histone-arginine methyltransferase METTL23
- Histidine protein methyltransferase 1 homolog
Sequence:
MVQLAPAAAMDEVTFRSDTVLSDVHLYTPNHRHLMVRLNSVGQPVFLSQFKLLWSQDSWTDSGAKGGSHRDVHTKEPPSAETGSTGSPPGSGHGNEGFSLQAGTDTTGQEVAEAQLDEDGDLDVVRRPRAASDSNPAGPLRDKVHPMILAQEEDDVLGEEAQGSPHDIIRIEHTMATPLEDVGKQVWRGALLLADYILFRQDLFRGCTALELGAGTGLASIIAATMARTVYCTDVGADLLSMCQRNIALNSHLAATGGGIVRVKELDWLKDDLCTDPKVPFSWSQEEISDLYDHTTILFAAEVFYDDDLTDAVFKTLSRLAHRLKNACTAILSVEKRLNFTLRHLDVTCEAYDHFRSCLHALEQLADGKLRFVVEPVEASFPQLLVYERLQQLELWKIIAEPVT
Protein: Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (Q6FP06)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- 6-phosphogluconolactonase-like protein
- 6-phosphogluconolactonase-like protein
- Glucose-6-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- 6-phosphogluconolactonase-like protein
- Pyruvate dehydrogenase E1 component subunit alpha
- Fructose-bisphosphate aldolase
- Phosphotransferase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glyceraldehyde-3-phosphate dehydrogenase 1
Sequence:
MSEPVKFEKNTVVVVFGASGDLAKKKTFPALFGLFREGYLHESTKIIGYARSSLTVEELTERIKPHLKTPRGKEDEAKIPQFFKLLTYVSGPYDQDDGFIRLREQIETFEGAKCSTVPHRLFYFALPPSVFLPVATNIKRLVYAENGVTRLIVEKPFGRDLETARKLQADLSPLFKEEEIYRIDHYLGKELVKNLLVMRFGNQFLNSAWNRDNIQSIQISFKEPFGTEGRGGYFDNIGIIRDVMQNHLLQVLTLLTMERPVSFDPEAIRDEKVKVLKAMAPFDPKDILIGQYGKSEDGSKPAYLDDETVKPGSKCVTFAAIAFQIENERWEGVPIVMRAGKALNEGKVEIRLQYKAVASGVFKNIPHNELVIRIQPNEAVYMKFNAKTPGLSNATQVTDLDLTYSSRYKDFWIPEAYEALIRDALLGDHSNFVRDDELDVSWSLFTPLLNYLEGPDAPQPEIYPYGSRGPSGLRDYLKKHNYMIEEKHPYTWPVTTPDED
Protein: Subtilisin-like protease SBT5.3 (EC 3.4.21.-) (Auxin-induced in root cultures protein 3) (Subtilase subfamily 5 member 3) (AtSBT5.3) (Subtilisin-like protease AIR3) (Q9ZSP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease. Has a substrate preference for the hydrophobic residues Phe and Ala and the basic residue Asp in the P1 position, and for Asp, Leu or Ala in the P1' position. May play a role in the degradation of structural proteins in the extracellular matrix of cells located above sites of lateral root formation and thus facilitate lateral root emergence (By similarity).
Subcellular location: Secreted {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Ureide permease 4
- Subtilisin-like protease
Sequence:
MKLTHNFSFLLLLLLVHMSSKHILASKDSSSYVVYFGAHSHVGEITEDAMDRVKETHYDFLGSFTGSRERATDAIFYSYTKHINGFAAHLDHDLAYEISKHPEVVSVFPNKALKLHTTRSWDFLGLEHNSYVPSSSIWRKARFGEDTIIANLDTGVWPESKSFRDEGLGPIPSRWKGICQNQKDATFHCNRKLIGARYFNKGYAAAVGHLNSSFDSPRDLDGHGSHTLSTAAGDFVPGVSIFGQGNGTAKGGSPRARVAAYKVCWPPVKGNECYDADVLAAFDAAIHDGADVISVSLGGEPTSFFNDSVAIGSFHAAKKRIVVVCSAGNSGPADSTVSNVAPWQITVGASTMDREFASNLVLGNGKHYKGQSLSSTALPHAKFYPIMASVNAKAKNASALDAQLCKLGSLDPIKTKGKILVCLRGQNGRVEKGRAVALGGGIGMVLENTYVTGNDLLADPHVLPATQLTSKDSFAVSRYISQTKKPIAHITPSRTDLGLKPAPVMASFSSKGPSIVAPQILKPDITAPGVSVIAAYTGAVSPTNEQFDPRRLLFNAISGTSMSCPHISGIAGLLKTRYPSWSPAAIRSAIMTTATIMDDIPGPIQNATNMKATPFSFGAGHVQPNLAVNPGLVYDLGIKDYLNFLCSLGYNASQISVFSGNNFTCSSPKISLVNLNYPSITVPNLTSSKVTVSRTVKNVGRPSMYTVKVNNPQGVYVAVKPTSLNFTKVGEQKTFKVILVKSKGNVAKGYVFGELVWSDKKHRVRSPIVVKL
Protein: Geranylfarnesyl diphosphate synthase (GFPS) (EC 2.5.1.81) (Farnesylgeranyl diphosphate synthase) (FGPP synthase) (Q9UWR6)
Organism: Aeropyrum pernix
Function: Probably involved in biosynthesis of the precursor for C25 (sesterterpanyl chain) moiety of C25-C25 diether (2,3-di-O-sesterterpanyl-sn-glycero) membrane lipid. Catalyzes the condensation of isopentenyl pyrophosphate with the allylic pyrophosphates to yield all-trans geranylfarnesyl diphosphate (GFPP). Geranylgeranyl diphosphate (GGPP) is the preferred substrate, however methylallyl diphosphate (DMAPP), farnesyl diphosphate (FPP) and geranyl diphosphate (GPP) can also be used as allylic substrate.
Interaction partners:
Sequence:
MLIDHYIMDFMSITPDRLSGASLHLIKAGGKRLRPLITLLTARMLGGLEAEARAIPLAASIETAHTFSLIHDDIMDRDEVRRGVPTTHVVYGDDWAILAGDTLHAAAFKMIADSREWGMSHEQAYRAFKVLSEAAIQISRGQAYDMLFEETWDVDVADYLNMVRLKTGALIEAAARIGAVAAGAGSEIEKMMGEVGMNAGIAFQIRDDILGVIGDPKVTGKPVYNDLRRGKKTLLVIYAVKKAGRREIVDLIGPKASEDDLKRAASIIVDSGALDYAESRARFYVERARDILSRVPAVDAESKELLNLLLDYIVERVK
Protein: Kanamycin B dioxygenase (EC 1.14.11.37) (Kanamycin biosynthesis protein J) (Q6L732)
Organism: Streptomyces kanamyceticus
Function: Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A.
Interaction partners:
Sequence:
MALAAPPGELTLALTPDDKTLDPASLDRALAILAEHGILVLTGMLRTRLTDQLRTAMLDDLPEVLRQQDVPTNFVPGHVQQDPPVRESLLFPDVLLNPVVYQITHAVLGADARNAVYSGNMNLPGSHEQPVHLDEPHLWPGISHPPYCLCVDVPLIDFTLENGSTEYWPGSHVLNPDECYDERGCVLPAELERRRAVAPPVRFPIPVGSVVIRDGRLWHRGVPNLSAAPRPLLAMTHYTEWFDMPPIQLPDTVKSWVDGSDRHTHAHFVAGDVDHLTGDHPFAVR
Protein: Disintegrin and metalloproteinase domain-containing protein 17 homolog (ADAM 17 homolog) (EC 3.4.24.-) (Q94316)
Organism: Caenorhabditis elegans
Function: Metalloprotease (By similarity). Acts together with protease sup-17 to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision. By modulating glp-1/Notch signaling, plays a role in germline development.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Protein lin-12
Sequence:
MKIQDRSLLIFLVLGILKSDAFNTRVKRHAPIRFQRSTRQSVVHFEFLDQEYVVDLEPNHSTFHENFKVFTQDGPQIVPRDEYIGTVREPRAGRAVLTQLEENVYIGSLYFVDDTLHLEPSYPHQLSDDLGPVVGYFESDLDLNLDLSAMPVRNQVSFRRANPFLKHRRAIAIPSDRRKDVLNVKRNRCTLKLVADYSFYSIFGKNNTGIVTKFLVNMIARVNEIYTPINWDVGKEDDISGRGRFQNMGFSIKEIKVLDRPNASDSHYNSYSRIWEVERLLREFAFAEGSKDFCLVHLVTARTFREVATLGLAYVSYKKWDETAGGICSKQETFNGRVAYINVLLSTSFANSEQSTYPLITKEIDIVVSHEYGHAWGATHDPTIDSDDPDVEECSPNDQNGGKYLMSQYAQKGYDANNVLFSPCSRKLIRDVLIGKWESCFQEEMTSFCGNGIVEDGEECDNGVDTDNEFNCCDKFCRLAVGAKCSPLNHICCTPTCQFHNSTHVCLPGDSLLCKADAVCNGFSGECPSAPPVRDGQECLEGGECLNGVCLPFCEKMSIGKKSCICEDLELSCRLCCRDYNGTCAPVPGHVYLRDGVRCSKGSCRDRKCVNEVVDNVRNYFLITFQTTGGVLEFIKTHIVVIAIIFFTLIFVGIYKIVKYGENFTEKVTHKTAGGCRSVFVKADVN
Protein: pH-response transcription factor pacC/RIM101 (J9WUP1)
Organism: Penicillium digitatum (Green mold)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTENHTPSTTQATLPAPVAEPAPIQATPTPSASVTATAVAATAAVNNPSMNGAGELLPCQWVGCTEKSPTAESLYEHVCERHVGRKSTNNLNLTCQWGTCNTTTVKRDHITSHIRVHVPLKPHKCDFCGKAFKRPQDLKKHVKTHADDSEIRSPEPSMKHPDMMFPQNPKGYAAATHYFESPINGINGQYSHAPPPQYYQPHPQPQAATNPHSYGNVYYALSQGQEGGHPYDRKRGYDALNEFFGDLKRRQFDPNSYAAVGQRLLGLQALQLPFLSGPVPEYQQMPASVAVGGGGYSPGGSQPPGYHLPPMSNVRTKNDLINIDQFLEQMQNTIYESDENVAAAGVAQPGAHYVHGGMNYRATHSPPIQLPPSHMTATTSAPMGAASAHSPSVGTPALSPPSSAQSYTSNRSPISMHHAHRVSPPHESGPGMYPRLPSATVADSMSAGYPNTSGAAPPSTLSVAYDHDDRRRYTGGTLQRARPAERASPEDRMDISHDSKYDGERTPTKAALHISESLIDPALSGTSSDPDQEAAKRTAQAATEVAERDVNVAWVEKVRLLENLRRLVSELLEAGTAEYDAHTSSASPTPGLDAMEGVENTKERAASEQLREEPKSASEGVFYPTLRGVDEDEDGGSKMPE
Protein: Histone H3 (C1BF09)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAVHAKRVTIMPKDIQLARRIRGERA
Protein: Kunitz-type protease inhibitor 1 (Hepatocyte growth factor activator inhibitor type 1) (HAI-1) (O43278)
Organism: Homo sapiens (Human)
Function: Inhibitor of HGF activator. Also acts as an inhibitor of matriptase (ST14).
Subcellular location: Secreted {ECO:0000269|PubMed:9045658}. Cytoplasm {ECO:0000269|PubMed:28710277}. Cell membrane {ECO:0000269|PubMed:28710277}.
Interaction partners:
- Hepatocyte growth factor activator serine protease
- Suppressor of tumorigenicity 14 protein
- Hepatocyte growth factor
- Prostasin
- Hepatocyte growth factor-like protein
- Serine protease hepsin
Sequence:
MAPARTMARARLAPAGIPAVALWLLCTLGLQGTQAGPPPAPPGLPAGADCLNSFTAGVPGFVLDTNASVSNGATFLESPTVRRGWDCVRACCTTQNCNLALVELQPDRGEDAIAACFLINCLYEQNFVCKFAPREGFINYLTREVYRSYRQLRTQGFGGSGIPKAWAGIDLKVQPQEPLVLKDVENTDWRLLRGDTDVRVERKDPNQVELWGLKEGTYLFQLTVTSSDHPEDTANVTVTVLSTKQTEDYCLASNKVGRCRGSFPRWYYDPTEQICKSFVYGGCLGNKNNYLREEECILACRGVQGGPLRGSSGAQATFPQGPSMERRHPVCSGTCQPTQFRCSNGCCIDSFLECDDTPNCPDASDEAACEKYTSGFDELQRIHFPSDKGHCVDLPDTGLCKESIPRWYYNPFSEHCARFTYGGCYGNKNNFEEEQQCLESCRGISKKDVFGLRREIPIPSTGSVEMAVAVFLVICIVVVVAILGYCFFKNQRKDFHGHHHHPPPTPASSTVSTTEDTEHLVYNHTTRPL
Protein: Ubiquitin carboxyl-terminal hydrolase 32 (EC 3.4.19.12) (Deubiquitinating enzyme 32) (Renal carcinoma antigen NY-REN-60) (Ubiquitin thioesterase 32) (Ubiquitin-specific-processing protease 32) (Q8NFA0)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20549504}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- TBC1 domain family member 3
- TBC1 domain family member 3B
Sequence:
MGAKESRIGFLSYEEALRRVTDVELKRLKDAFKRTCGLSYYMGQHCFIREVLGDGVPPKVAEVIYCSFGGTSKGLHFNNLIVGLVLLTRGKDEEKAKYIFSLFSSESGNYVIREEMERMLHVVDGKVPDTLRKCFSEGEKVNYEKFRNWLFLNKDAFTFSRWLLSGGVYVTLTDDSDTPTFYQTLAGVTHLEESDIIDLEKRYWLLKAQSRTGRFDLETFGPLVSPPIRPSLSEGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRDMVVALLEVWKDNRTDDIPELHMDLSDIVEGILNAHDTTKMGHLTLEDYQIWSVKNVLANEFLNLLFQVCHIVLGLRPATPEEEGQIIRGWLERESRYGLQAGHNWFIISMQWWQQWKEYVKYDANPVVIEPSSVLNGGKYSFGTAAHPMEQVEDRIGSSLSYVNTTEEKFSDNISTASEASETAGSGFLYSATPGADVCFARQHNTSDNNNQCLLGANGNILLHLNPQKPGAIDNQPLVTQEPVKATSLTLEGGRLKRTPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIKNSKTDIPELELFPRYLLFLRQQPATRTQQSNIWVNMGNVPSPNAPLKRVLAYTGCFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSENYLTLLDDEDHKLEYLKIQDEQHLVIEVRNKDMSWPEEMSFIANSSKIDRHKVPTEKGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGTTPVRYGLRLNMDEKYTGLKKQLSDLCGLNSEQILLAEVHGSNIKNFPQDNQKVRLSVSGFLCAFEIPVPVSPISASSPTQTDFSSSPSTNEMFTLTTNGDLPRPIFIPNGMPNTVVPCGTEKNFTNGMVNGHMPSLPDSPFTGYIIAVHRKMMRTELYFLSSQKNRPSLFGMPLIVPCTVHTRKKDLYDAVWIQVSRLASPLPPQEASNHAQDCDDSMGYQYPFTLRVVQKDGNSCAWCPWYRFCRGCKIDCGEDRAFIGNAYIAVDWDPTALHLRYQTSQERVVDEHESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCQHKPLTPQGDELSEPRILAREVKKVDAQSSAGEEDVLLSKSPSSLSANIISSPKGSPSSSRKSGTSCPSSKNSSPNSSPRTLGRSKGRLRLPQIGSKNKLSSSKENLDASKENGAGQICELADALSRGHVLGGSQPELVTPQDHEVALANGFLYEHEACGNGYSNGQLGNHSEEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFYEQQGIDYAQFLPKTDGKKMADTSSMDEDFESDYKKYCVLQ
Protein: Oligopeptide permease homolog AI (O31304)
Organism: Borreliella burgdorferi (Lyme disease spirochete) (Borrelia burgdorferi)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MKYIKIALMLIIFSLIACISNAKKEKIVFRVSNLSEPSSLDPQLSTDPYGSNIITNLFLGLAVKDSQTGKYKPGLAKSWNISEDGIIYTFNLREDIVWSDGVAITAEEIKKSYLRILNKKTAAMYANLIKSTIKNAQEYFDETVPESELGIKAIDSKTLEITLTSPKPYFPDMLTHSAYIPVPMHIVEQYGENWTNPENIVVSGAYKLKERSINDKIVIEKNEKYYNAKNVEIDEVIFYPTEGSVAYNMYINGELDFLQGAEKNNLEEIKIRDDYYSGLKNGMAYIAFNTTIKPLDNLKVRQAISLAIDRETLTKVVLKGSSDPTRNLTPKFDDYSYGKNLILFDPENAKKLLAEAGYPDGKGFPTLKYKISEGRPTTAEFLQEQFKKILNINLEIENEEWTTFLGSRRTGNYQMSSVGWIGDYFNPLTFLDSLFTTENHFLGAYKYSNKEYDALIKKSNFELDPIKRRDILRQAEEIIAEKDFPMAPLYIPKSHYLFRNDKWTGWVPNIAESYLYEDIKTKK
Protein: Beta-1,4-galactosyltransferase 5 (Beta-1,4-GalTase 5) (Beta4Gal-T5) (b4Gal-T5) (EC 2.4.1.-) (Beta-1,4-GalT II) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 5) (O43286)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity). Plays a role in the glycosylation of BMPR1A and regulation of its protein stability (By similarity). Essential for extraembryonic development during early embryogenesis (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000250|UniProtKB:A0A1S6M251}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Ceramide glucosyltransferase
- Beta-1,4-galactosyltransferase 6
Sequence:
MRARRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNVRTIGAQVYEQVLRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDYIHELFSKDPTIKLGGHWKPSDCMPRWKVAILIPFRNRHEHLPVLFRHLLPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPHHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYFANITYDALYKNITVNLTPELAQVNEY
Protein: Neurensin-1 (Neuro-p24) (Vesicular membrane protein of 24 kDa) (Vesicular membrane protein p24) (P97799)
Organism: Mus musculus (Mouse)
Function: May play an important role in neural organelle transport, and in transduction of nerve signals or in nerve growth. May play a role in neurite extension.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, neuron projection {ECO:0000269|PubMed:16527258}.
Interaction partners:
- Serine/threonine-protein phosphatase with EF-hands 2
- Ribonucleoside-diphosphate reductase large subunit
Sequence:
MTSCSNTCGSRRAQADTEGGYQQRYGVRSYLHQFYEDCTASIWEYEDDFQIQRSPNRWSSVFWKVGLISGTVFVILGLTVLAVGFLVPPKIEAFGEADFMVVDTHAVKYNGALDTCKLAGAVLFCIGGTSMAGCLLMSVFAKSYSKEEKFLQQKFKERIADIKAHTQPITKAPGPGDTKIPVTLSRVQNVQPLSAT