wanglab/gogpt-training-data huggingface dataset:
Protein: Elongation factor P lysine hydroxylase (EF-P lysine hydroxylase) (EC 1.14.13.-) (EF-P post-translational modification enzyme C) (P76938)
Organism: Escherichia coli (strain K12)
Function: Is involved in the final hydroxylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine.
Interaction partners:
- Probable membrane transporter protein YfcA
- L-lysine 2,3-aminomutase
- Elongation factor P--
- Elongation factor P
- Uncharacterized protein YfcL
- Elongation factor P-like protein
- Penicillin-insensitive murein endopeptidase
- Chorismate synthase
- Ribosomal protein uL3 glutamine methyltransferase
Sequence:
MNSTHHYEQLIEIFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCPDGRDAQTQSQFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGDFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQNYYHTPELTAEQFPWPEALN
Protein: Mitogen-activated protein kinase kinase 10 (AtMKK10) (MAP kinase kinase 10) (EC 2.7.12.2) (Q9LQM8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Methyltransferase family protein
- Mitogen-activated protein kinase 17
- 6,7-dimethyl-8-ribityllumazine synthase, chloroplastic
Sequence:
MTLVRERRHQEPLTLSIPPLIYHGTAFSVASSSSSSPETSPIQTLNDLEKLSVLGQGSGGTVYKTRHRRTKTLYALKVLRPNLNTTVTVEADILKRIESSFIIKCYAVFVSLYDLCFVMELMEKGSLHDALLAQQVFSEPMVSSLANRILQGLRYLQKMGIVHGDIKPSNLLINKKGEVKIADFGASRIVAGGDYGSNGTCAYMSPERVDLEKWGFGGEVGFAGDVWSLGVVVLECYIGRYPLTKVGDKPDWATLFCAICCNEKVDIPVSCSLEFRDFVGRCLEKDWRKRDTVEELLRHSFVKNR
Protein: DNA helicase (EC 3.6.4.12) (A0A8I6ACF8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEDDPEEDLSEAETPKLKKKKKPKKPRDPKIPKSKRQKKELGDSSGEGPEFVEEDEEAALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTAKKKKKGEEEVTAVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDPEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESTEGEKEVKPTAPEVTVECAQPPAPAPAPASGPGPTPGPAPAPEDDKAPAEPPEGEEKVEKAEVKERAEEPMETESKGTTEVEKAEEKSAVDLTPIVVEDKGRCYVKYAILSSFLLSNLPLNSSSELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPPPQQVAQQQ
Protein: Cell shape-determining protein MreC (Cell shape protein MreC) (Rod shape-determining protein MreC) (P16926)
Organism: Escherichia coli (strain K12)
Function: Involved in formation and maintenance of cell shape. Responsible for formation of rod shape. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15612918}; Single-pass membrane protein {ECO:0000269|PubMed:15612918}.
Interaction partners:
- Cell shape-determining protein MreB
- Peptidoglycan D,D-transpeptidase MrdA
- Rod shape-determining protein MreD
- Peptidoglycan glycosyltransferase MrdB
- Cytoskeleton protein RodZ
- Penicillin-binding protein 1A
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Peptidoglycan D,D-transpeptidase FtsI
- Probable peptidoglycan glycosyltransferase FtsW
- dTTP/UTP pyrophosphatase
Sequence:
MKPIFSRGPSLQIRLILAVLVALGIIIADSRLGTFSQIRTYMDTAVSPFYFVSNAPRELLDGVSQTLASRDQLELENRALRQELLLKNSELLMLGQYKQENARLRELLGSPLRQDEQKMVTQVISTVNDPYSDQVVIDKGSVNGVYEGQPVISDKGVVGQVVAVAKLTSRVLLICDATHALPIQVLRNDIRVIAAGNGCTDDLQLEHLPANTDIRVGDVLVTSGLGGRFPEGYPVAVVSSVKLDTQRAYTVIQARPTAGLQRLRYLLLLWGADRNGANPMTPEEVHRVANERLMQMMPQVLPSPDAMGPKLPEPATGIAQPTPQQPATGNAATAPAAPTQPAANRSPQRATPPQSGAQPPARAPGGQ
Protein: Carbonic anhydrase 2 (EC 4.2.1.1) (Carbonate dehydratase 2) (P45148)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Interaction partners:
- Formate channel FocA
Sequence:
MDKIKQLFANNYSWAQRMKEENSTYFKELADHQTPHYLWIGCSDSRVPAEKLTNLEPGELFVHRNVANQVIHTDFNCLSVVQYAVDVLKIEHIIICGHTNCGGIHAAMADKDLGLINNWLLHIRDIWFKHGHLLGKLSPEKRADMLTKINVAEQVYNLGRTSIVKSAWERGQKLSLHGWVYDVNDGFLVDQGVMATSRETLEISYRNAIARLSILDEENILKKDHLENT
Protein: Zinc finger protein 624 (Q9P2J8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein TXNRD3NB.
Sequence:
MSLQDSTLSREGKPEGEIMAAVFFSVGRLSPEVTQPDEDLHLQAEETQLVKESVTFKDVAIDFTLEEWRLMDPTQRNLHKDVMLENYRNLVSLGLAVSKPDMISHLENGKGPWVTVREISRIPYPDMEPKPATKKATRTKAISEDLSQEAILEKLTENGLWDSRMEGLWKWNDRILRLQNNQENHLSQRIIPLKKTPTSQRGFRFESILIPEPGIATEELHSRCQTQEENFTENLNLITDTHLGKIICKEMKGSKAIRQTSELTLGKKSNNKEKPYKCSTCEKAFHYRSLLIQHQRTHTKEKPYECNECGKTFSQPSYLSQHKKIHTGEKPYKCNECGKAFIASSSLMVHQRIHTKEKPYQCNVCGKSFSQCARLNQHQRIQTGEKPYKCSECGKAFSDKSKLARHQETHNGEKPYKCDDCGKAFRNKSYLSVHQKTHTEEKPYQCNECGKSFKNTTIFNVHQRIHTGEKPFRCNECGKAYRSNSSLIVHIRTHTGEKPYECNECGKAFNRIANFTEHQRIHTGEKPYKCNECGKAFINYSCLTVHHRMHTGEKPYKCTECGKAFMRSSSLIIHQRIHTEEKPYLCNECGESFRIKSHLTVHQRIHTGEKPYKCTDCERAFTKMVNLKEHQKIHTGVKPYKCYDCGKSFRTKSYLIVHQRTHTGEKPYKCNECEKAFTNTSQLTVHQRRHTGEKPYKCNECGKVFTSNSGFNTHQRTHTGEKPFKCNDCGKAFSQMVHVTEHQKIHSGEKPYKCDVCGKAFRRGSYLTVHWRTHTGEKPYTCKECGKGCITLSQLTLHQRIHTGERPYKCEECGKAFRTNSDFTVHLRMHTGEKPYKCNECGKAFRSSSSLTVHQRIHQRETQLI
Protein: At1g11210 (Cotton fiber protein, putative (DUF761)) (T28P6.13 protein) (Q9SXA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g39675
- Tetratricopeptide repeat
- CRS1 / YhbY
- F28K20.8 protein
- At1g16880
- Protein SPIRAL1-like 2
- Protein QUIRKY
- Myb family transcription factor PHL12
Sequence:
MASWMKAVLISTGVVATAMHLKVIVPVAMDFSQNPIILSSFLTWLKPPYLYVITNVIIIVVGVSYRITTVSSHVDGKDYEASYSGDNKFQTDHQQIVQEAPLRRRTETKDADFGFIGKVLQIVKEPEVVYEEKERPATVEEEEKKCIIVVSKSENQPPVEKPLVTARIGQKKPVVKTTPAERNSMRALRVAKPKRNETLENTWKMIMEGNKSTLPLTSYYKRPDTFGLGEETKQSGVLKKSETFSDRTNCYQSLPPPPPPLVKVKKVKVSRSRDELNRKVEAFIKKCNDERFASMKLDNEVARHGLSY
Protein: Spermatogenesis-associated protein 33 (Q8C624)
Organism: Mus musculus (Mouse)
Function: Plays an important role in sperm motility and male fertility. Required for sperm midpiece flexibility and for the localization of sperm calcineurin to the mitochondria. Promotes mitophagy as well as acts as an autophagy mediator in male germline cells. Links damaged mitochondria to autophagosomes via its binding to the outer mitochondrial membrane protein VDAC2, as well as to key autophagy machinery component ATG16L1.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23844118}. Nucleus {ECO:0000269|PubMed:23844118}. Cytoplasm {ECO:0000269|PubMed:33087875}. Mitochondrion {ECO:0000269|PubMed:33087875, ECO:0000269|PubMed:34446558}.
Interaction partners:
Sequence:
MGQSKSKPREKKEEEKSTTTLVTKSKEKVMEKEAKQSDKESQPAESLLFATSKHSRPSSSSEDKPETKQRSSKKRSVIPQIIITRASNETLISYGIPDNDEQRTIREHADWGPYHRHRSPSTIAAYDVHNTE
Protein: Peptide transport periplasmic protein SapA (Q7VM01)
Organism: Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Interaction partners:
- Peptide transport system permease protein SapB
- Peptide transport system permease protein SapC
- Peptide transport system ATP binding protein SapD
- Dipeptide transport system permease protein
- Dipeptide transport system permease protein
- ABC transporter, ATP-binding protein and permease protein
- HTH-type transcriptional regulatory protein TyrR
Sequence:
MKILALSILKFSPFFAVFCWISTAYSAPRVPKELSADSLIYCTSISGLSFNPQKADVGTNMNVVTEQIYDKLFEIDRHTHRVIPSLAETFSVSDDGKEITLNLRRQVAFHKTPWFTPTRLFNAEDVVFSLNRMIGNVEELPALDFNEDSKEQFQQNQRYAYHFKANLAHYPYFESVALKKKIAKISAPNEYTVKIHLVAPDNSVLAHLASQYAVILSKEYALLLNADENLAQLDLLPVGTGVYQLSDYIQNEYVRLKPNPVYWGEKAKINNVVVDFSSNSTGRMAKYLNQECDIVAQPEPSQRRVISSYEIVESPGANLAFLAFNMQKEKMQDIAFRRQIAQAINRERLVKALFYGSAEVADNVLPSALFAQKNPAAYPYKAPQPRAKNAKLDRLIFWVLDESRVYNLHPLKMAEMIRNDLKKINIDVIIRPVSRAKVVQLAAAGKADYDLILTGWLANNLDPNAFLSPILSCRTQNKVTNLANWCHQQFDEWLEIAKANQVPYVRNMIYKQTQALLEEQLPILPLLHAQRSLFVNQKIKNAHIEPFGQVRLSELTLHQE
Protein: Protein DML1 (Drosophila melanogaster misato-like protein 1) (Q03652)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12702300}. Mitochondrion {ECO:0000269|PubMed:12702300, ECO:0000269|PubMed:14690591}.
Interaction partners:
- Divalent cation/proton antiporter GDT1
- Small ribosomal subunit protein uS19m
- tRNA-specific adenosine deaminase 1
Sequence:
MHEVVTISVSQRANHLTTQFFNIQEGYLQLSKEQQVNDSKIFLNSVVDKVSKTISYAPRALLWDARTGNGSLGTYQYSESQDYHFGNEDKFKEQTVIKTHPRIPKSEYQSSLDAGAPLPCLNRENTMYWSDYSKLIYGPSSFNILRNWYHDTENPNQPDFQNLGERKFDRYSIGYDEFTENYLQEFFDGNLHRELEKCDTLQGFNLVSDMESGWGGFSSALLVELRNELPKKAVFSWGHNEDDPFTDDFPMKRLSKKWLPIISNKLRSTINMMQESDLYFPLYAAPGLTNWETAGKSCRIFDSINATISQSNLEQRKTMDYLTTAITLGYSSRNMVTGMVIGDTDYSFCSRVLPFKNSHKPNSTHIFSKSFIDRGNQTHKHHSEPDSRSKMIEMYTHRYFPSDTIPTEFSNDREFVLELESSEKNRDIFKHWNEFVVRYFKNDSDREELKNELSDYASAYESGWYEDEDSGDDDM
Protein: Translation initiation factor eIF2B subunit delta (GCD complex subunit GCD2) (Guanine nucleotide exchange factor subunit GCD2) (eIF2B GDP-GTP exchange factor subunit delta) (P12754)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as essential component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD2 is also required for cell viability. Its function can partially be replaced by GCN3 under normal growth conditions in GCD2-defective mutants, under AA starvation conditions GCN3 is an antagonist (GCN4 translational activator).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09924}.
Interaction partners:
- Translation initiation factor eIF2B subunit gamma
- Eukaryotic translation initiation factor 2 subunit gamma
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 2 subunit alpha
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 2 subunit beta
- Protein DSS4
- eIF-2-alpha kinase GCN2
- Protein LTV1
Sequence:
MSESEAKSRSATPPSKAKQATPTTTAAANGEKKLTNKELKELKKQEKAAKRAAMKQANGISIEQQQQQAQMKKEKKQLQREQQQKREQKQKNANKKKQNERNVKKSTLFGHLETTEERRATILALTSAVSSPKTSRITAAGLMVPVVASALSGSNVLTASSLMPVGPNASSTVSASAPASTTTTLPASSAALSAGTSSASTNTPTAIQQEIASSNASDVAKTLASISLEAGEFNVIPGISSVIPTVLEQSFDNSSLISSVKELLLNKDLIHPSILLLTSHLAHYKIVGSIPRCIAMLEVFQIVIKDYQTPKGTTLSRNLTSYLSHQIDLLKKARPLSVTMGNAIRWLKQEISLIDPSTPDKAAKKDLCEKIGQFAKEKIELADQLIIDNASTQIEESTTIVTYGSSKVLTELLLHNAISLKKNIKVIVVDSRPLFEGRKMAETLRNAGVNVMYALITSLDTIFNMDVDYVFLGAHSILSNGFLYSRAGTAMLAMSAKRRNIPVLVCCESLKFSQRVQLDSVTFNELADPNDLVNIDYENPVERRGNKGALLNQFIKERKFEKKKLAMENKPKGNKIGGKKGSEGESKDASNEEDSNSKNILDGWQELPSLNIVNILYDLTPPEYIKKVITEFGALPPSSVPVILREYKGSA
Protein: F-box and leucine rich repeat protein 3 (C9J0Y7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKRGGRDSDRNSSEEGTAEKSKKLRTTNEHSQTCDWGNLLQDIILQVFKYLPLLDRAHASQVCRNWNQVDSSKESAEAACDILSQLVNCSLKTLGLISTARPSFMDLPKSHFISALTVVFVNSKSLSSLKIDDTPVDDPSLKVLVANNSDTLKLLKMSSCPHVSPAGILCVADQCHGLRELALNYHLLSDELLLALSSEKHVRLEHLRIDVVSENPGQTHFHTIQKSSWDAFIRHSPKVNL
Protein: Torsin-2A (Torsin family 2 member A) (Torsin-related protein 1) (Q5JU69)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250}.
Interaction partners:
- Peptidyl-glycine alpha-amidating monooxygenase
Sequence:
MAAATRGCRPWGSLLGLLGLVSAAAAAWDLASLRCTLGAFCECDFRPDLPGLECDLAQHLAGQHLAKALVVKALKAFVRDPAPTKPLVLSLHGWTGTGKSYVSSLLAHYLFQGGLRSPRVHHFSPVLHFPHPSHIERYKKDLKSWVQGNLTACGRSLFLFDEMDKMPPGLMEVLRPFLGSSWVVYGTNYRKAIFIFISNTGGKQINQVALEAWRSRRDREEILLQELEPVISRAVLDNPHHGFSNSGIMEERLLDAVVPFLPLQRHHVRHCVLNELAQLGLEPRDEVVQAVLDSTTFFPEDEQLFSSNGCKTVASRIAFFL
Protein: Centromere protein P (HCG1643604) (X6R9C8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQEKYPDAVYLSEGPSSCSMGIRSASRPGFELVIVWRIQIDEDGKVFPKLDLLTKVPQRALELDKNRAIETAPLSFRTLVGLLGIEAALESLIKSLCAEENN
Protein: Nuclear receptor corepressor 2 (C9J0Q5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGSTQPVAQTWRATEPRYPPHSLSYPVQIARTHTDVGLLEYQHHSRDYASHLSPGSIIQPQRRRPSLLSEFQPGNERSQELHLRPESHSYLPELGKSEMEFIESKRPRLELLPDPLLRPSPLLATGQPAGSEDLTKDRSLTGKLEPVSPPSPPHTDPELELVPPRLSKEELIQNMDRVDREITMVEQQISKLKKKQQQLEEEAAKPPEPEKPVSPPPIESKHRSLVQIIYDENRKKAEAAHRILEGLGPQVELPLYNQPSDTRQYHENIKINQAMRKKLILYFKRRNHARKQWEQKFCQRYDQLMEAWEKKVERIENNPRRRAKESKVREYYEKQFPEIRKQRELQERMQRVGQRGSGLSMSAARSEHEVSEIIDGLSEQENLEKQMRQLAVIPPMLYDADQQRIKFINMNGLMADPMKVYKDRQVMNMWSEQEKETFREKFMQHPKNFGLIASFLERKTVAECVLYYYLTKKNENYKSLVRRSYRRRGKSQQQQQQQQQQQQQQQQQPMPRSSQEEKDEKEKEKEAEKEEEKPEVENDKEDLLKEKTDDTSGEDNDEKEAVASKGRKTANSQGRRKGRITRSMANEANSEEAITPQQSAELASMELNESSRWTEEEMETAKKGLLEHGRNWSAIARMVGSKTVSQCKNFYFNYKKRQNLDEILQQHKLKMEKERNARRKKKKAPAAASEEAAFPPVVEDEEMEASGVSGNEEEMVEEAEATVNNSSDTESIPSPHTEAAKDTGQNGPKPPATLGADGPPPGPPTPPPEDIPAPTEPTPASEATGAPTPPPAPPSPSAPPPVVPKEEKEEETAAAPPVEEGEEQKPPAAEELAVDTGKAEEPVKSECTEEAEEGPAKGKDAEAAEATAEGALKAEKKEGGSGRATTAKSSGAPQDSDSSATCSADEVDEAEGGDKNRLLSPRPSLLTPTGDPRANASPQKPLDLKQLKQRAAAIPPIQVTKVHEPPREDAAPTKPAPPAPPPPQNLQPESDAPQQPGSSPRGKSRSPAPPADKEAEKPVFFPAFAAEAQKLPGDPPCWTSGLPFPVPPREVIKASPHAPDPSAFSYAPPGHPLPLGLHDTARPVLPRPPTISNPPPLISSAKHPSVLERQIGAISQGMSVQLHVPYSEHAKAPVGPVTMGLPLPMDPKKLAPFSGVKQEQLSPRGQAGPPESLGVPTAQEASVLRGTALGSVPGGSITKGIPSTRVPSDSAITYRGSITHGTPADVLYKGTITRIIGEDSPSRLDRGREDSLPKGHVIYEGKKGHVLSYEGGMSVTQCSKEDGRSSSGPPHETAAPKRTYDMMEGRVGRAISSASIEGLMGRAIPPERHSPHHLKEQHHIRGSITQGIPRSYVEAQEDYLRREAKLLKREGTPPPPPPSRDLTEAYKTQALGPLKLKPAHEGLVATVKEAGRSIHEIPREELRHTPELPLAPRPLKEGSITQGTPLKYDTGASTTGSKKHDVRSLIGSPGRTFPPVHPLDVMADARALERACYEESLKSRPGTASSSGGSIARGAPVIVPELGKPRQSPLTYEDHGAPFAGHLPRGSPVTTREPTPRLQEGSLSSSKASQDRKLTSTPREIAKSPHSTVPEHHPHPISPYEHLLRGVSGVDLYRSHIPLAFDPTSIPRGIPLDAAAAYYLPRHLAPNPTYPHLYPPYLIRGYPDTAALENRQTIINDYITSQQMHHNAATAMAQRADMLRGLSPRESSLALNYAAGPRGIIDLSQVPHLPVLVPPTPGTPATAMDRLAYLPTAPQPFSSRHSSSPLSPGGPTHLTKPTTTSSSERERDRDRERDRDREREKSILTSTTTVEHAPIWRPGTEQSSGSSGGGGGSSSRPASHSHAHQHSPISPRTQDALQQRPSVLHNTGMKGIITAVEPSTPTVLRSTSTSSPVRPAATFPPATHCPLGGTLDGVYPTLMEPVLLPKEAPRVARPERPRADTGHAFLAKPPARSGLEPASSPSKGSEPRPLVPPVSGHATIARTPAKNLAPHHASPDPPAPPASASDPHREKTQSKPFSIQELELRSLGYHGSSYSPEGVEPVSPVSSPSLTHDKGLPKHLEELDKSHLEGELRPKQPGPVKLGGEAAHLPHLRPLPESQPSSSPLLQTAPGVKGHQRVVTLAQHISEVITQDYTRHHPQQLSAPLPAPLYSFPGASCPVLDLRRPPSDLYLPPPDHGAPARGSPHSEGGKRSPEPNKTSVLGGGEDGIEPVSPPEGMTEPGHSRSAVYPLLYRDGEQTEPSRMGSKSPGNTSQPPAFFSKLTESNSAMVKSKKQEINKKLNTHNRNEPEYNISQPGTEIFNMPAITGTGLMTYRSQAVQEHASTNMGLEAIIRKALMGKYDQWEESPPLSANAFNPLNASASLPAAMPITAADGRSDHTLTSPGGGGKAKVSGRPSSRKAKSPAPGLASGDRPPSVSSVHSEGDCNRRTPLTNRVWEDRPSSAGSTPFPYNPLIMRLQAGVMASPPPPGLPAGSGPLAGPHHAWDEEPKPLLCSQYETLSDSE
Protein: Nicastrin (Q9VC27)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch. It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Presenilin homolog
- Gamma-secretase subunit Aph-1
- Gamma-secretase subunit pen-2
- Neurogenic locus Notch protein
- ADAM10 endopeptidase
- ADAM10 endopeptidase
- Amyloid-beta-like protein
- Protein numb
- Furin-like protease 2
- Furin-like protease 1, isoforms 1/1-X/2
Sequence:
MEMRLNAASIWLLILSYGATIAQGERTRDKMYEPIGGASCFRRLNGTHQTGCSSTYSGSVGVLHLINVEADLEFLLSSPPSPPYAPMIPPHLFTRNNLMRLKEAGPKNISVVLLINRTNQMKQFSHELNCPNQYSGLNSTSETCDASNPAKNWNPWGTGLLHEDFPFPIYYIADLDQVTKLEKCFQDFNNHNYETHALRSLCAVEVKSFMSAAVNTEVCMRRTNFINNLGGSKYCDPLEGRNVYATLYPRKPAIENNLETVHTNEKFILVTCRLDTTTMFDGVGLGAMDSLMGFAVFTHVAYLLKQLLPPQSKDLHNVLFVTFNGESYDYIGSQRFVYDMEKLQFPTESTGTPPIAFDNIDFMLDIGTLDDISNIKLHALNGTTLAQQILERLNNYAKSPRYGFNLNIQSEMSAHLPPTSAQSFLRRDPNFNALILNARPTNKYYHSIYDDADNVDFTYANTSKDFTQLTEVNDFKSLNPDSLQMKVRNVSSIVAMALYQTITGKEYTGTKVANPLMADEFLYCFLQSADCPLFKAASYPGSQLTNLPPMRYISVLGGSQESSGYTYRLLGYLLSQLQPDIHRDNCTDLPLHYFAGFNNIGECRLTTQNYSHALSPAFLIDGYDWSSGMYSTWTESTWSQFSARIFLRPSNVHQVTTLSVGIVVLIISFCLVYIISSRSEVLFEDLPASNAALFG
Protein: 14-3-3h protein (D9Z6D5)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MDFSKERERFVYIAKLAEQAERFDDMVTSMKKLAELDVELTVEERNLLSVGYKNVIGARRASWRILSSIEQKEESKGNEQNVKKIKTSRQKVESELSNICKDIMGVINEHLIPSCSGGESTGFYYKMKGDYYRYLAEFKMGDERKEAADQSMKAYQSATTTAEAELPPTHPIRLGLALNFSVFYYEIMNSPERACHLAKQAFDEAISELDTLSEESYKDSTLIMQLLRDNLTLWTSDIPEDGEEAAKLGAAKVGEGDE
Protein: Nucleolar and spindle-associated protein 1 (NuSAP) (Q9BXS6)
Organism: Homo sapiens (Human)
Function: Microtubule-associated protein with the capacity to bundle and stabilize microtubules (By similarity). May associate with chromosomes and promote the organization of mitotic spindle microtubules around them.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Chromosome {ECO:0000250}. Note=Found in the cytoplasm and nucleolus during interphase and redistributes to the mitotic spindle in prometaphase (By similarity). Localizes to the mitotic spindle during anaphase and telophase then disappears from around the chromosomes during cytokinesis (By similarity). Localizes to multiple distinct regions of chromosomes throughout mitosis. {ECO:0000250, ECO:0000269|PubMed:17276916, ECO:0000269|PubMed:17618083}.
Interaction partners:
- DNA topoisomerase 2-alpha
- Kinesin-like protein KIF11
- Disks large-associated protein 5
- Ubiquitin-conjugating enzyme E2 C
- Targeting protein for Xklp2
- G2/mitotic-specific cyclin-B2
- Kinesin-like protein KIF20A
- Lymphokine-activated killer T-cell-originated protein kinase
- Baculoviral IAP repeat-containing protein 5
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
Sequence:
MIIPSLEELDSLKYSDLQNLAKSLGLRANLRATKLLKALKGYIKHEARKGNENQDESQTSASSCDETEIQISNQEEAERQPLGHVTKTRRRCKTVRVDPDSQQNHSEIKISNPTEFQNHEKQESQDLRATAKVPSPPDEHQEAENAVSSGNRDSKVPSEGKKSLYTDESSKPGKNKRTAITTPNFKKLHEAHFKEMESIDQYIERKKKHFEEHNSMNELKQQPINKGGVRTPVPPRGRLSVASTPISQRRSQGRSCGPASQSTLGLKGSLKRSAISAAKTGVRFSAATKDNEHKRSLTKTPARKSAHVTVSGGTPKGEAVLGTHKLKTITGNSAAVITPFKLTTEATQTPVSNKKPVFDLKASLSRPLNYEPHKGKLKPWGQSKENNYLNQHVNRINFYKKTYKQPHLQTKEEQRKKREQERKEKKAKVLGMRRGLILAED
Protein: Maturase K (Q5QKX9)
Organism: Oryza eichingeri
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
PFDKPRNISLSLIQVEIQMEKFEGYSEKLKFPRQYFVYPLLFQEYIYVFAHDYGLNGSELVEIFGSNNKKFSSLLVKRLMIRMYQQNFWINLVNRPNQDRLLDYNNYFYSEFYSQILSEGFAIVVKIPFSLREQSCPEEKEIPKFQNLRSIHSIFPFLEDKFLHLHYLAHIEIPYPIHLDILLQLLQYRIQDVPSLHLLRFFLNYYSNWNSFITSMKSIFILKKENKRLFRFLYNSYVSEYEFFLVVLRKQSSCLRLTSSGTFLERIHFSRKMEHFGVMYPAFFRKTIWFVMDPLMHYVRNQGKAILASKGTLLLKKKWKCYLVRLWQYSFSFWTQPQRIHLNQLANSCFDFLGYFSSVPINSLLVRNQMLENSFLIDTQMKKFDTKVPVTPLIGSLAKAQFCTGSGHPISKPIWTDLSDWDILDRFGRICRNLFHYHSGSSKKKTLYRLKYILRLSCARTLARKHKSTVRAFMQWLGSVFLEEFFTEEEQVFSLMFAKTTYFSFRGSHSERIWYL
Protein: Nuclear transcription factor Y subunit B-6 (AtNF-YB-6) (AtNF-YB6) (Protein LEAFY COTYLEDON 1-LIKE) (Q84W66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters. Plays a role in the regulation of the embryogenesis. Involved in the abscisic acid (ABA) signaling pathway.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit C-2
- Nuclear transcription factor Y subunit C-1
- ABSCISIC ACID-INSENSITIVE 5-like protein 1
- Nuclear transcription factor Y subunit A-2
- Nuclear transcription factor Y subunit A-6
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit A-1
- Nuclear transcription factor Y subunit A-4
- Nuclear transcription factor Y subunit C-4
Sequence:
MERGGFHGYRKLSVNNTTPSPPGLAANFLMAEGSMRPPEFNQPNKTSNGGEEECTVREQDRFMPIANVIRIMRRILPAHAKISDDSKETIQECVSEYISFITGEANERCQREQRKTITAEDVLWAMSKLGFDDYIEPLTLYLHRYRELEGERGVSCSAGSVSMTNGLVVKRPNGTMTEYGAYGPVPGIHMAQYHYRHQNGFVFSGNEPNSKMSGSSSGASGARVEVFPTQQHKY
Protein: Fibulin-1 (O77469)
Organism: Caenorhabditis elegans
Function: Incorporated into fibronectin-containing matrix fibers. Plays a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Important for certain developmental processes and contributes to the supramolecular organization of ECM architecture, in particular to those of basement membranes.
Subcellular location: [Isoform a]: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:17043142}.
Interaction partners:
- Metalloprotease mig-17
- Large ribosomal subunit protein mL51
- Collagen alpha-1
- Collagen alpha-2
- A disintegrin and metalloproteinase with thrombospondin motifs gon-1
- Abnormal cell migration protein 18
- Papilin
- Amidohydrolase-related domain-containing protein
- Basement membrane proteoglycan
- Agrin
Sequence:
MRICFLLLAFLVAETFANELTRCCAGGTRHFKNSNTCSSIKSEGTSMTCQRAASICCLRSLLDNACDSGTDIAKEEESCPSNINILGGGLKKECCDCCLLAKDLLNRNEPCVAPVGFSAGCLRSFNKCCNGDIEITHASEIITGRPLNDPHVLHLGDRCASSHCEHLCHDRGGEKVECSCRSGFDLAPDGMACVDRNECLTRQSPCTQSEDCVNTIGGYICQRRISRLVPHRHRANRIGNAPRRMRDDPYSRAGEYREASQANTEFGCPMGWLFQHGHCVDVDECNLGSHDCGPLYQCRNTQGSYRCDAKKCGDGELQNPMTGECTSITCPNGYYPKNGMCNDIDECVTGHNCGAGEECVNTPGSFRCQQKGNLCAHGYEVNGATGFCEDVNECQQGVCGSMECINLPGTYKCKCGPGYEFNDAKKRCEDVDECIKFAGHVCDLSAECINTIGSFECKCKPGFQLASDGRRCEDVNECTTGIAACEQKCVNIPGSYQCICDRGFALGPDGTKCEDIDECSIWAGSGNDLCMGGCINTKGSYLCQCPPGYKIQPDGRTCVDVDECAMGECAGSDKVCVNTLGSFKCHSIDCPTNYIHDSLNKNQIADGYSCIKVCSTEDTECLGNHTREVLYQFRAVPSLKTIISPIEVSRIVTHMGVPFSVDYNLDYVGQRHFRIVQERNIGIVQLVKPISGPTVETIKVNIHTKSRTGVILAFNEAIIEISVSKYPF
Protein: Agouti related protein (Q9QXJ3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
LFPEFSGLSLKKTAADRAEDVLLQKAEALAEVLDPQNRESRSPRRCVRLHESCLGQQVPCCDLCATCYCRFFKTCYCR