wanglab/gogpt-training-data huggingface dataset:
Protein: Purine nucleoside phosphorylase YlmD (EC 2.4.2.1) (Adenosine deaminase YlmD) (EC 3.5.4.4) (S-methyl-5'-thioadenosine phosphorylase YlmD) (EC 2.4.2.28) (P84138)
Organism: Geobacillus stearothermophilus (strain DSM 13240 / CIP 106956 / 10)
Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Interaction partners:
Sequence:
MPDIFQQEARGWLRCGAPPFAGAVAGLTTKHGGESKGPFASLNMGLHVGDDRTDVVNNRRRLAEWLAFPLERWVCCEQVHGADIQKVTKSDRGNGAQDFATAVPGVDGLYTDEAGVLLALCFADCVPIYFVAPSAGLVGLAHAGWRGTAGGIAGHMVWLWQTREHIAPSDIYVAIGPAIGPCCYTVDDRVVDSLRPTLPPESPLPWRETSPGQYALDLKEANRLQLLAAGVPNSHIYVSERCTSCEEALFFSHRRDRGTTGRMLAFIGRREEWT
Protein: Zona pellucida sperm-binding protein 4 (RC55) (Zona pellucida glycoprotein 4) (Zp-4) (Zona pellucida glycoprotein X) (Zp-X) (Zona pellucida protein B) [Cleaved into: Processed zona pellucida sperm-binding protein 4] (Q00193)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor.
Subcellular location: [Processed zona pellucida sperm-binding protein 4]: Zona pellucida {ECO:0000269|PubMed:22842159}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22842159}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 3
- Clarin-1
Sequence:
MAPGSTMWLLGYIFLCFPVSFALIKQPKPETPTDPGVLHCRPWNFKFTINFQNQETGSSPVLVTWDNQGRLHRLQNDTDCGTRVGEGPGPSVVLEANYSSCYVTESEPYYVMLVGVEEVDAAGQNLVTKQQLLKCPMHLPAPDAGLCDSVPVQDRLPCATAPISQEDCEELGCCHSSEEVNACYYGNTVTSHCTQEGHFSIAVSRNVSSPPLHLDSVHLVFGNDSECQPVVATRAFVLFLFPFTACGTTRQITGDRAIYENELLATREVRTWSRGSITRDSIFRLRVSCSYSISSSALPVDMHVLTLPPPLPETQPGPLTVVLQIAKDKDYHSYYTMDDYPVVKLLRDPIYVDVSILYRTDPYLGLRLHQCWATPRTNPLYQPQWPILVKGCPYTGDNYQTQLIPVQEAFDLPFPSHHQRFSISTFSFLDSSVAKEALKGPIYLHCSVSVCQPTGTQSCTVTCPIDSRRRNSDINFQNSTANISSKGPMILLQATEDPSEKLHKHSGVPVHPGALWVAGLSGIFIIGALLVSYVAIRTRR
Protein: Tight junction protein ZO-1 (Q8I103)
Organism: Caenorhabditis elegans
Interaction partners:
- Yes-associated protein homolog 1
- Juxtamembrane domain-associated catenin
- Afadin
- Cell junction protein VAB-9
- Uncharacterized protein.
- Beta-catenin-like protein hmp-2
- Cell death protein 3
- Guanylate kinase
- EF-hand domain-containing protein
- Rho-associated protein kinase let-502
Sequence:
MSEDPSWYKTSMSSTSSCIEEEHEPVDQDEEEMYNPSGCTWQLLSVSLHRAANLGFGIAISGGRDNPHFTSGDPVVVISDVVPNGPAWGLLQVNDRILSANQVSFENIEYSSAVDIIKNKDHIDMIVKRRVAVPMLEYEQRTLKFTLSKSRKKDDFGIVVGCKFYIKEIRNPKLAEKDPGLKEGDSVLRINGQSLEGASLEEVNKWLERSRDKLCLVIQRDVRRGTSRWPSQNTVYERVGSVAATPRHSPSPMLPHMPITQRNSHEYVNSPRHRSDGSVERRVSSPANSQLSNFNGMASSQITTQDYDCYTRQPSRSIDANGVANIMFRKVGGSVGVRVIGGNEVGIFVSAVAADSPASLHGVSCGDRILEVNGRNMRGVTRESAVQLLLGLDDRVSLRLEHARQDFEHVRANQLGDNFYIRSHFSREKRDKASPLELSINEGDIFHVTDTLFGGTVGLWQAARVYSSSENKGEPVKGVIPNQATAEQIAKEWRVYVEAKQAKSGGSGTLLRRKFESRRTKSLPKNMICDPTELNLPLPAYERVALNTPSFHRPVVLFGPLADIARHQLLTQFSARFGSPESDGGVIRLSSVDHVIASMKHCVLDISIESVERLQLAQYAPIVVFLDVDGRSKIREIRKKCNAPHLSSRKLAENGNQIKKHHSHLLSATIDATHETGWFDALRELIGHLQQRRLWMPEFPPNLPLEDVLLFPLPKWDGDVDSLKSEYVDYQDSLPRKGGEKKWDSSPLQTPGDLPSEMREYSTMPRPQHHQLGQDFGGNRNRQSSNSQSTLSTFVTTASSSNPPRPLLTPTRDESASRTTTPHGYYHVKQLLDDDSLYQDARLANEIANARLREEAKLREERVNRQRSELSPSNMQHRLDNTTPSNFDFSNVQPSNSNPVPNGRYHPLTPSSMTSSSSGASRTAGQGQQQTAPPPRPPPVNSGNSSPYTQSYIRNKWNNDGAMDARGAENQTPPVVPARTNGSASPANASISLTVSNVPTGSSIASKSPTPRLDENENGQKSEEEEPTVVEESTALIGSLGGVIRCEKSNVELRIPAGAITEGQEHEIYVKVCREGDSSPIDRSKGETLLSPLVMCGPQGLKFEKQCELRMPHTGPVTADSDGQWSFSLKTGEGGEWKHMEIEQQQATNANLDQFLTVPITHF
Protein: DNA-directed RNA polymerase subunit epsilon (RNAP epsilon subunit) (EC 2.7.7.6) (RNA polymerase epsilon subunit) (Transcriptase subunit epsilon) (Q97T34)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: A non-essential component of RNA polymerase (RNAP).
Interaction partners:
Sequence:
MIYKVFYQETKERSPRRETTRTLYLDIDASSELEGRITARQLVEENRPEYNIEYIELLSDKLLDYEKETGAFEITEF
Protein: Transcriptional activator of proteases prtT (Zn(2)-C6 zinc finger-containing protein prtT) (Q4WPQ8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Transcription factor required for protein utilization and degradation. Regulates transcription of major secreted proteases including a serine alkaline protease (alk1), a metalloprotease (mep), an aspergillopepsin (pep1), a sedolisin (sed2) and two dipeptidyl-peptidases (dppIV and dppV). However, it is not a virulence determinant in leukopenic mice.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
Sequence:
MMHIQTLRKITILDVQDKQRCLSTNQNVPDNVFQLIACWCYFPPFLSIAKIKPLIALKAGISENPVLIGCRRIKMAHCPYSEAMTRTTSVEDVKFEIPAWDNSNVDVADGSGRPESSTSGDTIRPKGRIRRSMTACNTCRKLKTRCDLDPRGHACRRCLSLRIECKLPETAERFQDNASMWSDATAAIPSIEERLISLERSMTEMTSMMRRMMDRSPSISGSSVSMLTRSGITDETASIEGSQSSSFAPRPIRLFQDLQSDFTGEANVLPADSRSLGDLFTKGIIDPKLSQKLIQLFVDHFGIWISVDNPSDIHNELRATDPLLYSTACLLASRYVPGIPLSVIHAMYLQIRHATVNVLWNKTPLKHETLQALALLALWPTAVQKETPMDSWLLSGISINHAIISFDFLNHAPSDLIVDNDMVAKLRVWNALCLTQLQSAIGNARPFHIQQRYLEHCPRLLEHPAATFEDGKIVAEIQLYLIALKLQNFSHRMRLGDFEYEEIERWKMEWAHLLKLSLWYCQLLLYRTAMRFHWESEHLISEILRNSRLILSKFLLVRFPNALAFPDQIYYIVGYAALNLCDFSPMDPLIDQVQTFLLHLSPNEDHIAYRFSYTITELKRRCATGPNPHNVVKGAFGDTRKLSMGQQIPFMNPLMDTMMGEYGGLEHLIPEVPPNSLPDMLTSVAGELQAFRTAIL
Protein: Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48) (Q12341)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- HAT1-interacting factor 1
- Histone acetyltransferase type B subunit 2
- Histone H4
- Histone H3
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
- Origin recognition complex subunit 4
- Origin recognition complex subunit 2
- Origin recognition complex subunit 6
- Origin recognition complex subunit 1
Sequence:
MSANDFKPETWTSSANEALRVSIVGENAVQFSPLFTYPIYGDSEKIYGYKDLIIHLAFDSVTFKPYVNVKYSAKLGDDNIVDVEKKLLSFLPKDDVIVRDEAKWVDCFAEERKTHNLSDVFEKVSEYSLNGEEFVVYKSSLVDDFARRMHRRVQIFSLLFIEAANYIDETDPSWQIYWLLNKKTKELIGFVTTYKYWHYLGAKSFDEDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAIIQSWLEDKSITEITVEDPNEAFDDLRDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSLKLEERQFNRLVEMLLLLNNSPSFELKVKNRLYIKNYDALDQTDPEKAREALQNSFILVKDDYRRIIESINKSQG
Protein: Carboxypeptidase (EC 3.4.16.-) (Q94269)
Organism: Caenorhabditis elegans
Interaction partners:
- C-type LECtin
- C-type LECtin
- Peptidase_M13_N domain-containing protein
- Serine protease K12H4.7
- EGF-like domain-containing protein
- Putative serine protease K12H4.7
- Putative serine protease F56F10.1
- Putative phospholipase B-like 2
- Neprilysin
- EGF-like domain-containing protein
Sequence:
MLRSLGILCLLGAALAAPSRIASKDTDLVNDLPGLSFTPTFKQYSGYLDGSQGNHLHYWLVESQTNPQTAPIVLWLNGGPGCSSLLGLLSENGPYRIQKDGVTVIENVNSWNKAANVLFLESPRDVGFSYREKSATPDLLYNDDKTATDNALALVQFFQRFPEYQGRDFYITGESYGGVYVPTLTKLVVQMIQNNTTPYINLKGFAVGNGALSRKHLTNSGIDLLYYRGMLGTTQWENLRQCCPDTLNNPLVDCDYSKYVVFDNFGNPSPRNDTNDAQAIACGKMVINLSLNSIWETYNDVYNSYQDCYNFDSSVFGAAEERHAKVHQQTMRKIMRTTLSTTGANDAYNLFSNGFNPFIDQGSLYNKMSTDALNNYPCYIDDATTAWLGRTDVRSALHIPAAAPVWQECSDDINAKYYIQQYPDTTPVFQFLVDSGYPLKVLIYNGDVDLACNYLGDQWFVENLATVSYQMTLTTPRQQWNFTRAGTQNKYIPTLAGYLKSWNYQQFSIDLLTVKGAGHMVPMDRPGPALQIFYNYLYNTNGGYSNQVPYDLTATPLRSQFLAPPQKTWTRKQADRVWNLPGITYGLNFKQYSGYLNGVTGNYLHYWFVESQGNPTTDPLVLWLTGGPGCSGLMAMLTELGPFHPNPDGKTLFENVYSWNKAANVIFLESPRGVGFSVQDPSLNNDTIWDDQRTATDTYLALKDFLTVYPEYINRPFFVTGESYGGVYVPTITSLLIDKIQSGDFAQLNLVGMSIGNGELSAIQQFNSAIMMSYFHGLFSKDDFDSLQPCCNQTKTSSQWFEYCNFAQYIHLGPDGTAIPNDKSFCANKVADLGQQRFWNSLNDVYNIYQDCYQQADRAFGSRMSIKQKKEHMRGFIDQGAKISTSSTDNQGGLACYGTTQAANWINLPDVRSALHVSSAAGAWSACNDTINGLYVQQHNDTTSVFQHILDSKYPLRVLIYNGDVDQACNYLGDQWFIEAFALKNQLPVTKPRADWRYMTQIAGYAKKFDNNAGFSVDLITVKGAGHLVPTDRPGPALQMIANFFRNQDYSNPTVIDTTLHPLKNTYVVAEQLAASLNRSSTGVAHNGNRVHVKVHKVVRAGNFAKTGEQDTVRQPTERDAPPPPPTQTKAQDEVTNLPGLTFTPNFKQYSGYLNASAGNYLHYWLVESQLNATYDPLILWLNGGPGCSSIGGFLEELGPFHVNADGKTLFENTFSWNKAGNVLFLEAPRDVGYSFRSNEFAPDTMYNDTYTASDTVLALASFFNKFPEYQNRPFYITGESYGGIYVPTLTRALINAIQTGTIKNVNLVGVAIGNGELSGIQQINSAVSLLYFRGERDKSDWDAISKCCDTSVPQAYCDYIKYVNIDTSGNVWPKVNDNSLAGQCGQLVTQQGFLDVWTTDNDVYNTFADCYTAPGAGDSKLNELASGIRRVQNRRSKRAADVSPFLPSTLFVDQAKKINYQSTDANGGFTCFSGASSENYMNLPEVRTALHIPTSLPYWTDCNDNMNENYIQQHNDTSSVFTDIFATGYPLRFLIYNGDVDMACQFLGDQWFLEKLAKDNGLAVTRQHGPWNYTQGQFLPRVGGYWKQFTYTNTAKNTKVVFDQLTVKGAGHFVPQDRPGPALQMIYNFVNQLDYNRNLTLDYSRKQLLPQYQPAPVTVPRRKADHIFSLPGVTWNVNFMQHSGYLQATRGNKLFYWFVESQSGNEGDPIILWLQGGPGCASTGGLFSEIGPFFVNPDGETLFENIYSWNKAAHILIIDSPRGVGFSYQDKNVNNDTTWDDDKTALDTYTALEDFFVTYPPHRNSELYITGESYGGVYVPTLTRLLIQKIQAGQSNIQLRGMGIGNGMVSAVNDVRTLPDFLYFHGIYDKPMWEKLRACCPSADSSGDCNYDYYITIDSGVNVIAKQFPNNQTLQDCANLVENLSYDRNWKALYDQYNLYQDCYVTPRDQANPFAMKEKFSRLDVDHKLKTSIPQAITKTAPQDPLSTDATGGYSCWSLGAINNYLSLSHVRDALHIPDSVPRWGFCNKINYANLYNDTTQVFTDILNSGYNLKVLIYNGDVDSVCSMFEAESMINNFAAAQTFVSNQPRGSWMYGGQIGGYVQKFQKNNMTIDLLTVKGAGHMSPTDRPGPVLQMMNNFVHGQGNYNTSIAVSMVRQPLLAQFLEQGIGPVGTSAPVASTSTTNTPSPTNQSPVTQAPPVTLPPPSVATAGPTGPILTVVPVSSAPTSGAVSSTTNTPSPTNQSPVTLPPPSVATAGPTGPILTVVPVSSAPTSGAVSSTATAAPVITTTKTSSVLSVSFSMFIVLITKFLL
Protein: C-type lectin BJcuL (CTL) (Galactose-specific lectin) (Snake venom galactoside-binding lectin) (SVgalL) (P83519)
Organism: Bothrops jararacussu (Jararacussu)
Function: Galactose-binding lectin which recognizes specific carbohydrate structures and agglutinates a variety of animal cells by binding to cell-surface glycoproteins and glycolipids. Calcium-dependent lectin. Also binds lactose and raffinose. Shows high hemagglutinating activity on mammalian erythrocytes. It also involved in immunological functions, since it is able of inducing potent neutrophil activation. In vivo, it causes edema and increases vascular permeability after injection into mouse hind paws (10-100 ug/paw). In anesthetized rats, it decreases the blood pressure by approximately 15%, with a rapid return to the resting level. Is an effective inhibitor of cell growth in some cancer cell lines, especially against renal and pancreatic cancer cell lines, human breast and ovarian carcinoma, glioblastoma and a bovine brain microvascular endothelial cell line.
Subcellular location: Secreted {ECO:0000269|Ref.5}.
Interaction partners:
Sequence:
MGRFLFVASSACWFVFLSLSGAKGNNCPQDWLPMNGLCYKIFNELKAWKDAEMFCRKYKPGCHLASIHLYGESPEIAEYISDYHKGQSEVWIGLCDKKKDFSWEWTDRSCTDYLSWDKNQPDHYQNKEFCVELVSNTGYRLWNDQVCESKNAFLCQCKF
Protein: Cysteine desulfurase (EC 2.8.1.7) (Cysteine sulfinate desulfinase) (CSD) (EC 3.13.1.-) (Selenocysteine beta-lyase) (SCL) (Selenocysteine lyase) (EC 4.4.1.16) (Selenocysteine reductase) (P77444)
Organism: Escherichia coli (strain K12)
Function: Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo. Can also desulfinate L-cysteine sulfinate (3-sulfino-L-alanine).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Iron-sulfur cluster assembly protein SufD
- Cysteine desulfuration protein SufE
- Probable ATP-dependent transporter SufC
- Iron-sulfur cluster assembly protein SufB
- Iron-sulfur cluster assembly protein SufA
- Iron-sulfur cluster assembly scaffold protein IscU
- Sulfur acceptor protein CsdE
- Selenide, water dikinase
- Thioredoxin reductase
- Cystathionine gamma-synthase
Sequence:
MIFSVDKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPPWEGGGSMIATVSLSEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRIHRLLG
Protein: Squalene monooxygenase SE2 (EC 1.14.14.17) (Squalene epoxidase 2) (PgSQE2) (SE2) (B7TWW5)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MELERSYRENDEYFLMFAATLLFGFVLYLFTLRRRRRRREKKGGAGSMEIINGAYKMTSSSEVNGHCTPEDIAGSSDDVIIVGAGVAGSALAYTLAKDGRRVHVIERDLTEQDRIVGELLQPGGYLKLVELGLEDCVNEIDAQRVFGYALYMDGKNTRLSYPLEKFHADVAGRSFHNGRFIQRMREKAASLPNVRMEQGTVTSLVEQKGTVKGVRYKTKNGQEMSAAYAPLTIVCDGCFSNLRHSLCNPKVDVPSCFVGLILENIDLPHINHGHVILADPSPILFYKISSTEIRCLVDVPGQKVPSIANGELAHYLKTSVAPQIPPELYKSFIAAIDKGKIKTMPNRSMPADPHSTPGALLLGDAFNMRHPLTGGGMTVALSDIVLIRDLLRPLRDLHDSSTLCKYLESFYTLRKPVASTINTLAGALYKVFCASPDKARQEMRDACFDYLSLGGICSEGPIALLSGLNPRPMSLFFHFFAVAIYGVGRLLIPFPSPRKMWLGARLISGASGIIFPIIKSEGVRQMFFPATVPAYYRAPPITKKM
Protein: Toll-like receptor 8 (CD antigen CD288) (Q9NR97)
Organism: Homo sapiens (Human)
Function: Endosomal receptor that plays a key role in innate and adaptive immunity. Controls host immune response against pathogens through recognition of RNA degradation products specific to microorganisms that are initially processed by RNASET2. Recognizes GU-rich single-stranded RNA (GU-rich RNA) derived from SARS-CoV-2, SARS-CoV-1 and HIV-1 viruses. Upon binding to agonists, undergoes dimerization that brings TIR domains from the two molecules into direct contact, leading to the recruitment of TIR-containing downstream adapter MYD88 through homotypic interaction. In turn, the Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3 leading to activation of downstream transcription factors NF-kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons, respectively.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:25297876}; Single-pass type I membrane protein {ECO:0000250}. Note=Endosomal localization confers distinctive proteolytic processing. {ECO:0000269|PubMed:25297876}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 7
- Protein unc-93 homolog B1
- Toll-like receptor 3
- Interleukin-1 receptor-associated kinase 4
- Myeloid cell nuclear differentiation antigen
- Toll-like receptor 2
- Leukocyte immunoglobulin-like receptor subfamily B member 2
- Toll-like receptor 9
- Interleukin-1 receptor-associated kinase 1
Sequence:
MENMFLQSSMLTCIFLLISGSCELCAEENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGNPGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKVCEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFPCVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSFNYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLSENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPDIACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNLKVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASLTELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSNLLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDVTAVILFFFTFFITTMVMLAALAHHLFYWDVWFIYNVCLAKVKGYRSLSTSQTFYDAYISYDTKDASVTDWVINELRYHLEESRDKNVLLCLEERDWDPGLAIIDNLMQSINQSKKTVFVLTKKYAKSWNFKTAFYLALQRLMDENMDVIIFILLEPVLQHSQYLRLRQRICKSSILQWPDNPKAEGLFWQTLRNVVLTENDSRYNNMYVDSIKQY
Protein: Uncharacterized protein (Q3TZQ0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MESKLAEEKQQTKTLSLELEVARLQLQELDLSSRSLLGTDLESVVRCQNDNYDIKESEVYISETTEKTPKQDTDQTCDKDIQQDLGLETSVTESETTRLTGEGCEEQPPKTNCEAPAEDKTQDCSECISELCSSSNVLVPMDVLEDQGSIQNLQLQKDTLNENLRLLPEVEDWDKKVESLLNEIMEADSKLSLQEVQLKMKIATCIQLEKIVKDLRKEKADLSEKLESLPCNQEVCLRVERSEEDLGFNLDMGANELLSKSTKDNATNTEDNYKEKFLDMERELTRIKSEKANIEHHILSVETNLEVVQAEKLCLERDTESKQKVIIDLKEELFTVISERNRLREELDNVS
Protein: NASP-related protein sim3 (CENP-A escort protein sim3) (Silencing in the middle of the centromere protein 3) (Q9USQ4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Histone H3 and H3-like CENP-A-specific chaperone. Promotes delivery and incorporation of CENP-A in centromeric chromatin, probably by escorting nascent CENP-A to CENP-A chromatin assembly factors. Required for central core silencing and normal chromosome segregation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18158900}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- Histone chaperone cia1
- Histone acetyltransferase type B subunit 2
- Histone H4
- Histone H3-like centromeric protein cnp1
- Histone H3.1/H3.2
- CENP-A histone chaperone scm3
- RbAp48-related WD40 repeat-containing protein prw1
- Inner kinetochore subunit sim4
- Histone-binding protein pcf3
Sequence:
MSSDTKTLENSKGNSATDADTKNPSSSDSRAIEQLVTQGNMAYAQKNYEEAVDKYGQALMQSESIHGSESLENRNVLWLYGKSLFQIAIENSQVLGNALGAKESVSQATESFEEPEAIGSFTFSGQKIENKYTVNEENSSIAHPEKESEEKETNEASPASEEDEDDFNVAWEVLDLTRVMQSKAVDAYPDSKDEKIRLADIYDLLGELSLEIENFSQASQDLKTALEWKEKVYNVSNNTLLSEAHYKLALALEFTNPEDPSNKSRACEHVEKAAEILKNVLNERENEVTDKKGKGKQKAEESTLTSDLENLREMLSELEQKTLDLKHGAPSLEEAVMSKMHESSLLSKDSSSLAQAVAEAVKNANDLGGLVKRKRTKQEVTSSSQKEGPKDKKKKD
Protein: Transcription factor GATA-6 (GATA-binding factor 6) (Q61169)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator that regulates SEMA3C and PLXNA2. May regulate genes that protect epithelial cells from bacterial infection (By similarity). Involved in gene regulation specifically in the gastric epithelium (By similarity). Involved in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions.
Subcellular location: Nucleus {ECO:0000269|PubMed:16199866}.
Interaction partners:
- LIM and cysteine-rich domains protein 1
- Homeobox protein Nkx-2.1
- Transcription factor SOX-17
- Lysyl oxidase homolog 2
- Zinc finger protein ZFPM2
- Homeobox protein Nkx-2.5
- Homeobox protein CDX-2
- Homeobox protein NANOG
- Transcription factor SOX-7
- POU domain, class 5, transcription factor 1
Sequence:
MALTDGGWCLPKRFGAAAADAGDSGPFPAREPSSPLSPISSSSSSCSRGGDRGPCGASNCRTPQLDAEAVAGPPGRSLLLSPYASHPFAAAHGAAAPGVAGPGSALSTWEDLLLFTDLDQAATASKLLWSSRGAKLSPFAAEQPEEMYQTLAALSSQGPAAYDGAPGGFVHSAAAAAAAAAAASSPVYVPTTRVGSMLSGLPYLQGAGSGPSNHAGGAGAHPGWSQASADSPPYGGGGAAGGGAAGPGGAGSATAHASARFPYSPSPPMANGAARDPGGYVAAGGTGAGSVSGGGGSLAAMGGREHQYSSLSAARPLNGTYHHHHHHHPTYSPYMAAPLTPAWPAGPFETPVLHSLQGRAGAPLPVPRGPSTDLLEDLSESRECVNCGSIQTPLWRRDGTGHYLCNACGLYSKMNGLSRPLIKPQKRVPSSRRLGLSCANCHTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMKKEGIQTRKRKPKNINKSKACSGNSSGSVPMTPTSSSSNSDDCTKNTSPSTQATTSGVGASVMSAVGENANPENSDLKYSGQDGLYIGVSLSSPAEVTSSVRQDSWCALALA
Protein: 8-demethyl-8-(2,3-dimethoxy-alpha-L-rhamnosyl)-tetracenomycin-C 4'-O-methyltransferase (EC 2.1.1.307) (O-methyltransferase III) (Q9AJU0)
Organism: Streptomyces olivaceus
Function: O-methyltransferase involved in the biosynthesis of the permethylated L-rhamnose moiety of elloramycin, an antitumor polyketide. Mediates the methylation of the hydroxy groups at the 4'-position after the sugar moiety has been attached to the aglycon.
Interaction partners:
Sequence:
MTEDARDLYLDLMKKVLTNLIYRDAPIQTFVYDGEPDADPRLLGRDWPSVAHTMVGLKRLDNLQYCVETVLADGVPGDLVETGVWRGGSSIFMRAVLRAHGDTARRVWVADSFEGMPEVGADSHAVDREMRLHEHNGVLAVPLEQVRANFERYGLLDDQVRFLPGWFKDTLPGAPTGRLAVIRLDGDLYESTTDALENLMPRLSPGGFVIIDDYAIDACRDAVHDYRGRYGISDPISEIDGTGVFWRHTAASARSLQPATV
Protein: Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12) (PSI-A) (PsaA) (P0C353)
Organism: Oryza sativa (Rice)
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00458}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00458}.
Interaction partners:
Sequence:
MMIRSPEPEVKIVVDRDPVKTSFEEWARPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTGDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALIFASLMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQIHVSLPINQFLDAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYAEFLSFRGGLDPITGGLWLSDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSTTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWVQNLHAGAPSVTAPGATTSTSLTWGGGELVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGTISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIIQGRAVGVTHYLLGGIATTWAFFLARIIAVG
Protein: SET domain-containing protein (Q584E3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFSQTRCSACIGKELYSRASTLPRDFYEACAKHFGIKMHQETFIGVRSSQIRGLFLSPSINKPLEANKPIATIPLSSLYTVTNIHTKPDTLHHVTLSNVRDAIRDVEFKAMTSQFYLGLQMSAIISSLPDITRAQNAEEMERITQILRGGAMPWVRLIDDEDFNEQFVFGMYGMALDSWQRQSYEEMTKVFHRNITSIHEKTNPPFSVDTFRRITRLILARAEHFPPLEYYNGSVLWRRVLRFVRRWSKIPEPSELCLVPLLDLVNHSNRPNCAIRIGPSAAMDGRPAITIYSIARINPGQEICRHYNFAINRPNALFRYGFLPFDLISIVEHDAIDEYLVKNQHMLREETEEAQIKRAKERAELQRLEQIFQKARSGSVPADS
Protein: Glutamate receptor interacting protein 2 (F7BQ55)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XDMLCGLSRDSSAEADDGPYSKGGKDTAGADGALVCRRQSIPEEFRGITMVELIKREGSTLGLTISGGTDKDGKPRVSNLRPGGLAARAPSWQTLYSFPPHATPKPLPPESPPGLPTKE