wanglab/gogpt-training-data huggingface dataset:
Protein: Grainyhead-like protein 3 homolog (Sister of mammalian grainyhead) (Transcription factor CP2-like 4) (Q8TE85)
Organism: Homo sapiens (Human)
Function: Transcription factor playing important roles in primary neurulation and in the differentiation of stratified epithelia of both ectodermal and endodermal origin (By similarity). Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. xhibits functional redundancy with GRHL2 in epidermal morphogenetic events and epidermal wound repair (By similarity). Exhibits functional redundancy with GRHL2 in epidermal morphogenetic events and epidermal wound repair but is essential to form the epidermal barrier with TGM3 as critical direct target gene among others. Despite being dispensable during normal epidermal homeostasis in the adulthood, is again required for barrier repair after immune-mediated epidermal damage, regulates distinct gene batteries in embryonic epidermal differentiation and adult epidermal barrier reformation after injury. Plays unique and cooperative roles with GRHL2 in establishing distinct zones of primary neurulation. Essential for spinal closure, functions cooperatively with GRHL2 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure (By similarity). Also required for proper development of the oral periderm. No genetic interaction with GRHL3, no functional cooperativity due to diverse target gene selectivity.
Subcellular location: Nucleus {ECO:0000269|PubMed:21081122}.
Interaction partners:
- Interferon regulatory factor 6
- Protein-glutamine gamma-glutamyltransferase K
- Zinc finger protein 750
Sequence:
MSNELDFRSVRLLKNDPVNLQKFSYTSEDEAWKTYLENPLTAATKAMMRVNGDDDSVAALSFLYDYYMGPKEKRILSSSTGGRNDQGKRYYHGMEYETDLTPLESPTHLMKFLTENVSGTPEYPDLLKKNNLMSLEGALPTPGKAAPLPAGPSKLEAGSVDSYLLPTTDMYDNGSLNSLFESIHGVPPTQRWQPDSTFKDDPQESMLFPDILKTSPEPPCPEDYPSLKSDFEYTLGSPKAIHIKSGESPMAYLNKGQFYPVTLRTPAGGKGLALSSNKVKSVVMVVFDNEKVPVEQLRFWKHWHSRQPTAKQRVIDVADCKENFNTVEHIEEVAYNALSFVWNVNEEAKVFIGVNCLSTDFSSQKGVKGVPLNLQIDTYDCGLGTERLVHRAVCQIKIFCDKGAERKMRDDERKQFRRKVKCPDSSNSGVKGCLLSGFRGNETTYLRPETDLETPPVLFIPNVHFSSLQRSGGAAPSAGPSSSNRLPLKRTCSPFTEEFEPLPSKQAKEGDLQRVLLYVRRETEEVFDALMLKTPDLKGLRNAISEKYGFPEENIYKVYKKCKRGETSLLHPRLSRHPPPDCLECSHPVTQVRNMGFGDGFWRQRDLDSNPSPTTVNSLHFTVNSE
Protein: Nuclear export factor-b (Q99JG4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
KYSRDLKRQRDSSMRMQLLKHTKHDIVNSLSLLPKTQHDLCSFLVDLFLHTEMMLCFSVNGLFMEVEGKCRGCIRAFTRIFIAIPCSDSRAHSSFRICIMNDELIVRNASPKEIQKAFTSLPAPDTSFKPLLSEEQQEMVKSFSVQSGMKLDWSQKCLQDNEWDYTKAGEALTALQNEGKIPKEFFK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9JJ75)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASSSQAQPRDNEALASPCPRPWPCAGPTYSPTYWCPAPLGTQGPPDRPVEEVEQLPPQRYWPVVWTPGPQF
Protein: Trefoil factor 2 (Spasmolysin) (Spasmolytic polypeptide) (SP) (Q03403)
Organism: Homo sapiens (Human)
Function: Inhibits gastrointestinal motility and gastric acid secretion. Could function as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Mucin-5AC
- Mucin-6
- C-X-C chemokine receptor type 4
- Gastrokine-2
- Gastrin
- Cobalamin binding intrinsic factor
Sequence:
MGRRDAQLLAALLVLGLCALAGSEKPSPCQCSRLSPHNRTNCGFPGITSDQCFDNGCCFDSSVTGVPWCFHPLPKQESDQCVMEVSDRRNCGYPGISPEECASRKCCFSNFIFEVPWCFFPKSVEDCHY
Protein: Uncharacterized protein slr1417 (P72731)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Slr1098 protein
- Slr0635 protein
- Uncharacterized monothiol glutaredoxin ycf64-like
Sequence:
MSQATATQAKGIQLSDAALKHLLALKEQQGKDLCLRVGVRQGGCSGMSYMMDFEEPNRATEHDEVFDYEGFQIICDRKSLLYLYGLMLDYSNALIGGGFQFTNPNANQTCGCGKSFGV
Protein: DNA replication licensing factor MCM5 (EC 3.6.4.12) (Minichromosome maintenance protein 5) (AtMCM5) (O80786)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Subcellular location: Nucleus. Cytoplasm. Note=Localized in the nucleus during G1, S and G2 phases of the cell cycle, and released into the cytoplasmic compartment during mitosis.
Interaction partners:
- Probable DNA helicase MCM8
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM2
- DNA replication complex GINS protein PSF2
- DNA replication licensing factor MCM4
- Minichromosome maintenance 10
- Origin of replication complex subunit 2
- CDT1-like protein a, chloroplastic
- Cell division cycle 45
- Protein ENHANCER OF LHP1 1
Sequence:
MSGWDEGAVYYSDQPQFPEAGDAATISPHAVLTKFKEFIRNFEIEQNCFPYREALLDNPKRLVVHLEDLLSFDSDLPSLIRSAPADYLPVFEKAAGEVLTGLKMREANEGGVMEEPLTRDVQILLTSREDPVSMRLLGAQYISKLVKISGISIAASRVKAKATYVFLVCKNCKKTREVPCRPGLGGAIVPRSCDNIPQPGEEPCPLDPWMVVPDRSQYVDQQTLKLQENPEDVPTGELPRNMLLSVDRHLVQTIVPGTRLTVMGIYSIFQASSSSNSHKGAVAIRQPYIRVVGLEDTNEASSRGPANFTPDEEEEFKKFADSQDVYKNICTKIAPSIFGHEDVKRAAACLLFGGSRKSLPDGVKLRGDINVLLLGDPSTAKSQFLKFVEKTAPIAVYTSGKGSSAAGLTASVIRDSSTREFYLEGGAMVLADGGVVCIDEFDKMRPEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPPSGRYDDLKTAQDNIDLQTTILSRFDLIFIVKDIRKYSQDKEIASHIIRVHASANKFSDENTDSKEDNWLKRYIQYCRARCHPRLSKDAAENLQRKYVTIRMDMKRRAHETGEAAPIPITVRQLEAIVRLSESLAKMRLSHEATPDDVDKAFKLFDTSTMDAARSGINQQINITGEMANEIKQAETQIKRRMGIGARLSERRLIEDLARMGMNDSMVRRALLIMHQRGEVEYQRERRSIVRKA
Protein: Sulfofructose kinase (SF kinase) (EC 2.7.1.184) (P32143)
Organism: Escherichia coli (strain K12)
Function: Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP).
Interaction partners:
- Sulfofructosephosphate aldolase
- Sulfoquinovose isomerase
- HTH-type transcriptional repressor CsqR
- 3-sulfolactaldehyde reductase
- Sulfoquinovosidase
- Uncharacterized protein YihR
- Putative 2,3-dihydroxypropane-1-sulfonate exporter
- Putative sulfoquinovose importer
- D-ribose pyranase
- Inner membrane ABC transporter permease protein YdcV
Sequence:
MIRVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDTGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMVDTKGERIIINYPSPDLLPDAEWLEEIDFSQWDVVLADVRWHDGAKKAFTLARQAGVMTVLDGDITPQDISELVALSDHAAFSEPGLARLTGVKEMASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRAGIPDCDQTRSFLSLFV
Protein: Arginase-1 (EC 3.5.3.1) (Liver-type arginase) (Type I arginase) (P07824)
Organism: Rattus norvegicus (Rat)
Function: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P05089}. Cytoplasmic granule {ECO:0000250|UniProtKB:P05089}.
Interaction partners:
- Ornithine aminotransferase, mitochondrial
- Ornithine transcarbamylase, mitochondrial
- Ornithine decarboxylase
- Argininosuccinate lyase
- Antizyme inhibitor 2
- Nitric oxide synthase, inducible
- Antizyme inhibitor 2
- Nitric oxide synthase 1
- Nitric oxide synthase 3
- Glycine amidinotransferase, mitochondrial
Sequence:
MSSKPKPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAFVDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDHSMAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFGTKREGNHKPETDYLKPPK
Protein: histidine kinase (EC 2.7.13.3) (A0A6H3AF39)
Organism: Bacillus anthracis
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MKFKFHNIVLYILLVILPMIGIGATFYSYHSYKMKQENKRIAHTVLFLYRDYLDHHLGEAISALEMLSKVVGTETGNINGMKEIVHDTDGNDARFSGLYYTTPEGIITIASEGDRPPVDVSDRKYIQNALQTKKTTVSSVITDRVLGHQAIMIASPIFNKQKELSGLLLASLRFDYISSSLNAIKPQYHFEVTDKYDVVFLTDDNNETSDAHSNMLTTPLQRLDWKVSVSPLPIHQKTLNQWVAVECIATLFLMSILFLLAQYMLLKRQTKLERQQNELQKIELVGTFAASTAHEIRNPLTGIKGLVALLKEKYKDEQDQFYFSIIEQEIKRINEIVSEFLILGKPTATIEQTYDVRTILNEVALIIQSEANLHNIVFHLHLPDHPVHIRCSKDHMKQVVLNITKNAIEAMTSGDTLTISVTSNETHAQLQIIDTGKGIPKHIQKHLFHPFFTNKDTGTGLGLVICKRIVEMYNGHLFIDSIENEGTTVHAEIPLHIV
Protein: Tudor and KH domain-containing protein (Tudor domain-containing protein 2) (Q9Y2W6)
Organism: Homo sapiens (Human)
Function: Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs. May act in pi-bodies and piP-bodies by transferring piRNA precursors or intermediates to or between these granules.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q80VL1}. Mitochondrion {ECO:0000250|UniProtKB:Q80VL1}. Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Colocalizes with pi- and piP-bodies, a subset of the nuage which contains secondary piRNAs. Associated with mitochondria in the germline. {ECO:0000250|UniProtKB:Q80VL1}.
Interaction partners:
- Piwi-like protein 1
- Piwi-like protein 4
- Methylosome subunit pICln
- Protein maelstrom homolog
- Piwi-like protein 2
- Probable non-functional immunoglobulin heavy variable 3-16
- ATP-dependent RNA helicase TDRD9
- Tudor domain-containing protein 6
- RNA helicase Mov10l1
- Putative ATP-dependent RNA helicase TDRD12
Sequence:
MSTERTSWTSLSTIQKIALGLGIPASATVAYILYRRYRESREERLTFVGEDDIEIEMRVPQEAVKLIIGRQGANIKQLRKQTGARIDVDTEDVGDERVLLISGFPVQVCKAKAAIHQILTENTPVSEQLSVPQRSVGRIIGRGGETIRSICKASGAKITCDKESEGTLLLSRLIKISGTQKEVAAAKHLILEKVSEDEELRKRIAHSAETRVPRKQPISVRREDMTEPGGAGEPALWKNTSSSMEPTAPLVTPPPKGGGDMAVVVSKEGSWEKPSDDSFQKSEAQAIPEMPMFEIPSPDFSFHADEYLEVYVSASEHPNHFWIQIVGSRSLQLDKLVNEMTQHYENSVPEDLTVHVGDIVAAPLPTNGSWYRARVLGTLENGNLDLYFVDFGDNGDCPLKDLRALRSDFLSLPFQAIECSLARIAPSGDQWEEEALDEFDRLTHCADWKPLVAKISSYVQTGISTWPKIYLYDTSNGKKLDIGLELVHKGYAIELPEDIEENRAVPDMLKDMATETDASLSTLLTETKKSSGEITHTLSCLSLSEAASMSGDDNLEDDYLL
Protein: Cytochrome c oxidase subunit 4 (H3BN72)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367145}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367145}.
Interaction partners:
Sequence:
MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYGE
Protein: Stonin-2 (Stoned B) (Q8BZ60)
Organism: Mus musculus (Mouse)
Function: Adapter protein involved in endocytic machinery. Involved in the synaptic vesicle recycling. May facilitate clathrin-coated vesicle uncoating (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Note=Some fraction is membrane-associated.
Interaction partners:
- Epidermal growth factor receptor substrate 15
- Intersectin-1
- Transcription initiation factor IIA subunit 1
- Synaptotagmin-1
- Synaptotagmin-2
- Epidermal growth factor receptor substrate 15-like 1
- Intersectin-2
- Clathrin coat assembly protein AP180
- Disabled homolog 2
- Vesicle-associated membrane protein 2
Sequence:
MTTLDHVIATHQSEWVSFSEEPLFPTPLEGGTEEHFPGLSSSSERSESSSGENHVVDEGSQDLSHSEQDDSSEKMGLISEAASPPGSPVQPTPDLASAISNWVQFEDDTPWSSTSPPHKETALTLTMPCWTCPSFDSLRRCPLTSESSWTTHSEDTSSPSVAPSYTDLQLINTEEQASGRASGTDSTDNSSSLQEDEEVEMEAISWWAGSPAMNGHPAAPPVTTARFPSWVTFEDNEVGCPSPPVPSPKKPNTPSAATAAPDVPFNSTGSFKRDRPKSTLMNLPKVQKLDISSLNRPPSVIEAPPWRATNPFLNETLQDVQPSPINPFSAFFEEQERRSQNSSVSSTTGKSQRDSLIVVYQDAISFDDSGKSQPHPDAIEKLKQLQIDDPDPVGNTALPDDDPTASVELDAPSPASALSQPRDGWPMMLRIPEKKNIMSSRHWGPIYIKLTASGYLQLYYEQGLEKPFREFKLEICHEVSEPRLQNYDENGRIHSLRIDRVTYKEKKKYQPKPAVAHAAEREQVIKLGTTNYDDFRSFIHAVQDRLMDLPVLSMDLSTVGLNYLEEEITVDVRDEFSGTVGKGDNQILQHHVLTRIHILSFLSGLAECRLGLNDILIKGNEIVSRQDIMPTTTTKWIKLHECRFHGCVDEDVFNSSRVILFNPLDACRFELMRFRTVFAEKTLPFTLRTAASINGAEVEVQSWLRMSPGFSSNRDPLTQVPCENVMVRYPVPSEWVKNFRRDSVLGEKSLKAKVNRGASFGSAGASGSEPVMRVTLGTAKYEHAFNSIVWRINRLPDKNSASGHPHCFFCHLELGSDREVPSRFANYVNVEFSMPTTSASKAAVRSVSVEDKPDVRKWVNYSAHYSYKVEIEQKKSLKPDFEGEDLENPKECGVQ
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 3-like central domain-containing protein (H2KYN6)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein Phosphatase Four Regulatory subunit
- Nucleolar GTP-binding protein 1
- Nucleolar GTP-binding protein 2
- Forkhead box protein O
- Guanine nucleotide-binding protein-like 3 homolog
- Ribosome biogenesis protein NOP53
- Serine/threonine-protein phosphatase 4 catalytic subunit 1
- Serine/threonine-protein phosphatase 4 catalytic subunit 2
- Pescadillo homolog
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MSDTKEVSDDPMELGTSSTVIAKEENDKESLKRMEVDDEKEPEEEIVEKTEEKQEEEDVTVKLEDETETEVESVDGGQEEKEVVDEKQVDAERVNTKTEELSPKKEVKAEEDPETETKKKDPSEQTNGQVKKKSDKQSPKKKEKSEGKENSPGSKLTNRDHILDHLDIKRDATNRVKLYVLCDQRIWEDRGTGHVVTHQLSAEDGAPSNAGNTMVLVRLEGQNKNMLESRIQMDTVYQKQQETLIVWSETDVMDLALSFQEKSGCEELWQKICEVQGRDPGDPDATFDDGDDSDVGEMPSSASRLQLPPIEIGRLGELDALLHMHLTTNSAREKMTLAIENDNVVTKLCEVFRMCEDIEHTEGLRTFYSIVKNLFMLNRNTVIEMLLDDNNIKDVIGMFEFDPAYKHPRKHRDFVYKKAKFREVLNISCDELRDKIHRLYRAQYIQDACLPSLGLFEENLLSTLSSHVFFCRVDIVTLLQKDKKAMSELFGQLISEETDVIRRRDLALFLKEMISLSTSIPSNGPAATKETFFKLQLQNMFNSEILDSLEPCFKSPDHETRAVMVDVLRTMVDANAQMIRDFLLKQSKTKDKNEDVLLNMMIRHLLTDIDVHLTSGSEIVLIMKTLLDPENMTTVKSERSDFLQLFYNRCYESLLKPILENVSGGNIKKDDYMIANRQSVILRLLTFCVEHHSFSMRQRCVSNDLMNKVLVLLKSKHSFLVLSALKLLQRVVTVKDDKYIRYIVKEKVLDPVMECFRKNGNRYNIINSSVLHLFEFVRSEDVRPLIKYVVENHMEVVDSVNYVKTFKEIKIRYDQHRDREETMSVRSEDNSLASPRSFRKDRNEDQWFDEDEDLEVGTMLESIEKDSVAVSPKKEEAGQRKTGMEPMFPSLLKRKNAFDDDEAPVFGGGSAAVINNTEKKIVIKVNSDRSPSRTPSPASSPRASSSPGPSRDDEVTSSQNNKESSPTPTVKSLVDYDESDDSDDDPPSPDAVPSSSTGSPEKEGDSADGKKGDSPEYNDVSSTSNEEKFDSRNGAPVTNENGGVEAAAPTVEISRKRTSDGIDPDAKRIRTEETAPAATATVSQA
Protein: DNA-directed RNA polymerase II subunit RPB3 (RNA polymerase II subunit 3) (RNA polymerase II subunit B3) (DNA-directed RNA polymerase II 33 kDa polypeptide) (RPB33) (DNA-directed RNA polymerase II subunit C) (RPB31) (P97760)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P19387}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB2
Sequence:
MPYANQPTVRITELTEENVKFIIENTDLAVANSIRRVFIAEVPIIAIDWVQIDANSSVLHDEFIAHRLGLIPLTSDDIVDKLQYSRDCTCEEFCPECSVEFTLDVRCNEDQTRHVTSRDLISNSPRVIPVTSRNRDNDPNDYVEQDDILIVKLRKGQELRLRAYAKKGFGKEHAKWNPTAGVAFEYDPDNALRHTVYPKPEEWPKSEYSELDEDESQAPYDPNGKPERFYYNVESCGSLRPETIVLSALSGLKKKLSDLQTQLSHEIQSDVLTIN
Protein: 4-nitrophenol 2-monooxygenase, oxygenase component (EC 1.14.13.29) (4-nitrophenol hydroxylase) (4-NP hydroxylase) (Two-component 4-nitrophenol hydroxylase) (Q8RQQ0)
Organism: Rhodococcus sp
Function: Utilizes the flavins supplied by NphA2 to catalyze the degradation of 4-nitrophenol (4-NP) via 4-nitrocatechol (4-NC) which is used as the sole carbon, nitrogen, and energy source. Can also degrade phenol and 4-chlorophenol as rapidly as 4-NP.
Interaction partners:
Sequence:
MTTSAFVDDRVGVPNDVRPMTGDEYLESLRDGREVYFRGERVDDVTTHPAFRNSARSVARMYDALHQPEQEGVLAVPTDTGNGGFTHPFFKTARSADDLVLSRDAIVAWQREVYGWLGRSPDYKASFLGTLGANADFYGPYRDNALRWYKHAQERMLYLNHAIVNPPIDRDKPADETADVCVHVVEETDAGLIVSGAKVVATGSAITNANFIAHYGLLRKKEYGLIFTVPMDSPGLKLFCRTSYEMNAAVMGTPFDYPLSSRFDENDAIMVFDRVLVPWENVFAYDTDTANGFVMKSGFLSRFMFHGCARLAVKLDFIAGCVMKGVEMTGSAGFRGVQMQIGEILNWRDMFWGLSDAMAKSPEQWVNGAVQPNLNYGLAYRTFMGVGYPRVKEIIQQVLGSGLIYLNSHASDWANPAMRPYLDQYVRGSNGVAAIDRVQLLKLLWDAVGTEFGGRHELYERNYGGDHEAVRFQTLFAYQATGQDLALKGFAEQCMSEYDVDGWTRPDLIGNDDLRIVRG
Protein: Calponin-homology (CH) domain-containing protein (Q9TYW4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAQPKRLDQEEEVVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMGWIQEKREDGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIHPEIDEMSVMTYLSQFPATKPIIMKPKVQATISNLDKILQVNDPREFDLKLSRDGFKPKVSIRDEDGQDIHLSLKKVEDKENAYKVKFTPTKIGFIHVDVAANDVHTFETQTIPEASVICQVVPIARLLDYNKTAKVGDDVKFAVVDAIEGPVEAIVVDPTGKEHRMVILDGTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRGKPKNSFKVWGRGIAPEGIRKNDVVGVHVESLDPEENIANANISLEVLKPSDGSHLPVSVGYNDESQSMDFEYSPKQAPDDLEVLVKVAGEVIESHKIHVAPESSSKIRAFGAGLEGGIVNEPCVFDVEMNGESKDLSFAVEGPSKAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHIQDSPFVLRVTEPIEGLKPSATRVTGIDESKVYNVGEKIPFRVDTRLCGVDLVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAGVSVPGAPFSVKVKEPTDASKLKIFGPGVDGPVYSKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGEEISPIEINVKPNVDVSGIRVEGLENAVVTVNVEKEIHVFTTDGENTRIVITSPSGRVVEAIIESTPTGFRVRFTPSEVGNYTIDVTYQDIPIERSPFTLQSVEGPKNQDDSEILDGENQENPGDRTLAEAEYLVFGSGPPCADMVTVSGPGLGPLVAQRSTYVSIDTTNAGFGDIDVYVDGPTRTPLHCVDNQDGILKMSFTPKQPGLYYLRVMFDNEHVPGSPFQIVAVAALLGNPLDQRSKTESPYSSISSGSSSTPNPNPQACT
Protein: Immunoglobulin kappa variable 1D-16 (Ig kappa chain V-I region HK146) (Ig kappa chain V-I region HK189) (P01601)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVLAQLLGLLLLCFPGARCDIQMTQSPSSLSASVGDRVTITCRASQGISSWLAWYQQKPEKAPKSLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYNSYP
Protein: Actin-related protein 8 (hArp8) (INO80 complex subunit N) (Q9H981)
Organism: Homo sapiens (Human)
Function: Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize.
Subcellular location: Nucleus {ECO:0000269|PubMed:18163988}. Chromosome {ECO:0000269|PubMed:18163988}. Note=Specifically localizes to mitotic chromosomes.
Interaction partners:
- RuvB-like 1
- Actin-related protein 5
- RuvB-like 2
- INO80 complex subunit C
- Actin-like protein 6A
- Chromatin-remodeling ATPase INO80
- Nuclear factor related to kappa-B-binding protein
- INO80 complex subunit E
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
- INO80 complex subunit B
Sequence:
MTQAEKGDTENGKEKGGEKEKEQRGVKRPIVPALVPESLQEQIQSNFIIVIHPGSTTLRIGRATDTLPASIPHVIARRHKQQGQPLYKDSWLLREGLNKPESNEQRQNGLKMVDQAIWSKKMSNGTRRIPVSPEQARSYNKQMRPAILDHCSGNKWTNTSHHPEYLVGEEALYVNPLDCYNIHWPIRRGQLNIHPGPGGSLTAVLADIEVIWSHAIQKYLEIPLKDLKYYRCILLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDGVSHRNTRLCLAYGGSDVSRCFYWLMQRAGFPYRECQLTNKMDCLLLQHLKETFCHLDQDISGLQDHEFQIRHPDSPALLYQFRLGDEKLQAPMALFYPATFGIVGQKMTTLQHRSQGDPEDPHDEHYLLATQSKQEQSAKATADRKSASKPIGFEGDLRGQSSDLPERLHSQEVDLGSAQGDGLMAGNDSEEALTALMSRKTAISLFEGKALGLDKAILHSIDCCSSDDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRRIIENVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWIYQREWQRFGVRMLRERAAFVW
Protein: Histone deacetylase 1 (HD1) (EC 3.5.1.98) (Protein deacetylase HDAC1) (EC 3.5.1.-) (Protein deacylase HDAC1) (EC 3.5.1.-) (P56517)
Organism: Gallus gallus (Chicken)
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Also functions as deacetylase for non-histone proteins. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13547}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Histone-binding protein RBBP4
- Histone-binding protein RBBP7
- Histone deacetylase 2
- YY1 transcription factor
- SIN3 transcription regulator family member B
- DNA
- Retinoblastoma-associated protein
- Chromodomain helicase DNA binding protein 5.
- C-terminal binding protein 1
Sequence:
MALTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSAGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVISKVMETFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQPIPEDAVQEDSGDEEEEDPEKRISIRNSDKRISCDEEFSDSEDEGEGGRKNVANFKKAKRVKTEEEKEEEEKKDEKEEEKAKEEKAEPKGVKEETKST
Protein: C-C motif chemokine 4-like (Lymphocyte activation gene 1 protein) (LAG-1) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (Monocyte adherence-induced protein 5-alpha) (Small-inducible cytokine A4-like) (Q8NHW4)
Organism: Homo sapiens (Human)
Function: Chemokine that induces chemotaxis of cells expressing CCR5 or CCR1. Inhibits HIV replication in peripheral blood monocytes that express CCR5.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MKLCVTVLSLLVLVAAFCSLALSAPMGSDPPTACCFSYTARKLPRNFVVDYYETSSLCSQPAVVFQTKRGKQVCADPSESWVQEYVYDLELN