wanglab/gogpt-training-data huggingface dataset:
Protein: Integrin subunit alpha 2b (D3ZAC0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
- Integrin beta-3
- von Willebrand factor
- Aa1018
- Talin 1
- FERM domain containing kindlin 3
- Talin 2
- Filamin, alpha
- Guanine nucleotide-binding protein subunit alpha-13
- Actin, cytoplasmic 1
- Proto-oncogene tyrosine-protein kinase Src
Sequence:
MARASCAWNTLWLLQWTPLFLGPSAAPPAWALNLDSVKFSVYTGPNGSHFGFSVDFHKDSHGSVSIVVGAPRALNANQEETGGVFLCPWKANNGTCTSLLFDLRDETRKLSLQTFQTFKTGQGLGASVLSWNDVIVACAPWQHWNVLEKYDEAEKTPVGGCFVAELQSGGRAEYSPCRSNTMSSVYSQGFSKRWSAIGLLFQAGELVLGAPGGYFFLGMCPNIISSYRPGTLLWHVSNQRFSYDSSNPVYFHGYRGYSVAVGEFDGDLSTTEYIFGAPTWSWTLGAVEILDSYYQTLHRLHGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRVDRKLAEVGRVYLFLQPKGLQALSSPTLVLTGTQVYGRFGSAIAPLGDLNRDGYNDVAVAAPYGGPSGQGQVLIFLGQSEGLSPRPSQVLDSPFPTGSGFGFSLRGSVDIDDNGYPDLIVGAYGASKVAVYRAQPVVMATVQLMVQDSLNPTLKNCVLEQTKTPVSCFNVQMCVGATGHNIPQKLHLKAELQLDLQKPRQARRVLLLASRQASLTLSLDLGGRNKPICHTIKAFLRDEADFRDKLSPIVLSLNVSLPPEETGVAPAVVLHGVTHVQEQTRIILDCGEDNLCVPQLQLTATAGDSPLLIGADNVLELKVNASNDGEGAYEAELAVHLPPGAHYIRAFSNVKGFERLVCTQKKENESRLALCELGNPMKKDTRIGITMLVSVEILEEAGDSVSFQLQIRSKNSQNPNSEAVLLPVAVRAEAAVELRGNSFPASLVVAAEEVDKEQDGLDSWVSRVEHTYELHNNGPGTVNGLSLIIHLPGQSQPSDLLYILDVQPKGGLLCSTQPPPKLLKVDRRLTTPSPSSIRRIHHDRDRREASPQGSKQTEQQDPVLVSCNGSAPCTVVECELQEMVRGQRAMVTVQATLGLSILRQRPQEQFVLQSHAWFNVSSLPYSVPVVSLPSGQGLVQTHLLRALEERDIPVWWVLVGVLGGLLLLTLLVLAMWKVRLKGRHRLPN
Protein: LD47622p (Q960J6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVPQQAKFPDCIAMVFDEQRSKVSCVYNDHSLYIWDLRDISRVGKSHSFLYHSTCIWGVETVPYNVEREPSQTLPEECFVTCSSDDTIRVWGLDGCTNNDIYRRNIYSKELLKIVYSDDELQFIKDQGSSLFDKAGNSSYDGRNGVRCIKISPELQHLASGDRCGNIRVYSLVNLRLLTTIEAHESEVLCLEYSNEKIERKLLASASRDRLIHVFDVAQNYLLLQTLDDHSSSITSIKFVGAGLNFQMISCGADKSIMFRSFQGNIFMRGTNTSGKTTLYDMEVDSNAKHILTACQDRNVRVYGTQNAKQTKTFKGSHSDEGSLIKLSLDPSGIYVATSCTDKTLAVYDYYSNECMARMYGHSELVTGLKFTNDCRHLISASGDGCIFIWQVPHDMIVTMQARMSQQRLRSGHAPLPRPLAPISPPDGIVLESPTSEIEQPQLQPKFGVAERFSDVGQLPQWAMRKAAADSDSGALSIPTPSGGSATVPGMHAASSMGNLSSSPSQQMTGLAPRARGRWAQRSTQLETADDLRSNSESPLGTVSSVGGHSGVNVQTSDYNSASSKDITYNQTYLSEDSSIDSGMETRRGELKFIGSSNNGTVVTVSSVSSIAVSASNGAMSTGSGAAQQRLQLPDKRLKPGLRFDTHTHDHDGDVEDISDGERTSSDHGMFYNNLAPSTPTDFKVTAMNEDELRKSVRRQKFEKSGLQLTPSALSGNGSSHTASTGTGTSDTEDEGSTPSAENAERSLASTLGGSSENLPQSSTNSFLHAALPEGPGLTTPMERGGSSRRSISAKHNTENGKSVAAPPTITKSYTSTKKEELLQVINKVKQQLENVGHRPLRGSHSISDLSLAANLDGSRNAGGGPGRYQKPGNPKTLNPMPIEESSIRRACSLSDLHMGNFGKPGKSQNGTPQKPQVQHRNGNVSRSASKRNSLQGKTGLGASSNSMNVLNQGSDSEPEDSNRLRSASNGQGRSNGPIAANRQYSNKINNVNNNRRKTPNFSSATPMQDDSSSEETPNSTVNNKPIVPPRPRNLAFDHKSKLMINNSGSPGGNAKQRSGVTSTEDFEGTDPEAQVHNVINKLYTTTQAAMQLHANLKNTLLLKELENALIMSRNMLSSITNRQADKTNNGGGGLGVGGSGGLNHDQLNADNGDYLMMVNNCADLLSNLRTKHKPDDCENNS
Protein: Protein lin-7 homolog A (Lin-7A) (Mammalian lin-seven protein 1) (MALS-1) (Vertebrate lin-7 homolog 1) (Veli-1) (Q9Z250)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Cell junction {ECO:0000250|UniProtKB:Q8JZS0}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8JZS0}. Note=Mainly basolateral in renal epithelial cells. {ECO:0000250|UniProtKB:Q8JZS0}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Peripheral plasma membrane protein CASK
- Amyloid-beta A4 precursor protein-binding family A member 1
- MAGUK p55 subfamily member 7
- PTPRF interacting protein alpha 2
- Protein PALS1
- Phagosome assembly factor 1
- Disks large homolog 1
- ATP-sensitive inward rectifier potassium channel 12
- Liprin-alpha-4
Sequence:
MLKPSVTSAPTADMATLTVVQPLTLDRDVARAIELLEKLQESGEVPVHKLQSLKKVLQSEFCTAIREVYQYMHETITVNGCPEFRARATAKATVAAFAASEGHSHPRVVELPKTDEGLGFNVMGGKEQNSPIYISRIIPGGVAERHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAKDSVKLVVRYTPKVLEEMEARFEKLRTARRRQQQQLLIQQQQQQQQQPQQNHMS
Protein: Adenylate cyclase type 9 (EC 4.6.1.1) (ATP pyrophosphate-lyase 9) (Adenylate cyclase type IX) (Adenylyl cyclase 9) (AC9) (Adenylyl cyclase type 10) (ACTP10) (P51830)
Organism: Mus musculus (Mouse)
Function: Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors. Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and by beta-adrenergic receptors.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8662814}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Rap guanine nucleotide exchange factor 3
- Guanine nucleotide-binding protein G
- Rap guanine nucleotide exchange factor 4
- Adenylate cyclase type 6
- Adenylate cyclase type 3
- Bis
- Protein kinase C delta type
Sequence:
MASSPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNTHPKHCKYSISSSCSSSGDSGGLPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSMNLEEACLERCFPQTQRRFRYALFYVGFACLLWSIYFAVHMKSKVIVMVVPALCFLVVCVGFFLFTFTKLYARHYAWTSLALTLLVFALTLAAQFQVWTPLSGRVDSSNHTLTATPADTCLSQVGSFSICIEVLLLLYTVMQLPLYLSLFLGVVYSVLFETFGYHFRNEDCYPSPGPGALHWELLSRALLHVCIHAIGIHLFVMSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKRHATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEQTKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMEDGRVIERLGQSVVADQLKGLKTYLISGQRAKESHCSCAEALLSGFEVIDDSRESSGPRGQGTASPGSVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGTVQNGCQDEPKTSTKASGGPNSKTQNGLLSPPAEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNIREKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTFASATFSSLLDVFLSTTVFLILSITCFLKYGATATPPPPAALAVFGADLLLEVLSLIVSIRMVFFLEDVMTCTKWLLEWIAGWLPRHCIGAILVSLPALAVYSHITSEFETNIHVTMFTGSAVLVAVVHYCNFCQLSSWMRSSLATIVGAGLLLLLHISLCQDSSIVMSPLDSAQNFSAQRNPCNSSVLQDGRRPASLIGKELILTFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTKIQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKECYRVLNELIGDFDELLSKPDYNSIEKIKTIGATYMAASGLNTAQCQEGGHPQEHLRILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDNGVVPQHQLSISPDIRVQVDGSIGRSPTDEIANLVPSVQYSDKASLGSDDSTQAKEARLSSKRSWREPVKAEERFPFGKAIEKDSCEDIGVEEASELSKLNVSKSV
Protein: MARVEL domain-containing protein 3 (Q9D956)
Organism: Mus musculus (Mouse)
Function: As a component of tight junctions, plays a role in paracellular ion conductivity.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250}.
Interaction partners:
Sequence:
MKNTSGHREPRTRPRERDPDRRPHPDRDHHVERSRDRGGDRHRERNGDVRGNGDRRAGREQRTDRDQRQDRHRDAGHRASEQRALEKSRQSRARPEPWGPSWDAAPTPGPAPWGPRELSQKHGLGRRGLESERASERYVPTYSVPALQEEEYYQSEAEGLLDCHKCRYLCTGRACWQMLKALLNLLILACSSVSYNSTGGYTGITSLGGIYYYQYGGAYSGFDGADGERAQQLDVQFYQLKLPTVTAAMAYSGALMTFSCLTLLAGALRVPWHCPLWLVIEGLMDALIAGAYVPGLYFFFQHLSAAYSSDVCKERETLYQSKGYSGFNCGVHGGDIGAGVFAAMAIGVFAVGAVLAFRGYRKVKKLKEKPTEMLEF
Protein: Eukaryotic translation initiation factor 4E homologous protein, isoform C (MIP06235p) (C1C3I0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSMEKVANKQYETKNWPDIVDSDDSDVDNQIDVDNLPPLEVGPGENRLQHTYCLWFSRKETQRAAADYSKSLHMVGRCASVQQWWSLYSHLIRPTALKPYRELLLFKQGIIPMWEDPANSKGGQWLIRLRKNKVDRAWENVCMAMLGEQFLVGDEICGVVLQTKYPIKTEHSRPMHTNERRSDGVT
Protein: Hepatocyte growth factor-regulated tyrosine kinase substrate (A0A0S2Z4R4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004469}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004469}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004469}.
Interaction partners:
Sequence:
MGRGSGTFERLLDKATSQLLLETDWESILQICDLIRQGDTQAKYAVNSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKDLLKRQVEVNVRNKILYLIQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVMTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLNRKAEGKATSTTELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLALALSQSEAEEKERLRQKSTYTSYPKAEPMPSASSAPPASSLYSSPVNSSAPLAEDIDPELARYLNRNYWEKKQEEARKSPTPSAPVPLTEPAAQPGEGHAAPTNVVENPLPETDSQPIPPSGGPFSEPQFHNGESEESHEQFLKALQNAVTTFVNRMKSNHMRGRSITNDSAVLSLFQSINGMHPQLLELLNQLDERRLYYEGLQDKLAQIRDARGALSALREEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQEYLEVQRQLAIQRLQEQEKERQMRLEQQKQTVQMRAQMPAFPLPYAQLQAMPAAGGVLYQPSGPASFPSTFSPAGSVEGSPMHGVYMSQPAPAAGPYPSMPSTAADPSMVSAYMYPAGATGAQAAPQAQAGPTASPAYSSYQPTPTAGYQNVASQAPQSLPAISQPPQSSTMGYMGSQSVSMGYQPYNMQNLMTTLPSQDASLPPQQPYIAGQQPMYQQMAPSGGPPQQQPPVAQQPQAQGPPAQGSEAQLISFD
Protein: Serpin A9 (Centerin) (Germinal center B-cell-expressed transcript 1 protein) (Q86WD7)
Organism: Homo sapiens (Human)
Function: Protease inhibitor that inhibits trypsin and trypsin-like serine proteases (in vitro). Inhibits plasmin and thrombin with lower efficiency (in vitro).
Subcellular location: [Isoform 1]: Secreted.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 7]: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Neprilysin
Sequence:
MASYLYGVLFAVGLCAPIYCVSPANAPSAYPRPSSTKSTPASQVYSLNTDFAFRLYRRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQGLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNFPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVLPSKGKMRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNVFDKNADFSGIAKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSKDGPSYFTVSFNRTFLMMITNKATDGILFLGKVENPTKS
Protein: Cyclin-dependent kinase-like 3 (EC 2.7.11.22) (Serine/threonine protein kinase NKIATRE) (Q9JM01)
Organism: Rattus norvegicus (Rat)
Subcellular location: [Isoform 2]: Nucleus. Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
Interaction partners:
Sequence:
MEMYETLGKVGEGSYGTVMKCKHKDTGRIVAIKIFYEKPEKSVNKIATREIKFLKQFRHENLVNLIEVFRQKKKIHLVFEFIDHTVLDELQHYCHGLESKRLRKYLFQILRAIEYLHNNNIIHRDIKPENILVSQSGITKLCDFGFARTLAAPGDVYTDYVATRWYRAPELVLKDTTYGKPVDIWALGCMIIEMATGNPYLPSSSDLDLLHKIVLKVGNLTPHLHNIFSKSPIFAGVVLPQVQHPKNARKKYPKLNGLLADIVHACLQIDPAERISSTDLLHHDYFTRDGFIEKFIPELRAKLLQEAKVNSFIKPKENFKENEPVRDEKKPVFTNPLLYGNPTLYGKEVDRDKRAKELKVRVIKAKGGKGDVPDLKKTESEGEHRQQGTAEDTHPTSLDRKPSVSELTNPVHPSANSDTVKEDPHSGGCMIMPPINLTSSNLLAANPSSNLSHPNSRLTERTKKRRTSSQTIGQTLSNSRQEDTGPTQVQTEKGAFNERTGQNDQIASGNKRKLNFSKCDRKEFHFPELPFTIQAKEMKGMEVKQIKVLKRESKKTDSPKIPTLLSMDSNQEKQEVFNIFPGWCKRGNLNWPS
Protein: Dbj|BAA84809.1 (Lung seven transmembrane receptor family protein) (Q9FHX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 20b
- Transcription factor ABORTED MICROSPORES
- AT3g59090/F17J16_140
- SAC3 family protein C
- Sulfite exporter TauE/SafE family protein 4
- RING-type E3 ubiquitin transferase
Sequence:
MDLSSRFSSILILLLISISIASAEIRKSEIRSDDRPIIPLDEFGFTHSGRLELDASKIWLSNSNPDLDLSKVGFFLCTRDAWVHVIQQLEEEEITCALQSDLVKHVFTFNNLKGGDKSRFSTVFTENDADQYSLVFANCLQQVKISMDVRSAMYNLEGKKGGRDYLSAGRTVLPKVYFLFSVIYFSLAATWIYVLYKKRLTVFAIHFFMLGVVVLKALNLLCEAEDKSYIKKTGTAHGWDVLFYIFNFLKGITLFTLIVLIGTGWSFLKPYLQDKEKKVLMIVIPLQVVANFAQVVIDETGPYGQDWVTWKQIFLLVDVVCCCAVLFPIVWSIKNLREAAKTDGKAAVNLVKLTLFRQYYIVVICYIYFTRVVVYALETITSYKYMWTSVVASELATLAFYLFTGYKFRPEVHNPYFVVDDEEEEAAAEALKLEDEFEL
Protein: PFL-like enzyme TdcE (Keto-acid formate acetyltransferase) (Keto-acid formate-lyase) (Ketobutyrate formate-lyase) (KFL) (EC 2.3.1.-) (Pyruvate formate-lyase) (PFL) (EC 2.3.1.54) (P42632)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Pyruvate formate-lyase 1-activating enzyme
- Phosphate acetyltransferase EutD
- Phosphate acetyltransferase
- Putative reactive intermediate deaminase TdcF
- Pyruvate formate-lyase 2-activating enzyme
- Putative pyruvate formate-lyase 3-activating enzyme
- D-lactate dehydrogenase
- Acetaldehyde dehydrogenase
- Pyruvate dehydrogenase
Sequence:
MKVDIDTSDKLYADAWLGFKGTDWKNEINVRDFIQHNYTPYEGDESFLAEATPATTELWEKVMEGIRIENATHAPVDFDTNIATTITAHDAGYINQPLEKIVGLQTDAPLKRALHPFGGINMIKSSFHAYGREMDSEFEYLFTDLRKTHNQGVFDVYSPDMLRCRKSGVLTGLPDGYGRGRIIGDYRRVALYGISYLVRERELQFADLQSRLEKGEDLEATIRLREELAEHRHALLQIQEMAAKYGFDISRPAQNAQEAVQWLYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDFKAGVLNEQQAQELIDHFIMKIRMVRFLRTPEFDSLFSGDPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMGPAPEPNLTILWSEELPIAFKKYAAQVSIVTSSLQYENDDLMRTDFNSDDYAIACCVSPMVIGKQMQFFGARANLAKTLLYAINGGVDEKLKIQVGPKTAPLMDDVLDYDKVMDSLDHFMDWLAVQYISALNIIHYMHDKYSYEASLMALHDRDVYRTMACGIAGLSVATDSLSAIKYARVKPIRDENGLAVDFEIDGEYPQYGNNDERVDSIACDLVERFMKKIKALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRRAGTPFAPGANPMHGRDRKGAVASLTSVAKLPFTYAKDGISYTFSIVPAALGKEDPVRKTNLVGLLDGYFHHEADVEGGQHLNVNVMNREMLLDAIEHPEKYPNLTIRVSGYAVRFNALTREQQQDVISRTFTQAL
Protein: Actin-related protein 2/3 complex subunit 3 (Arp2/3 complex 21 kDa subunit) (p21-ARC) (Q3T035)
Organism: Bos taurus (Bovine)
Function: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15145}. Cell projection {ECO:0000250|UniProtKB:O15145}. Nucleus {ECO:0000250|UniProtKB:O15145}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2
- Actin-related protein 3
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 5-like protein
- Actin-related protein 2/3 complex subunit 1A
- Uncharacterized protein
Sequence:
MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ
Protein: 6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78) (Riboflavin synthase beta chain) (Q9UUB1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. Also binds riboflavin with an unexpected high affinity.
Interaction partners:
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- Riboflavin synthase
- Probable GTP cyclohydrolase-2
- Riboflavin kinase
- 2,5-diamino-6-ribosylamino-4
- Diaminohydroxyphosphoribosylamino-pyrimidine deaminase
- Probable glutamine--fructose-6-phosphate aminotransferase
- Uracil-regulated protein 1
- S-adenosylmethionine synthase
- Inosine-5'-monophosphate dehydrogenase
Sequence:
MFSGIKGPNPSDLKGPELRILIVHARWNLQAIEPLVKGAVETMIEKHDVKLENIDIESVPGSWELPQGIRASIARNTYDAVIGIGVLIKGSTMHFEYISEAVVHGLMRVGLDSGVPVILGLLTVLNEEQALYRAGLNGGHNHGNDWGSAAVEMGLKALY
Protein: Voltage-dependent L-type calcium channel subunit alpha (G3V9W8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
- Calcium voltage-gated channel auxiliary subunit alpha2delta 4
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- cGMP-dependent protein kinase 2
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Voltage-dependent L-type calcium channel subunit alpha-1D
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MSESEVGKDTTPEPSPANGTGPGPEWGLCPGPPTVGTDTSGASGLGTPRRRTQHNKHKTVVVASAQRSPRALFCLTLTNPIRRSCISIVEWKPFDILILLTIFANCVALGVYIPFPEDDSNTANHNLEQVEYVFLVIFTVETVLKIVAYGLVLHPSAYIRNGWNLLDFIIVVVGLFSVLLEQGPGRPGDAPHTGGKPGGFDVKALRAFRVLRPLRLVSGVPSLHIVLNSIMKALVPLLHIALLVLFVIIIYAIIGLELFLGRMHKTCYFLGSDMEAEEDPSPCASSGSGRSCTLNQTECRGRWPGPNGGITNFDNFFFAMLTVFQCITMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQMEEDLRGYLDWITQAEELDLHDPSVDGNLASLAEEGRAGHRPQLSELTNRRRGRLRWFSHSTRSTHSTSSHASLPASDTGSITDTPGDEDEEEGTMASCTLCLNKIMKTKVCRHFRRANRGLRARCRRAVKSNACYWAVLLLVFLNTLTIASEHHGQPVWLTQTQEYANKVLLCLFTVEMLLKLYGLGPSVYVASFFNRFDCFVVCGGILETTLVEVGAMQPLGISVLRCVRLLRIFKVTRHWASLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDQTHTKRSTFDTFPQALLTVFQILTGEDWNVVMYDGIMAYGGPFFPGMLVCVYFIILFICGNYILLNVFLAIAVDNLASGDAGAAKDKGREKSSEGNPPQENKVLVPGGENEDTEGTKSEGAAPGMEEEEEEEEEEEEENGAGHVELLQEVVPKEKVVPIPEGSAFFCLSQTNPLRKACHTLIHHHVFTSLILVFIILSSVSLAAEDPIRAHSFRNHILGYFDYAFTSIFTVEILLKMTVFGAFLHQGSFCRSWFNLLDLLVVSVSLISFGIHSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYSCTDEAKHTLKECKGSFLIYPDGDVSRPLVRERLWVNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDAHAEDEGPIYNYHVEISVFFIVYIIIIAFFMMNIFVGFVIITFRAQGEQEYQNCELDKNQRQCVEYALKAQPLRRYIPKNPHQYRVWATVNSAAFEYLMFLLILLNTVALAMQHYEQTAPFNYAMDILNMVFTGLFTVEMVLKIIAFKPKHYFADAWNTFDALIVVGSVVDIAVTEVNNGGHLGESSEDSSRISITFFRLFRVMRLVKLLSKGEGIRTLLWTFIKSFQALPYVALLIAMIFFIYAVIGMQMFGKVALQDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLASLPGNRCDPESDFGPGEEFTCGSNFAIVYFISFFMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPGAKGRIKHLDVVALLRRIQPPLGFGKLCPHRVACKRLVAMNVPLNSDGTVTFNATLFALVRTSLRIKTEGNLDQANQELRMVIKKIWKRIKQKLLDEVIPPPDEEEVTVGKFYATFLIQDYFRKFRRRKEKGLLGADAPTSTSSVLQAGLRSLQDLGPEIRQALTYDTEEEEEEEEAAGQEAEEEEAENNPETYKDSIDSQPQAQWNSRISVSLPVKEKLPDSLSTGPSDDDGVAPNSRQPSGLQAGSQPHRRSSGVFMFTIPEEGSTQLKGVQGQDNQNEEQEVPDWTPNLDEQAGMPSNPVLLPPHWSQQHVNGHHVPRRRLLPPTPAGRKPSFTIQCLQRQGSCEDLPIPGTYHRGRTSGPGRAQGSWAAPPQKGRLLYAPLLLVEESTVGEGYLGKLGGPLRTFTCLQVPGAPSDPSHRKRGSADSLVEAVLISEGLGLFAQDPRFVALAKQEIADACHLTLDEMDSAASDLLAQRTTSLYSDEESILSRFDEEDLGDEMACVHAL
Protein: Epidermal growth factor-like protein 6 (EGF-like protein 6) (MAM and EGF domains-containing gene protein) (Q8IUX8)
Organism: Homo sapiens (Human)
Function: May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}.
Interaction partners:
Sequence:
MPLPWSLALPLLLSWVAGGFGNAASARHHGLLASARQPGVCHYGTKLACCYGWRRNSKGVCEATCEPGCKFGECVGPNKCRCFPGYTGKTCSQDVNECGMKPRPCQHRCVNTHGSYKCFCLSGHMLMPDATCVNSRTCAMINCQYSCEDTEEGPQCLCPSSGLRLAPNGRDCLDIDECASGKVICPYNRRCVNTFGSYYCKCHIGFELQYISGRYDCIDINECTMDSHTCSHHANCFNTQGSFKCKCKQGYKGNGLRCSAIPENSVKEVLRAPGTIKDRIKKLLAHKNSMKKKAKIKNVTPEPTRTPTPKVNLQPFNYEEIVSRGGNSHGGKKGNEEKMKEGLEDEKREEKALKNDIEERSLRGDVFFPKVNEAGEFGLILVQRKALTSKLEHKDLNISVDCSFNHGICDWKQDREDDFDWNPADRDNAIGFYMAVPALAGHKKDIGRLKLLLPDLQPQSNFCLLFDYRLAGDKVGKLRVFVKNSNNALAWEKTTSEDEKWKTGKIQLYQGTDATKSIIFEAERGKGKTGEIAVDGVLLVSGLCPDSLLSVDD
Protein: Endolysin CS74L (I1TJX3)
Organism: Clostridium phage phi8074-B1
Interaction partners:
Sequence:
MKIGIDMGHTLSGADYGVVGLRPESVLTREVGTKVIYKLQKLGHVVVNCTVDKASSVSESLYTRYYRANQANVDLFISIHFNATPGGTGTEVYTYAGRQLGEATRIRQEFKSLGLRDRGTKDGSGLAVIRNTKAKAMLVECCFCDNPNDMKLYNSESFSNAIVKGITGKLPNGESGNNNQGGNKVKAVVIYNEGADRRGAEYLADYLNCPTISNSRTFDYSCVEHVYAVGGKKEQYTKYLKTLLSGANRYDTMQQILNFINGGK
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FMW8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGIKWKKFIPHLRVLPEDLEGDVSSDNNSSIEEHIHHDDSKSIDDDKYHESHVVYAVDTSSNNANGKSSLPINSAHGSVKLQKGIPYELRDEANKSRWKFFDEYEYRLNKEYRKSRKWYEFLYPNHISQSKAERRLLYKLDIIVALYFLIVNWSRSVDSSNYTNAYVSHMKEDLHFKGNDYIYTSTIANVGSIVFQLPFIYILPRFPAHYVLPIMDFGWSWFTFACYRAKSLPELRAYRFILSSFGAAYYPVAQYLMGCWYAPDEISSRVCLFFCGQLLGSVTSGLLQARIFKSLNGVHGLAGWRWMFLIDAIAISIPTAILGFFVIPGIPSKCYSLFLTDEEIRIARARNKRNQIVDGVDRSKLPHIWSWKVWKKVFFTPTFWVLVIFDLCSWNNMTAYSGSYTLWLKSNTSYSIEKVNNLSVLPACLGFAFVFFCAFGSDLFRNKWPFMVFSQCMNCISCAILIKWDVASSTKWFAFLITYFSVAASPCLWSFINDFLRHDPQVKAITWIAIYSISQSTYAWIPTLTWKTVDAPRFKTGYIASLIFSAIYGLWTFVVLFFYKRNEKKNALGNGIILYNSSKGESPPTFVETDMVLKNGYYYVKEDCE
Protein: Cryptochrome DASH, chloroplastic/mitochondrial (Cryptochrome-3) (Q84KJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May have a photoreceptor function. Binds ss- and ds-DNA in a sequence non-specific manner. Has a photolyase activity specific for cyclobutane pyrimidine dimers in ssDNA.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12834405}. Mitochondrion {ECO:0000269|PubMed:12834405}.
Interaction partners:
- Timeless family protein
- Phototropin-1
- Phototropin-2
- Phytochrome E
- Transcription factor HY5
- Phytochrome A
- Deoxyribodipyrimidine photo-lyase
- E3 ubiquitin-protein ligase COP1
- Phytochrome C
- Phytochrome B
Sequence:
MAASSLSLSSPLSNPLRRFTLHHLHLSKKPLSSSSLFLCSAAKMNDHIHRVPALTEEEIDSVAIKTFERYALPSSSSVKRKGKGVTILWFRNDLRVLDNDALYKAWSSSDTILPVYCLDPRLFHTTHFFNFPKTGALRGGFLMECLVDLRKNLMKRGLNLLIRSGKPEEILPSLAKDFGARTVFAHKETCSEEVDVERLVNQGLKRVGNSTKLELIWGSTMYHKDDLPFDVFDLPDVYTQFRKSVEAKCSIRSSTRIPLSLGPTPSVDDWGDVPTLEKLGVEPQEVTRGMRFVGGESAGVGRVFEYFWKKDLLKVYKETRNGMLGPDYSTKFSPWLAFGCISPRFIYEEVQRYEKERVANNSTYWVLFELIWRDYFRFLSIKCGNSLFHLGGPRNVQGKWSQDQKLFESWRDAKTGYPLIDANMKELSTTGFMSNRGRQIVCSFLVRDMGLDWRMGAEWFETCLLDYDPCSNYGNWTYGAGVGNDPREDRYFSIPKQAQNYDPEGEYVAFWLQQLRRLPKEKRHWPGRLMYMDTVVPLKHGNGPMAGGSKSGGGFRGSHSGRRSRHNGP