wanglab/gogpt-training-data huggingface dataset:
Protein: Rabphilin (Q768S2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDFQNRNNTANKFVCPSDRQLALRAKLKAGWSSSKTSEPLRPEEQEAIISVIRRNEEIEVAERQRVGRLVERVEKIKQHAVERGPNCCRLCGDTFGILRPQRILCEDCRQSVCTKCSVDINIRYHTSERSREIWLCRICSETREMWKKSGAWFFKGLPKYDMPRSASATPIPNPGPGSMAGDTR
Protein: Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase Sak) (Q7ZVS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as sass6, cenpj/cpap, ccp110, cep135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O00444}. Note=Associates with centrioles throughout the cell cycle. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles (By similarity). {ECO:0000250}.
Interaction partners:
- SCL-interrupting locus protein homolog
- Spindle assembly abnormal protein 6 homolog
- Centrosomal protein 192.
- Centrosomal P4.1-associated protein
- Centrosomal protein of 135 kDa
- Extra spindle pole bodies-like 1, separase.
- Kinesin family member 11
- Centrosomal protein of 63 kDa
- Pericentrin
- Centrosomal protein 152
Sequence:
MSVSIGDKIEDFKVLTLLGKGSFACVYRAKSVNTGLEVAIKMIDKKAMHKAGMVQRVINEVEIQCRLKHPSVLELYNYFEDSNYVYLVLEMCHNGEMSRYLKERKNPFTEEEARHFMHQIVKGMLYLHTHGIMHRDLTLTNLLLTTSMNIKIADFGLATQLKLPSEKHFTMCGTPNYISPEVATRSAHGLESDVWSLGCMFYAFLTGRPPFDTDTVKRTLNKVVLGEYQMPMHISAEAQDLIQQLLQKNPALRPSLSAVLDHPFMTQSGPTASKDSGSSNGGSIDSGIATISTASNATNNSSSSRLQRRTRQMIGQPLPSRMAPIPSHSHHSTSSSFKSGQDWQPNSQDDLSRMGVGRIPVGADSGRPHSRYLRRAHSSDRSAVGYSHNPQEAELERCHSEEMLSGAGRLFPQTSGYRNAPHGYSKHDRLPSPPVKQPANPASSFSTSTHSTRQQMPDSQTQPWFSNDGVFKRPADMSGHSSSGSFHSERGPIGTQTSCSDKPSGLHSQQQPILFQHNNPGPCREDAFVSGHMSEPQAYSDAQFPCPPLSKGKANTEKKDKVCLKKSFPPLCAARLKPIRQKTKNAVVSILGNGEVCMELLKGQGAQERVKEVLRISCDGSMVTVYQPNEGKGFPVLDHPPSPPEDILICSFDDLPEKYWKKYQYATKFVQLVKSKTPKVTLYTKFAKCMLMENSPNPDLEVCFYDGAKTHKTSEQVRVVEKSGKSYTVKGDVGLSGLNPECRLYIELSEEGHRMCLSLEAAITAEEQRSAKNTPFFPITIGRRPVNPVPPAPAPSSSSSCRPAAAAEVAHVCLSPPQHPQITPSMISYAGSDLTTASVAKGSSPVHKDERTVNSGKVLKSIFVPNIGWVSQLTTGEVWVQFNDGSQLMVQVGVSCIIFTSPEGHITRYKENEKLPELVKEKLHCLSSILGLLANPAARC
Protein: Zinc finger protein 641 (F8VZ73)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLSEQTAALGTGWESMNVQLDGAEPQVERGSQEERPWRTVPGPLEHLCCDLEEEPQSLQEKAQSAPWVPAIPQEGNTGDWEMAAALLAAGSQGLVTIKDVSLCFSQE
Protein: Trans-aconitate 2-methyltransferase (EC 2.1.1.144) (P76145)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate at high affinity and of cis-aconitate, isocitrate, and citrate at lower velocities and affinities.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10224113}.
Interaction partners:
- (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase (Autoinducer 2-degrading protein LsrG) (AI-2-degrading protein LsrG) (Phospho-(S)-4,5-dihydroxy-2,3-pentanedione isomerase) (Phospho-AI-2 isomerase)
- 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
- Voltage-dependent anion channel-forming protein YneE
- Autoinducer 2-binding protein LsrB
- Autoinducer 2 import system permease protein LsrD
- Autoinducer 2 import ATP-binding protein LsrA
- Cellulose synthase operon protein C
- Transcriptional regulator LsrR
- Autoinducer 2 import system permease protein LsrC
Sequence:
MSDWNPSLYLHFSAERSRPAVELLARVPLENVEYVADLGCGPGNSTALLQQRWPAARITGIDSSPAMIAEARSALPDCQFVEADIRNWQPVQALDLIFANASLQWLPDHYELFPHLVSLLNPQGVLAVQMPDNWLEPTHVLMREVAWEQNYPDRGREPLAGVHAYYDILSEAGCEVDIWRTTYYHQMPSHQAIIDWVTATGLRPWLQDLTESEQQLFLKRYHQMLEEQYPLQENGQILLAFPRLFIVARRME
Protein: Spondin-1 (F-spondin) (Q8VCC9)
Organism: Mus musculus (Mouse)
Function: Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Amyloid-beta precursor protein
- Low-density lipoprotein receptor-related protein 8
- Amyloid beta precursor protein binding family B member 1
- Amyloid beta precursor like protein 1
Sequence:
MRLSPVSLRLSRGPALLALALPLAAALAFSDETLDKVTKSEGYCSRILRAQGTRREGYTEFSLRVEGDPDFYKPGSSYRVTLSAAPPSYFRGFTLIALKENQEGDKEEDHAGTFQIIDEEETQFMSNCPVAVTESTPRRRTRIQVFWIAPPTGTGCVILKASIVQKRIIYFQDEGSLTKKLCEQDPTLDGVTDRPILDCCACGTAKYRLTFYGNWSEKTHPKDYPRRANHWSAIIGGSHSKNYVLWEYGGYASEGVKQVAELGSPVKMEEEIRQQSDEVLTVIKAKAQWPAWQPVNVRAAPSAEFSVDRTRHLMSFLTMMGPSPDWNVGLSAEDLCTKECGWVQKVVQDLIPWDAGTDSGVTYESPNKPTIPQEKIRPLTSLDHPQSPFYDPEGGSITQVARVVIERIARKGEQCNIVPDNVDDIVADLAPEEKDEDDTPETCIYSNWSPWSACSSSTCEKGKRMRQRMLKAQLDLSVPCPDTQDFQPCMGPGCSDEDGSTCTMSEWITWSPCSVSCGMGMRSRERYVKQFPEDGSVCMLPTEETEKCTVNEECSPSSCLVTEWGEWDDCSATCGMGMKKRHRMVKMSPADGSMCKAETSQAEKCMMPECHTIPCLLSPWSEWSDCSVTCGKGMRTRQRMLKSLAELGDCNEDLEQAEKCMLPECPIDCELSEWSQWSECNKSCGKGHMIRTRTIQMEPQFGGVPCPETVQRKKCRTRKCLRSPSVQKLRWREARESRRSEQLREESDGEQFPGCRMRPWTAWSECTKLCGGGIQERYMTVKKRFKSSQFTSCKDKKEIRACNVHPC
Protein: Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase type II) (Carbapenem-hydrolyzing beta-lactamase BlaB-1) (CHbetaL-1) (Class B carbapenemase BlaB-1) (Metallo-beta-lactamase type II) (O08498)
Organism: Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MLKKIKISLILALGLTSLQAFGQENPDVKIEKLKDNLYVYTTYNTFNGTKYAANAVYLVTDKGVVVIDCPWGEDKFKSFTDEIYKKHGKKVIMNIATHSHDDRAGGLEYFGKIGAKTYSTKMTDSILAKENKPRAQYTFDNNKSFKVGKSEFQVYYPGKGHTADNVVVWFPKEKVLVGGCIIKSADSKDLGYIGEAYVNDWTQSVHNIQQKFSGAQYVVAGHDDWKDQRSIQHTLDLINEYQQKQKASN
Protein: WD repeat-containing protein JIP5 (Jumonji domain-interacting protein 5) (Q06214)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome biogenesis protein 15
- Ribosome biogenesis protein YTM1
- U3 small nucleolar RNA-associated protein 10
- ATP-dependent RNA helicase HAS1
- Probable ATP-dependent RNA helicase DHR1
- rRNA biogenesis protein RRP36
Sequence:
MAKSKKKTDVVDSTNLPILELLSLKAPIFQSLLHPELPIIITGFGTGHIVCHRYDPAKLQSHLDRRRRIDTATTGKDAKKGVCPWIRLDIDLETGDLKFVDIEEQQQQKQTGKDEDLGVKTLWKTKRHKGSVRAMCFDSKGDNIFSVGSDNVLKKANTMTGKVVKKVNLSSLFNSEEKKNDKFTKLCASQTHPFILIGDESGNIHVINSENLALSNSIRSIHFGDSINDIFHFDKRSAYKFISLGQTTLAYFDVRDKDAKPNVAGNEDGKILISDDQEDEVLCGCFVDPEVADTLLCGMGEGIVTVWKPNKNDLEDQMSRIKISKDESIDCIVPTLQDDNCVWCGCSNGNIYKVNAKLGKVVEIRNHSELDEVSFVDLDFEYRVVSGGLENIKIWELSSDDVEENASVESDSDEPLSHSDEDLSDDTSSDDETTLVGLSKEELLDELDKDLKEDHQEEKESNSKSVKKRKIMKENNKKKDLYEHGIKKFDDL
Protein: Glycogen phosphorylase, brain form (EC 2.4.1.1) (P11216)
Organism: Homo sapiens (Human)
Function: Glycogen phosphorylase that regulates glycogen mobilization. Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Interaction partners:
- Glycogen debranching enzyme
- 1,4-alpha-glucan-branching enzyme
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen phosphorylase, liver form
- Pancreatic alpha-amylase
- Alpha-amylase 2B
- demerged
- Maltase-glucoamylase
- Phosphopentomutase
- Glycogen [starch] synthase, liver
Sequence:
MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKVDWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFVPRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVEALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEAYMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNIPRD
Protein: RHOMBOID-like protein 10, chloroplastic (AtRBL10) (EC 3.4.21.-) (F4ICF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Required for correct root growth, floral development, fertility and photoprotection. May be involved in TIC22 processing during its import and in AOS accumulation in the chloroplast membrane.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:22416142, ECO:0000269|PubMed:22738221}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes probably to the inner membrane. {ECO:0000303|PubMed:22738221}.
Interaction partners:
- Rhomboid-like protein 11, chloroplastic
- Rhomboid-like protein 16, chloroplastic
- Rhomboid-like protein 17, chloroplastic
- Sec-independent protein translocase protein TATA, chloroplastic
- Signal peptide peptidase
- Rhomboid-like protein 20
- Rhomboid-like protein 18
- Rhomboid-like protein 15
- RHOMBOID-like protein 13
- Rhomboid-like protein 14, mitochondrial
Sequence:
MVSVSLSHHNLWPPESGSTAFRGFATAASVHACHHVSRHLRLDFHLRSSLKKLQHFSDDARMKFARYQRVFVFNGANFLKSRVDIRLSQSSPFVCFFNGGESRLNPRGGEEGSSNPETSKRNTVNGRRWTNVLLAINVIMYIAQIASDGKVLTWGAKINSLIERGQLWRLATASVLHANPMHLMINCYSLNSIGPTAESLGGPKRFLAVYLTSAVAKPILRVLGSAMSYWFNKAPSVGASGAIFGLVGSVAVFVIRHKQMVRGGNEDLMQIAQIIALNMAMGLMSRRIDNWGHIGGLLGGTAMTWLLGPQWKYEYTTRDGRRVFMDSAPIPLLLRWRNEQRRL
Protein: Progonadoliberin-1 (Progonadoliberin I) [Cleaved into: Gonadoliberin-1 (Gonadoliberin I) (Gonadotropin-releasing hormone I) (GnRH-I) (Luliberin I) (Luteinizing hormone-releasing hormone I) (LH-RH I); GnRH-associated peptide 1 (GnRH-associated peptide I)] (Q28588)
Organism: Ovis aries (Sheep)
Function: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.
Subcellular location: Secreted.
Interaction partners:
- Gonadotropin-releasing hormone receptor
- KiSS-1 receptor
- non-specific serine/threonine protein kinase
- Placental prolactin-related protein 4
- Placental prolactin-related protein 3-like
- Uncharacterized protein
- Metastasis-suppressor KiSS-1
- Mitogen-activated protein kinase
- mitogen-activated protein kinase
- Pro-FMRFamide-related neuropeptide VF
Sequence:
QHWSYGLRPGGKRNAKNVIDSFQEIAKEVDQPVEPKCCGCIVHQSHSPLRDLKAALESLIE
Protein: Proliferation and apoptosis adaptor protein 15 (B1AKZ5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKNNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA
Protein: Dicarboxylate carrier 3, isoform A (FI08040p) (A1Z787)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Lethal
- Uncharacterized protein
- LD13176p
Sequence:
MGEDSSRRLPRWWFGGVCAAIAVTGTHPIDLIKVQLQTQSQADRKTVGEILKGIHERSGILGFYNGISASWFRQLTYTTTRFALYEAGKDYVDTQKVSSKMALATFAGIVGGIVGVPGDVVTVRLQNDVKLPEEKRRNYKHVFDGLFRIYKEEGVSSLFRGTVPAVSRAVLLTIGTNAAYDQVKQMLKIATGAGEGVPLHFATSTIAGCIAVVITQPLDVIKTTFMNAQPGEFSGIGGAFLSTAKQGPLAFYKGFIPALIRVSPNTIITFVLYEQARMRFGYLPPDK
Protein: Pin4p (A0A1D8PRZ6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- CCR4-NOT core subunit
- mRNA 3'-end-processing protein RNA14
- Pre-mRNA polyadenylation factor FIP1
- Endoribonuclease YSH1
- RNA-processing protein
- Cleavage and polyadenylation specificity factor subunit 2
- Protein CFT1
- Poly
- Polyadenylation factor subunit 2
- mRNA cleavage and polyadenylation factor CLP1
Sequence:
MDFRNLSTTPNQMDTVMQRRPSLSSLSSASGYSSSNYGGNPTPNPNNSNTNNNSSGNSNNNTHGNNTPKLSTQRLTNNRNLQSLWINQPSIAPSNVVPWVEQQQQQTLDSLENNTKTDSSNDASATNNNNVNVNVNANANVNANANIHAQTHVNTNVNANTTATSINASTISNTTPSINDTNDNAKKINVSMISNNNNNNSNNNNNNTNNSSTGNSNIVNMLPSVSNATTMNNSNSINSTTNNTTINEADDDELIPTAIVIKNIPFAIKKEQLLDVMTKLNLPLPYAFNYHFDNGVFRGLAFANFTSTDETSAVVNQLNGREIGGRKLRVEYKKMLPAQERERIEREKREKRGQLEEQHRSASNASLASLLSAASTTAATKNLSVAGTNPSHTTERMFLNLPFNNSSFNAPPVEINFNDLEVLELYTQLVLYRDDITKSTFELAISPANLNISQRKIISILCNYLNLLELFDNGLIIIRRKPGYIAQCITQQSIIPNSQQVSGPTHPQQHQQNQLQQQQQQQHQHQHPSHSSSMMNLHQLGGTLAVPAHPELLRSQSQSALPLPRLRQQTSTPIQQNQQVQHQNQPPQQQQQQHVQPQYNYYNQQSIQSQPHSARPYSQSYNIYQQQQQQQQQQAQQQAQQQQQQQLQYQQGHQSQVSTPTLNSSSAAALLRSSSSRSFVDVRSTPPTSSFAQQQQQQQQQQQQPPLTSSIHDSPTPHHHLPLQQQQQQQNHYYSNNNQGFGSQPQTPLTNTADVNSRFQPFGQHSHLTSSFTSLSQTLPSTTTTTTNIDDFNNSIVDGNSISSKLNALGLGLGGGGGGGGNTNNTLTGNDNVTTTTTTTTNSTSGFDNSSTSGSGIWGPK
Protein: Defensin-like peptide 2/4 (DLP-2/DLP-4) (Ornithorhynchus venom defensin-like peptide B) (OvDLP-B) (P82140)
Organism: Ornithorhynchus anatinus (Duckbill platypus)
Function: Does not show antimicrobial, myotoxic, hemolytic and cell-promoting activities.
Subcellular location: Secreted {ECO:0000269|PubMed:10417345}.
Interaction partners:
Sequence:
MRLAYLLLLLVAVLFQAGGGSAKPIMFFEMQACWSHSGVCRDKSERNCKPMAWTYCENRNQKCCEY
Protein: Debris buster, isoform D (IP12256p) (A8JNI3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MGLEKHYLRYGRTARDHLLDWATCGRGRRQQQQQQQQQTHAQPSQGSTATGRRSRPHVTHRGTPLSMLISNGVRISNNRLAVIIIGIITLILGIILSSMPWLDYFILKNLRLWNDTLSYHYWQRPGVIRLTKLYIYNVTNPDGFLRGEKPHLQEVGPFVYREDMQKVNVKFHENNYTVSYQHKKILQFVPELSIDKDTPITTPNIPLLTLTSLSPKLGYLLSKTISVVVTAAQFKPFINVTAEQLAFGYDDALVSLAHRFYPKHMRPMERMGLLLGRNGTLTEVSSVKTGMDSMDQFGYIDQLNGLDHLPHWSEPPCTSIAGSEGSFFPPRELTKSEVVHIYDKDLCRIIPLKYVESLEKDGIAADLFRLPNNSYGDSAHNPENKCYDTSEYEPIQGLQNISPCQYGAPVYISNPHFFESHPDLLNSVEGLKPEREKHETYFKIQPKLGVPLEGKVRIQLNLKVTRAKDVYPVRDFRDFVFPVMWLEEGISELTPAIKRWIYLGTVIAPSAVPIGSYLMILGGAFAIIFSFVRAYQNFMFAQDPTLEILEMGRRSLRRGSSFIAHQQHRLLVHHRDSYSLLRHGPMATCLGEGNREEDAQPIIDVSLSGGISQES
Protein: HNF1 homeobox B (A0A087WXS2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVSKLTSLQQELLSALLSSGVTKEVLVQALEELLPSPNFGVKLETLPLSPGSGAEPDTKPVFHTLTNGHAKGRLSGDEGSEDGDDYDTPPILKELQALNTEEAAEQRAEVDRMLSEDPWRAAKMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFSQQSHGPGQSDDACSEPTNKKMRRNRFKWGPASQRLRSAKEPQQEREALVEECNRQNVCSEGCPPPKPTAWAPTWSLRSVSTTGLQTAGRRRHSGKSWPWTPIAPTRLTA
Protein: UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 (BGnT-7) (Beta-1,3-Gn-T7) (Beta-1,3-N-acetylglucosaminyltransferase 7) (Beta3Gn-T7) (EC 2.4.1.-) (Q8K0J2)
Organism: Mus musculus (Mouse)
Function: N-acetyl glucosamine (GlcNAc) transferase that catalyzes the transfer of GlcNAc via a beta1->3 linkage from UDP-GlcNAc to the non-reducing terminal galactose (Gal) in the linearly growing chain of N- and O-linked keratan sulfate proteoglycans. Cooperates with B4GALT4 galactosyltransferase and CHST6 and CHST1 sulfotransferases to construct and elongate mono- and disulfated disaccharide units [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer (By similarity). Involved in biosynthesis of N-linked keratan sulfate proteoglycans in cornea, with an impact on proteoglycan fibril organization and corneal transparency. May play a role in the maintenance of tissue architecture by suppressing cellular motility and invasion.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Keratocan
Sequence:
MSLWKKTLYKSVCLALALLVAVTVFQRSVTPGQFLQDPLPPTPGPAKTGNLVNPNSFWKSSKDVAAPTPTVPRGPQVWDVITTNCSININLTHQPWFQSLEPHFRQFLAYRHCRYFPMLLNHPEKCAGDVYMLVVVKSVITQHDRREVIRQTWGHEWESAGLGRGAVRTLFLLGTASKQEERTHYQQLLAYEDRLYADILQWDFLDSFFNLTLKEIHFLKWLDIYCPNVPFVFKGDDDVFVNPTNLLEFLSDRQPQENLFVGDVLKHARPIRKKDNKYYIPAVMYGKATYPPYAGGGGFLMSGSLARQLHHACDTLELFPIDDVFLGMCLEVLGVKPTGHEGFKTFGISRVRSSRMNKEPCFYRAMLVVHKLLPAELLAMWDLVHSNLTCSVKFQVL
Protein: UDP-glycosyltransferase 91C1 (EC 2.4.1.-) (Q9LTA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cytochrome P450 71B19
- NAD
- NAD
- Cytochrome P450, family 706, subfamily A, polypeptide 7
- Cytochrome P450, family 705, subfamily A, polypeptide 9
- Aldo-keto reductase family 4 member C11
- Cytochrome P450 76C4
Sequence:
MVDKREEVMHVAMFPWLAMGHLLPFLRLSKLLAQKGHKISFISTPRNIERLPKLQSNLASSITFVSFPLPPISGLPPSSESSMDVPYNKQQSLKAAFDLLQPPLKEFLRRSSPDWIIYDYASHWLPSIAAELGISKAFFSLFNAATLCFMGPSSSLIEEIRSTPEDFTVVPPWVPFKSNIVFRYHEVTRYVEKTEEDVTGVSDSVRFGYSIDESDAVFVRSCPEFEPEWFGLLKDLYRKPVFPIGFLPPVIEDDDAVDTTWVRIKKWLDKQRLNSVVYVSLGTEASLRHEEVTELALGLEKSETPFFWVLRNEPKIPDGFKTRVKGRGMVHVGWVPQVKILSHESVGGFLTHCGWNSVVEGLGFGKVPIFFPVLNEQGLNTRLLHGKGLGVEVSRDERDGSFDSDSVADSIRLVMIDDAGEEIRAKAKVMKDLFGNMDENIRYVDELVRFMRSKGSSSSS
Protein: Protein YciI (P0AB55)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Voltage-gated potassium channel Kch
- Probable fimbrial chaperone protein ElfD
Sequence:
MLYVIYAQDKADSLEKRLSVRPAHLARLQLLHDEGRLLTAGPMPAVDSNDPGAAGFTGSTVIAEFESLEAAQAWADADPYVAAGVYEHVSVKPFKKVF
Protein: Putative melanocortin 2 receptor (A7Y4C2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MNDVSALPSNHTDCQVVKVPHLVFLVLGMVSLSENLLVVVAVVRNKNLHSPMYMFICSLATFNTISSLSKTWETLMMEFSDVGQLDSRGDSVRRVDDIIDALLCMSFIGCICSFLAIAVDRYVTIFHALRYHNIMTTRRAAAALAGIWALCGVAGAVMVAFCDATVIKIFFIVLFLISLLLILFLYVHMFLLARSHARKIAALPGSAMPHRSLRGALTLTMLFGVFVVCWAPFFLHLLLLMVCVENPYCECYRSLFQLNLVLLMSHAVVDPAIYAFRSAELRNTFRKMLFCSDSPLCYKVKALFH
Protein: Transcription factor ILI4 (OsILI4) (Basic helix-loop-helix protein 172) (OsbHLH172) (Protein BRASSINOSTEROID UP-REGULATED 1) (OsBU1) (Protein INCREASED LEAF INCLINATION 4) (bHLH transcription factor bHLH172) (Q0DDF6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Atypical and probable non DNA-binding bHLH transcription factor that acts as a positive regulator of brassinosteroid (BR) response. Controls lamina inclination by participating in two BR signaling pathways involving BRI1 and RGA1. Involved in the RLI1-dependent modulation of leaf inclination by promoting lamina joint cell elongation, especially in response to phosphate (Pi) availability.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:19648232}.
Interaction partners:
Sequence:
MSSRRSSRSSVSEEEINELISKLQSLLPSSRRRGANQASTTKLLKETCSYIKSLHREVDDLSDRLSDLMAGMDHNSPGAEIIRSLLR
Protein: Dehydration-induced protein RD22-like protein (Q8VWQ1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MKVLSPILACLALAVVVSHAALSPEQYWSYKLPNTPMPKAVKEILHPELMEEKSTSVNVGGGGVNVNTGKGKPGGDTHVNVGGKGVGVNTGKPGGGTHVNVGDPFNYLYAASETQIHEDPNVALFFLEKDMHPGATMSLHFTENTEKSAFLPYQTAQKIPFSSDKLPEIFNKFSVKPGSLKAEMMKNTIKECEQPAIEGEEKYCATSLESMIDYSISKLGKVDQAVSTEVEKQTPMQKYTIAAGVQKMTDDKAVVCHKQNYAYAVFYCHKSETTRAYMVPLEGADGTKAKAVAVCHTDTSAWNPKHLAFQVLKVEPGTIPVCHFLPRDHIVWVPK
Protein: FI04457p (GRIP and coiled-coil domain containing 185 kDa) (Q9VGE4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Syntaxin 16
- Ras-related protein Rab6
- GRIP and coiled-coil domain containing 88 kDa
- Ran GTPase-activating protein
- ADP-ribosylation factor-like protein 1
- Probable nucleoporin Nup54
- Ras-related protein Rab-2
- LD27967p
- GTP-binding nuclear protein Ran-like
- GTP-binding nuclear protein Ran
Sequence:
MEAASPRETQKNPNPIEALSKDEIISKYKGLLNIAKKAKQAKDELTEENHRLKDALKRAAEKQSSLPAMQEMVQDFTDKNLILTEEVNNLKRKTKEDADRLTQFEIENESLKRQLGRLSDENDALLANVDRMEKAMQQVNALGNEQRKNLELLEVDIAKIKEAEAENASLRQQVATMEEESSVLQQKYQNIKELNSEQRKKFNSLKDRFIDVHRKLKNLKECKCVLLETQHEYAASVSKWQVEIIKASQLLCAKMASLQAENEKLKLNNGKSDNNPQTIDTGIDRKRLLQRVQEMDRLAKIVKQKQKNQRSNLNVEYLLKKITALEELAVIIKQQHRIDKEQLISVTKEQENTKNHARNLNVSLFQTKLDQMQNLVKVIAKERDNQQRKLQELEAICIELRQHNEDLLTRYHLKEQEHGELLTEMRELNEALKGRGDAISRLQEQHEAEVKRQRDLEAQLSNSQQAAQEKLQKIKQLQSRVEELEQANADAQSDVLSTSTISRAEELSRLRELDEGYEEKYHKLRAIAAKLKKKLQEQTQQLNEMEQSGALKEELEAIKLAQAQLQQDLNAARAENQKLKSKEKVKHSSVLNLEIEAAEKSLSEVSAKLTAKSSELEAVKESLASKENTIVQLRKEIAILEEAKNGEAAHSLELKEQIDRMQVQVKDAVHSKQQALTQNKDLEHGVEQAKLEAEQLRLQLSESAQQYESKLNTATQQLLSQTQELEMHLAEQKRLETALRNAERALEDLRVEYTEYKLKAQSVLRKNQNKGSNREQELEEELVALRESERNLRASNDGRAARLAQLDSQIEELRQDNTDLQKRSKELVSLVDELRQQNDLLSLENQRQLQFQHDLMQQHRQQVDELDAGHQLQLTQVQEQLEEAQKMQANVSQHTTASAASVDTSPEQAKIDYLLMDHETGLDGHAGDVSLAQLAAQRKISTASRRSHDFMPLDELLNTSMNQITSDTVTTISNFGRSVSQQEDEEAEMAARGDFSVQSAQLQATKERLSIQESRVKHLTALLAENEQDLAKLTQMNDMLKEELRRQERSEEREQHMHNSEYLKNVFLKFLTLNNVDERQRLVPVLNTILRLSRNEMEMLNCVAKGQKVSADGSSRSWTGFLTAWSGGGSPNNNN
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (F6SXL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGGRRPYDVFFSKVMAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCH
Protein: Olfactory receptor 51B5 (Odorant receptor HOR5'beta5) (Olfactory receptor OR11-37) (Q9H339)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MSSSGSSHPFLLTGFPGLEEAHHWISVFFLFMYISILFGNGTLLLLIKEDHNLHEPMYFFLAMLAATDLGLALTTMPTVLGVLWLDHREIGSAACFSQAYFIHSLSFLESGILLAMAYDRFIAICNPLRYTSVLTNTRVVKIGLGVLMRGFVSVVPPIRPLYFFLYCHSHVLSHAFCLHQDVIKLACADTTFNRLYPAVLVVFIFVLDYLIIFISYVLILKTVLSIASREERAKALITCVSHICCVLVFYVTVIGLSLIHRFGKQVPHIVHLIMSYAYFLFPPLMNPITYSVKTKQIQNAILHLFTTHRIGT
Protein: General transcription factor IIH subunit 5 (General transcription factor IIH polypeptide 5) (TFB5 ortholog) (TFIIH basal transcription factor complex TTD-A subunit) (TFIIH subunit p8) (Q8K2X8)
Organism: Mus musculus (Mouse)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell.
Subcellular location: Nucleus {ECO:0000269|PubMed:28888655}. Cytoplasm {ECO:0000269|PubMed:28888655}.
Interaction partners:
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 4
- General transcription factor IIH subunit 1
- General transcription factor IIH subunit 3
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIH subunit 2
- Cyclin-dependent kinase 7
- Cyclin-H
- General transcription factor IIE subunit 2
- General transcription factor IIF subunit 1
Sequence:
MVNVLKGVLIECDPAMKQFLLYLDEANALGKKFIIQDIDDTHVFVIAELVNVLQERVGELMDQNAFSLTQK