wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase MPK-2) (p50CSK) (P41241)
Organism: Mus musculus (Mouse)
Function: Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16166631}. Cell membrane {ECO:0000269|PubMed:16166631}. Note=Mainly cytoplasmic, also present in lipid rafts.
Interaction partners:
- Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
- Tyrosine-protein phosphatase non-receptor type 22
- Proto-oncogene tyrosine-protein kinase Src
- Paxillin
- T-cell surface glycoprotein CD3 epsilon chain
- Docking protein 3
- Caveolin-1
- SHC-transforming protein 1
- Proto-oncogene tyrosine-protein kinase LCK
- Docking protein 1
Sequence:
MSAIQAAWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCEGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTTDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYEVMKNCWHLDAATRPTFLQLREQLEHIKTHELHL
Protein: Suppressor of cytokine signaling at 16D, isoform B (M9PHY7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Elongin-B
- Cullin-5
- Elongin-C
- Cullin-2
- Protein gustavus
- S-phase kinase-associated protein 2
- Cullin homolog 1
- GEO01111p1
- Cullin 3, isoform F
- Ubiquitin-like protein NEDD8
Sequence:
MDSSIKLKDSNSNCSSNSNGNVGGGGVAGGGGSGSGGVCVSSICSSDSFSIMPPPHHELVSANSIELNAAASLSDDSGVPLTTNSSISSGDSYRLGMCKFEIEMVESDGEVSQFDSLDNCSEGGMSAENFNTLKKGPLAPIDPPPEFQDSPQTTLVRSISKNIVNSLRRWTSSQSSFEHLKDDATTMVSGLATAVLPEEPHPPSQELVLLLAKTECKLDALDGQALGQMSLKESYAINKHLYSSDSILNSHTDNIYDEPNNIVSSSLGNSVDLLDEEQSDASSCSPLPSPPPPVSIVKIKQTLCPYYQDHTRYFKAIPTEQDNIASAKAAAAQQRFNSAGLSEIHDYDLYYGARRQPVDNSSLQRRQASLYSPLGHTSHCHYHHSHGHGHGSHHHHHHHQPGYGYSHGQRPNSRNSLNSRLSSSHNSLNVSSANKPDDSIFITQAMSHDALFTREISDFYNVPIDSDIYAFPVDMIEQQQQQQLLVEEQQQQKPAAPTYHKASRRNKRNKRKQRYAGSGTGAGTETSDGDGEKSKHGKYRTPVGVGMGQVSESEPLHMTLDEVKQFYHTLYSDAGKPTPKPMVKSSNETIWSVSTNTTTTTARTRSSVGTTRGGGGPPGAGNGAGGASSDGGVGGGSAGGGGGKYLSKQNKHNLDNDKLNNNNNNNNNHQPSQQQLEKPPTEHHNQHQPPNNKHVLHSEKKSQFTLNLKQRFCSIFRFRRSNHSRCRGSGNNQTGTFASANANAAATAPLIPPIAVITSAPGAAGQTQLASELNGTLITAEADEPNADLRKKFQSRALPPLPKKALPFTAAAYAIEAVKSEPEEVKTNAIQEPRALQFTSSIEKVKDYGWYWGPLSSEAAEKVLSSEPDGSFIVRDSSDDHYIFSLSFKLNNCVRHVRIEQDQGTFSFGSYAKFKSQTITEFIEKAVEHSRSGRYLFFLHRRPEHGPMRVQLTNPVSRFKHVQSLQHMCRFVILKAVIRKDLIQTLPLPRRLLDYLNYKHCYSEQVESDSSHSQISGDGTM
Protein: Kinesin-related protein 5 (Kinesin family member 5) (Kinesin-1) (Q8T135)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end (By similarity). May connect microtubules to actin filaments. Associates with actin-based structures in cells and is likely involved in the organization of actin cytoskeletons in such structures.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14623897}.
Interaction partners:
- Lis-interacting protein
- Tubulin beta chain
- Probable mitochondrial Rho GTPase gemA
Sequence:
MATSCNIRVMCRFRPLNEREKALKENQTCVTFPDETQVIVSGQPFTFDRVFTPESTQKEVFESVKDTIHDVLLGYNGTLLAYGQTGSGKTFTMGSAAAESDFENVEQLGIIPRGNHLIFNTIAEESDGNAEFTIKCSYLEIYMENIQDLLNPKNNKQLKIRESKSQGIYVEGLTEEYVASEEDIMELIQVGESSRSVAKTNMNQRSSRSHSILIIAIEQKSSDGSKKRGKLNLVDLAGSEKVSKTGAEGIVLEQAKKINQSLSLLGNCIHALTDSKREHIPFRDSKLTRLLQDSLGGNTKTTLLVTASPHFNNVDETISTLKFGARAKSIKNNVKVNQEKSAAELQIIVNALTKELSILKVYSISLENLVNYFKSSSYQPGNPIPKELEPNKQNLLLLQQQSNSSSGGGGSGSSGGSSNGSLMMKPRSTTPTPPSINRPHSSASTHRHSIAITGTHSKEGSGGGLTSSISSSSISSMSSLSSSIDNDYNGSSLDDSNGSNGLFNPLAIVEMSIEMEKMKEDTQLLIEKFKDEISEITIQYQSTQEELNQCRQQLDQIKEQLEQQRSQFIKEQSLLKESERNATLDSTSKDLKIQSLISKIEDLRLLASQVIQYLERKRLSDDFDIGIFMGSQDGANGDSANMFSLISNSIDQGTYEDDVNIEDIIRYLSEEEVLTMQVKLQLQNKVHQLEQKIQQLVSDLNTTEINYNQSILQCQKFESENSLIKRKFKSMFSSSNNNNNNNNSPPSSPSSKLLIQSSNNNNNFDSNLNSSSLSSSLPSSNGIEQDQQVDHQVDHQVENDHLVNDEDNKLLDENSKLKENELKLLLEIKNLKLQSEKSNDETLKWKDELSIKSALYQNQILNLQNENQSLSNKLNVEKQQKQSSQSQQIEFATKLNDLIKSSEDDKELYRNEKNQMELEIASLKASLDEMDLKNKELQDQLISTQRLIGARRVVKIVRGGADSMKTALATKEVFGQFTLRKTENSKTLFQ
Protein: Transcription factor AP-2 gamma (Q5PQZ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- WW domain-containing oxidoreductase
- Cbp/p300-interacting transactivator, with Glu/Asp-rich carboxy-terminal domain, 2.
- PR domain zinc finger protein 14 isoform X1
Sequence:
MLWKLADNVKYEDDCEQERHDVSSNGNPRLPHIPAVSQHLYSPPPSLSHPASSDFQPPYFPPPYQPIPYTQPSDPYSHLGDPFNINPIHQSANSNQQQSWPGRQGQEGIGGHGRSGLGSPILGLEGGSSGMRRDGFRRPELLPPHIHGIDSLGDNIGLHDIGHGMEDVQHDGDHSIIIPDHTVIKKGPVSLPKGNAFGIPFQKESLLGMVSNPTEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTALVEGEAVHLARDFGYVCETEFPAKAIAEYLGRPHVERNEINSRKTMLLAAKQICKEFTDLLTQDRSPLGNSRPAPILEPGIQSCLTHFSLITHGFGSPAICAAMTSLQNYLNEALKQVDKMYVSSTGDSSQASSDGTNKADKMDKHRK
Protein: Ribosomal-protein-serine acetyltransferase (EC 2.3.1.-) (Acetylating enzyme for N-terminus of ribosomal protein L7/L12) (P13857)
Organism: Escherichia coli (strain K12)
Function: This enzyme acetylates the N-terminal serine of ribosomal protein L7/L12.
Subcellular location: Cytoplasm.
Interaction partners:
- [Ribosomal protein uS5]-alanine N-acetyltransferase
- [Ribosomal protein bS18]-alanine N-acetyltransferase
- L-amino acid N-acetyltransferase AaaT
Sequence:
MTETIKVSESLELHAVAENHVKPLYQLICKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGVISFNRIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGFILEGCLKQAEFLNDAYDDVNLYARIIDSQ
Protein: Gamma-secretase subunit PEN-2 (Liver regeneration-related protein LRRGT00140) (Presenilin enhancer protein 2) (Q6QI68)
Organism: Rattus norvegicus (Rat)
Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Cell membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Note=Predominantly located in the endoplasmic reticulum and in the cis-Golgi. {ECO:0000250|UniProtKB:Q9NZ42}.
Interaction partners:
- Presenilin-2
- Anterior pharynx defective 1a homolog
- Nicastrin
- Gamma-secretase subunit APH-1
- Presenilin-1
- Transmembrane emp24 domain-containing protein 10
- Neurogenic locus notch homolog protein 1
- Amyloid-beta precursor protein
- Tumor necrosis factor
- Gamma-secretase activating protein
Sequence:
MNLERVSNEEKLNLCRKYYLGGFAFLPFLWLVNIFWFFKEAFFAPAYTEQSQIKGYVWRSAVGFLFWVIVLTTWITIFQIYRPRWGALGDYLSFTIPLGTP
Protein: E93 (Q24079)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHISSYEISLERVAEECMGRRQWKHYQDKLTCSHLNIEEQQPIAIAGSEDEPSQYNHSSKEISQSNPNHCKTENHRLEQQHNGSQLLEEEDSENNQTSHDSSRTPTPGATSTPSPPPEPIDWRPSAKCNFCVNGRLLTVNAQGKLVAESAATATSSSTSNSHIHQHDSDSNSSASLPHHISSSSSSNNNSSGNRARHIAAASARATPAAATPANSLELYKLLTQRAAKMTSMDSMAAQLAQFSLLADFNLINSLASQQQQQQQQQIASAVTPTTSEVSAAAISPALKDTPSPSVDAPLDLSSKPSPNSSISGDVKSVRACATPTPSGRRAYSEEDLSRALQDVVANKLDARKSASQHHEQRSILDNRLFKMKHHDQEQDHDGDELEDSNDDAEAEVDSNASTPVYPAEFARAQLRKLSHLSEHNGSDLGEDVDRGSPKMGRHPACGNASANQGAPASIPLDANVLLHTLMLAAGIGAMPKLDETQTVGDFIKGLLVANSGGIMNEGLLNLLSASQENSNGNASLLLQQQQHQQHHQQHHQQQQQQQHVAAYRHRLPKSETPETNSSLDPNDASEDPILKIPSFKVSGPASSSSLSPGGLVGGHHHPLNNNNSLSISNNSNHSSNSHRNGSNRSPHSASPMLAAAVAQGGYSAGNSLLTSSSSSIQKMMASNIQRQINEQSGQESLRNGNVSDCSSNNGGSSSLGYKKPSISVAKIIGGTDTSRFGASPNLLSQQHHSAHHLTHQQQQQQLSAQEALGKGTRPKRGKYRNYDRDSLWRRSRRCRELKCRFIERVATMRTAFHTGVQGQGTSPDATAQARAQAAARSRRPDRTSQQAAAGQTEGGTTWWLQAEQCPQEPKQSGGCGGGGGSSSSGRCHAQRPETAPFRGGSTGVILSAEHVLAPDERHECLRPGLQSHHGGDAEFPGLQSPRLMKSAQDMVGERLRWHHQEDAAGEQGNGSAAGNGSNGSNGNGHGHGHGHGHALLDQLLVKKTPLPFTNHRNNDYVVTCSSASGESVKRSGSPMGNYADIKREALSADSGGSSDEEHSASHINNNNSDLAHNKNKSGGGGGGGNGQTNGNGRSSRMTSRDDSETDASSFKSGENGGQQNHKMMDLNGGRAAAVTSSANRRRPPDITVLDTTPRPYCTRSWSRSRPSKWTRRFSYWSSRWTRIQRSPWHRWSPTTTVSWRREGEHQIKPRFLVVPYKSLNRIIYIYIYIYILL
Protein: Trehalose-6-phosphate synthase (EC 2.4.1.15) (UDP-glucose-glucosephosphate glucosyltransferase) (Q875L7)
Organism: Pyricularia grisea (Crabgrass-specific blast fungus) (Magnaporthe grisea)
Interaction partners:
Sequence:
MGSVEDETALPSGGRLLLISNRLPITIKRSDDGQYSFSMSSGGLVTGLSGLAKTTSFQWYGWPGLEVPDAEAGPVVQRLKNEYGAHPVFVDDELADRHYNGFANSILWPLFHYHPGEITFDESAWSAYKEVNRLFAQTVVKDVQDGDMIWVHDYHLMLLPEMLREEIGDSKKNVKIGFFLHTPFPSSEIYRILPVRQALLQGVLHCDLLGFHTYDYARHFLSSCSRILSAPTTPNGVQFAGRFVTVGAFPIGIDPEKFVEGLQKPKVQQRIAALTRKFEGVKLIVGVDRLDYIKGVPQKLHALEVFLTEHPEWIGKIVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGKFGTIEFMPIHFLHQSVSFDELAALYAVSDVCLVSSTRDGMNLVSYEYIATQRDRHGVMILSEFTGAAQSLSGSLIVNPWNTEELANAIHDAVTMGPEQREANFKKLERYVFKYTSAWWGSSFVAELNRLAAGIEGADAEGSKTKIAIRGVGDAVADGAGKVADAVSSVLPGGDNKTEGN
Protein: Short-wave-sensitive opsin 1 (Blue cone photoreceptor pigment) (Blue-sensitive opsin) (BOP) (P03999)
Organism: Homo sapiens (Human)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (Probable). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:2937147, ECO:0000269|PubMed:31380578, ECO:0000269|PubMed:31730232}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:30168605}.
Interaction partners:
- Arrestin-C
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Retinol-binding protein 3
- Guanine nucleotide-binding protein G
- Rhodopsin
- Guanine nucleotide-binding protein G
- Zinc finger protein 513
Sequence:
MSEEEFYLFKNISSVGPWDGPQYHIAPVWAFYLQAAFMGTVFLIGFPLNAMVLVATLRYKKLRQPLNYILVNVSFGGFLLCIFSVFPVFVASCNGYFVFGRHVCALEGFLGTVAGLVTGWSLAFLAFERYIVICKPFGNFRFSSKHALTVVLATWTIGIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSESYTWFLFIFCFIVPLSLICFSYTQLLRALKAVAAQQQESATTQKAEREVSRMVVVMVGSFCVCYVPYAAFAMYMVNNRNHGLDLRLVTIPSFFSKSACIYNPIIYCFMNKQFQACIMKMVCGKAMTDESDTCSSQKTEVSTVSSTQVGPN
Protein: Calcium uniporter protein, mitochondrial (Q7S4I4)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:29954988}; Multi-pass membrane protein {ECO:0000269|PubMed:29954988}.
Interaction partners:
- FYVE-type domain-containing protein
- Prohibitin
- Uncharacterized protein
- Uncharacterized protein
- Potassium ion channel Yvc1
Sequence:
MNCVRMRLQCRLMPSSNTLARWCLESPQKNLTLHRPRISNVALRQASTSVSPKTRETEAEAKAKKLDQKRLDEHEEEVRAREQQVRRPWHREGADKPPVEGNADPIAKGKLLTTPTRLLKLILPLPLRVEKDQKNNGRNNEYGRSISLNSDIQPLALLIHPQQPLSYVERLIQAELPPVVENGQEKIPNVYFRAEDSEQGDQKPTSRAEARSKDDGGEPSEYNTNLSHVASYSGLGHRGPKRSSQDKRWVRWSSSTEMGDFIRDAARGREFAIEIEGYNIEMRVSVPSFGDRTYYMRQRLRKMSSEIDGLAKIKHECDLLAHRSAHRLAKGGFGLLAGWWGVVYYVTFHTEFGWDLVEPVTYLAGLTTIMGGYLWFLYINKDLSYKAAMNVTVSRRQHALYEMKGFDIERWEQLVQDANALRREIRVIAVEYDVDWDETRDVGEDVKDVLDEERSRRDDEHRSIEKEKDEKFTEDEKRKRKKDKESKETSGDS
Protein: Protein RecA (Recombinase A) (Q59180)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- DNA polymerase I
- DNA 3'-5' helicase
- RecBCD enzyme subunit RecB
- DNA mismatch repair protein MutL
- RecBCD enzyme subunit RecD
- Transcription elongation factor GreA
- Holliday junction branch migration complex subunit RuvB
- DNA 3'-5' helicase
- DNA topoisomerase 1
- Beta sliding clamp
Sequence:
MSKLKEKREKAVVGIERASKEEAIELARVQIEKAFGKGSLIKMGESPVGQGIKSMSSGSIVLDEALGIGGYPRGRIIEIFGPESSGKTTLTLQAIAEVQKEGGIAAFIDAEHALDPVYAKALGVNVAELWLSQPDTGEQALEIAEHLIRSGGVDLIVVDSVAALTPKLEIDGEMGDSQIGLQARLMSKALRKITGILSKSNTCIMFINQIRMRIGVMFGNPETTTGGNALKFYSSLRLEVRKIEQVTRSGSSDDVIGNKIRVKIVKNKVAPPFRKVELIIYFGKGISREAGILDAAIKHNLIQKTGSWYSLGDNKLGQGRESVIEYLSKEVELANNLDKRLRKIIFNNFDQENDNFIEFKEDESE
Protein: Small ribosomal subunit protein uS2c (30S ribosomal protein S2, chloroplastic) (P0C480)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MTRRYWNINLKEMIEAGVHFGHGIKKWNPKMAPYISAKRKGTHITNLARTTRFLSEACDLVFDAASQGKSFLIVGTKKRAADLVASAAIRARCHYVNKKWFSGMLTNWSITKTRLSQFRDLRAEEKMEKFHHLPKRDVAILKRKLSTLQRYLGGIKYMTRLPDIVIVLDQQKEYIALRECAILGIPTISLADTNCDPDLANISIPANDDTMTSIRLILNKLVFAICEGRSLYIRNH
Protein: Staufen double-stranded RNA binding protein 1 (Q5JW28)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKLGKKPMYKPVDPYSRMQSTYNYNMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKTRQAAKHDAAAKALRILQNEPLPERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFESFPLKQVARESGPPHMKNFVTKVSVGEFVGEGEGKSKKISKKNAAIAVLEELKKLPPLPAVERVKPRIKKKTKPIVK
Protein: Protein jagged-2 (Jagged2) (hJ2) (Q9Y219)
Organism: Homo sapiens (Human)
Function: Putative Notch ligand involved in the mediation of Notch signaling. Involved in limb development (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Protein jagged-1
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Transcription elongation factor SPT6
- Recombining binding protein suppressor of hairless
- Serrate RNA effector molecule homolog
- E3 ubiquitin-protein ligase MIB2
Sequence:
MRAQGRGRLPRRLLLLLALWVQAARPMGYFELQLSALRNVNGELLSGACCDGDGRTTRAGGCGHDECDTYVRVCLKEYQAKVTPTGPCSYGHGATPVLGGNSFYLPPAGAAGDRARARARAGGDQDPGLVVIPFQFAWPRSFTLIVEAWDWDNDTTPNEELLIERVSHAGMINPEDRWKSLHFSGHVAHLELQIRVRCDENYYSATCNKFCRPRNDFFGHYTCDQYGNKACMDGWMGKECKEAVCKQGCNLLHGGCTVPGECRCSYGWQGRFCDECVPYPGCVHGSCVEPWQCNCETNWGGLLCDKDLNYCGSHHPCTNGGTCINAEPDQYRCTCPDGYSGRNCEKAEHACTSNPCANGGSCHEVPSGFECHCPSGWSGPTCALDIDECASNPCAAGGTCVDQVDGFECICPEQWVGATCQLDANECEGKPCLNAFSCKNLIGGYYCDCIPGWKGINCHINVNDCRGQCQHGGTCKDLVNGYQCVCPRGFGGRHCELERDECASSPCHSGGLCEDLADGFHCHCPQGFSGPLCEVDVDLCEPSPCRNGARCYNLEGDYYCACPDDFGGKNCSVPREPCPGGACRVIDGCGSDAGPGMPGTAASGVCGPHGRCVSQPGGNFSCICDSGFTGTYCHENIDDCLGQPCRNGGTCIDEVDAFRCFCPSGWEGELCDTNPNDCLPDPCHSRGRCYDLVNDFYCACDDGWKGKTCHSREFQCDAYTCSNGGTCYDSGDTFRCACPPGWKGSTCAVAKNSSCLPNPCVNGGTCVGSGASFSCICRDGWEGRTCTHNTNDCNPLPCYNGGICVDGVNWFRCECAPGFAGPDCRINIDECQSSPCAYGATCVDEINGYRCSCPPGRAGPRCQEVIGFGRSCWSRGTPFPHGSSWVEDCNSCRCLDGRRDCSKVWCGWKPCLLAGQPEALSAQCPLGQRCLEKAPGQCLRPPCEAWGECGAEEPPSTPCLPRSGHLDNNCARLTLHFNRDHVPQGTTVGAICSGIRSLPATRAVARDRLLVLLCDRASSGASAVEVAVSFSPARDLPDSSLIQGAAHAIVAAITQRGNSSLLLAVTEVKVETVVTGGSSTGLLVPVLCGAFSVLWLACVVLCVWWTRKRRKERERSRLPREESANNQWAPLNPIRNPIERPGGHKDVLYQCKNFTPPPRRADEALPGPAGHAAVREDEEDEDLGRGEEDSLEAEKFLSHKFTKDPGRSPGRPAHWASGPKVDNRAVRSINEARYAGKE
Protein: G2/mitotic-specific cyclin CLB2 (Q5ALY0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: 2/mitotic-specific cyclin essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. Degradation is necessary for the cell to exit from mitosis. Plays a role in morphogenesis by negatively regulating polarized growth. Through binding to CDC28 regulates cytokinesis, partly by phosphorylation of the actomyosin ring component IQG1. Also involved in the phosphorylation of CDC6 and CDC54.
Interaction partners:
- Cyclin-dependent kinase 1
- Mitosis inhibitor protein kinase SWE1
- Cdh1p
- Anaphase promoting complex subunit
- Anaphase promoting complex subunit
- M-phase inducer phosphatase
- Anaphase promoting complex subunit
- Serine/threonine-protein kinase
- Ubiquitin-protein transferase activating protein
- Nucleoporin NSP1
Sequence:
MPQVTKTNNENEFRLTRSKVQHQESISTIKNTTISNSQHKQQTQQQISSPPQVSVTSSEGVSHVNTRQYLGDVSNQYITNAKPTNKRKPLGGDNAPLQKQQHRPSRPIPIASDNNNNGSTSSSSNSSNNNNNDANRLASLAVPSRLPQKRQATESSTNLVEKLRVPQPEVGERSQSYHKKSRLIDYEWQDLDEEDSDDQLMVSEYVNEIFSYYYELETRMLPDPQYLFKQTLLKPRMRSILVDWLVEMHLKFKLLPESLFLAVNVMDRFMSVEVVQIDKLQLLATAALFTAAKYEEVFSPSVKNYAYFTDGSYTPEEVVQAEKYMLTILNFDLNYPNPMNFLRRISKADDYDVQSRTLGKYLLEITIVDYKFIGMRPSLCCASAMYLARLILGKLPVWNGNLIHYSGGYRISDMRECIELMFQYLIAPIEHDEFFKKYAMRKFMRASTLCRNWAKKFQASGRDLFDERLSTHRLTLEDDDEEEEIVVAEAEE
Protein: DNA repair protein RAD55 (P38953)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for radiation resistance and meiotic viability and presumably acts in recombination and recombinational DNA repair pathways.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA repair protein RAD51
- DNA repair and recombination protein RAD54
- DNA repair and recombination protein RAD52
- DNA repair protein RAD57
- DNA repair protein RAD59
- ATP-dependent DNA helicase SRS2
- DNA repair and recombination protein RDH54
- ATP-dependent helicase SGS1
- Chromosome segregation in meiosis protein 2
- DNA topoisomerase 3
Sequence:
MSLGIPLSQLIVESPKPLSSGITGLDEILNLGFQARSIYEIFGPPGIGKTNFGIQLVCNSLEGIQQSEINDDKILWIETFQEMPINILRERFQKFKIVEENVKRVRITKFGQLLYFFQNLFKLSQSVRYKLVIIDGFSQLVCDHLCTLSKRGGGMIDKTIHELKCRHLILIFTVMTKYTHSTGSTIIVLNDCMNTAFQSNEFESLEEYYEILDDGSNFFVNSNNERRKNNVHILKSALVANIAMGSKDSTWEVFLRDRIGLFRDWNEQVDETVFVKSKRVKASSSQSNEGCTTIKEMRINKRNFENLRIAIVFNLHGEDRKREGRNLKRSRSSDDRNYIVKFDFDKATGQLRDIIDLKPDTANIASFPTLSTSSSSCSQVFNNIDSNDNPLPNAEGKEEIIYDSEG
Protein: Testis secretory sperm-binding protein Li 224n (A0A140VK97)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF
Protein: Lumican (Keratan sulfate proteoglycan lumican) (KSPG lumican) (P51885)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Fibrillin-1
- Tumor necrosis factor ligand superfamily member 6
- Decorin
- Collagen alpha-2
- SPARC
- E3 ubiquitin-protein ligase Mdm2
- Collagen alpha-1
Sequence:
MNVCAFSLALALVGSVSGQYYDYDIPLFMYGQISPNCAPECNCPHSYPTAMYCDDLKLKSVPMVPPGIKYLYLRNNQIDHIDEKAFENVTDLQWLILDHNLLENSKIKGKVFSKLKQLKKLHINYNNLTESVGPLPKSLQDLQLTNNKISKLGSFDGLVNLTFIYLQHNQLKEDAVSASLKGLKSLEYLDLSFNQMSKLPAGLPTSLLTLYLDNNKISNIPDEYFKRFTGLQYLRLSHNELADSGVPGNSFNISSLLELDLSYNKLKSIPTVNENLENYYLEVNELEKFDVKSFCKILGPLSYSKIKHLRLDGNPLTQSSLPPDMYECLRVANEITVN
Protein: Osiris 6 (Q7KN81)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFFVATACILLLAAGISADPVKAAEEQPGAFAQCLESDSISCLQLTLFRKAKSVFDNPQIELFGGVSLVKSNEGRQGKSLDNSLAVEAAPTVEARTAEMGNYFMDNAKSFFAERSLNFNFANAARSVARAIPDDIKADLRELVVESRTRKKKLLKKFLPILLGVGAKIAVLGVGSIFGLLFLAKKALVVSVIAFFLALAAGASSGLGRIGGSGGGGGLLGGLGGLFGGKNAGGSSAASTGGWSSGGGASSAGWSSGGSSGWDTHGAYSSPVAQTIAYQGYKQARR
Protein: H-2 class II histocompatibility antigen gamma chain (Ia antigen-associated invariant chain) (Ii) (Ii chain) (MHC class II-associated invariant chain) (CD antigen CD74) [Cleaved into: Class-II-associated invariant chain peptide (CLIP)] (P04441)
Organism: Mus musculus (Mouse)
Function: Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to compartments where peptide loading of class II takes place. Enhance also the stimulation of T-cell responses through interaction with CD44.
Subcellular location: [Isoform Long]: Late endosome {ECO:0000269|PubMed:11483509}. Lysosome {ECO:0000269|PubMed:11483509}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04233}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P04233}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04233}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P04233}. Endosome {ECO:0000250|UniProtKB:P04233}. Lysosome {ECO:0000250|UniProtKB:P04233}. Secreted {ECO:0000250|UniProtKB:P04233}. Note=Transits through a number of intracellular compartments in the endocytic pathway. It can either undergo proteolysis or reach the cell membrane. {ECO:0000250|UniProtKB:P04233}.
Interaction partners:
- Macrophage migration inhibitory factor
- H-2 class II histocompatibility antigen, A-B alpha chain
- H-2 class II histocompatibility antigen, A beta chain
- H-2 class II histocompatibility antigen, E-B beta chain
- CD44 antigen
- Ubiquitin-like protein FUBI
- C-X-C chemokine receptor type 4
- C-X-C chemokine receptor type 2
- H2-O alpha
- Class II histocompatibility antigen, M beta 1 chain
Sequence:
MDDQRDLISNHEQLPILGNRPREPERCSRGALYTGVSVLVALLLAGQATTAYFLYQQQGRLDKLTITSQNLQLESLRMKLPKSAKPVSQMRMATPLLMRPMSMDNMLLGPVKNVTKYGNMTQDHVMHLLTRSGPLEYPQLKGTFPENLKHLKNSMDGVNWKIFESWMKQWLLFEMSKNSLEEKKPTEAPPKVLTKCQEEVSHIPAVYPGAFRPKCDENGNYLPLQCHGSTGYCWCVFPNGTEVPHTKSRGRHNCSEPLDMEDLSSGLGVTRQELGQVTL
Protein: GTP 3',8-cyclase 2 (EC 4.1.99.22) (Molybdenum cofactor biosynthesis protein A 2) (P9WJS1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Interaction partners:
- Cyclic pyranopterin monophosphate synthase 2
- Cyclic pyranopterin monophosphate synthase 3
- Cyclic pyranopterin monophosphate synthase 1
- Molybdopterin synthase catalytic subunit 2
- Probable molybdopterin biosynthesis Mog protein
- MoaB/Mog domain-containing protein
- Molybdopterin synthase sulfur carrier subunit
- GTP 3',8-cyclase 1
- Riboflavin biosynthesis protein RibBA
- 3,4-dihydroxy-2-butanone-4-phosphate synthase
Sequence:
MTLTALGMPALRSRTNGIADPRVVPTTGPLVDTFGRVANDLRVSLTDRCNLRCSYCMPERGLRWLPGEQLLRPDELARLIHIAVTRLGVTSVRFTGGEPLLAHHLDEVVAATARLRPRPEISLTTNGVGLARRAGALAEAGLDRVNVSLDSIDRAHFAAITRRDRLAHVLAGLAAAKAAGLTPVKVNAVLDPTTGREDVVDLLRFCLERGYQLRVIEQMPLDAGHSWRRNIALSADDVLAALRPHFRLRPDPAPRGSAPAELWLVDAGPNTPRGRFGVIASVSHAFCSTCDRTRLTADGQIRSCLFSTEETDLRRLLRGGADDDAIEAAWRAAMWSKPAGHGINAPDFIQPDRPMSAIGG