wanglab/gogpt-training-data huggingface dataset:
Protein: Exosporium protein B (J7T0S1)
Organism: Clostridium sporogenes (strain ATCC 15579)
Subcellular location: Spore wall {ECO:0000269|PubMed:27375261}. Note=Localizes to the exosporium. {ECO:0000269|PubMed:27375261}.
Interaction partners:
Sequence:
MSKSSEEKMENKEVLNINSFNISEFCNAEEGSNFIHFKPCEICKRAILDPINVADTSRLLQVNVALRNVCIGKELTVGCILIDRTGTVLAFKSQTFTVGHGGSGCGCSEDKHGSPCTNTSRRFSFILPTRDLCSSMDLKVKIIANYTHPCN
Protein: Acyloxyacyl hydrolase (EC 3.1.1.77) [Cleaved into: Acyloxyacyl hydrolase small subunit; Acyloxyacyl hydrolase large subunit] (O18823)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P28039}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000250|UniProtKB:O35298}.
Interaction partners:
Sequence:
MKSPWRILVVSPLLLLPLHSSTSRAHDNQPGTIRSDHYTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEEWVLKTACYMMVHVFGADIIKLFDKDVNADVVCHTLEFCKQEPGQPLCHLYPLPKESWKFTLEKARHIVKQSPIMKYTRSGAGICSLPFLAKICQKIKLAIKNSVPIKDVDSDKYSIFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDAHRDSNCNGIWGVDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTVSQMSVNSFLNLPTAVTNELDWPQLSGTTGFLDSASKIKENSIYLRLRKRNRCNHRDYQNISKNGASSRNVKSLIESLSRNQLLDHPAIVIYAMIGNDVCNGRKTDPVSAMTTPEQLYANVLKMLEALNSHLPTGSHVILYGLAHGAFLWDTLHSRYHPLGQLNKDVTYTQLYSFLGCLQVSPCPGWMSANETLRALTSERAQQLSETLRKIAASKKFTNFNLFYLDFAFQEVVEEWQKMGGQPWELIEAVDGFHPNEVALLLFADQLWEKVQRQWPDVLGKENPFNPQIEEVFGDQGGH
Protein: Prophage integrase IntS (Putative prophage CPS-53 integrase) (P37326)
Organism: Escherichia coli (strain K12)
Function: Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome.
Interaction partners:
- Prophage bactoprenol-linked glucose translocase homolog
- Prophage integrase IntF
- Prophage integrase IntD
- Response regulator inhibitor for tor operon
- DNA polymerase III subunit alpha
- Uncharacterized protein YfdI
Sequence:
MLTVKQIEAAKPKEKPYRLLDGNGLYLYVPVSGKKVWQLRYKIDGKEKILTVGKYPLMTLQEARDKAWTARKDISVGIDPVKAKKASSNNNSFSAIYKEWYEHKKQVWSVGYATELAKMFDDDILPIIGGLEIQDIEPMQLLEVIRRFEDRGAMERANKARRRCGEVFRYAIVTGRAKYNPAPDLADAMKGYRKKNFPFLPADQIPAFNKALATFSGSIVSLIATKVLRYTALRTKELRSMLWKNVDFENRIITIDASVMKGRKIHVVPMSDQVVELLTTLSSITKPVSEFVFAGRNDKKKPICENAVLLVIKQIGYEGLESGHGFRHEFSTIMNEHEWPADAIEVQLAHANGGSVRGIYNHAQYLDKRREMMQWWADWLDEKVE
Protein: Dihydrolipoyl dehydrogenase, mitochondrial (DLD) (EC 1.8.1.4) (2-oxoglutarate dehydrogenase complex component E3) (OGDC-E3) (OGDHC subunit E3) (Alpha-ketoglutarate dehydrogenase complex subunit E3) (alpha-KGDHC subunit E3) (Dihydrolipoamide dehydrogenase) (Dihydrolipoamide:NAD(+) oxidoreductase) (Glycine decarboxylase complex subunit L) (GDC subunit L) (Lipoamide dehydrogenase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex E3 component) (PDC subunit E3) (PDH complex subunit E3) (P09624)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase complex protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Aminomethyltransferase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Glycine dehydrogenase
- Glycine cleavage system H protein, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
Sequence:
MLRIRSLLNNKRAFSSTVRTLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNIIVATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIHC
Protein: Brevinin-1OKb (C0HL09)
Organism: Nidirana okinavana (Kampira Falls frog) (Babina okinavana)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P86027}.
Interaction partners:
Sequence:
FFPFVINELAKLPSLISLLKK
Protein: AT-rich interactive domain-containing protein 4B (ARID domain-containing protein 4B) (180 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p180) (Breast cancer-associated antigen BRCAA1) (Histone deacetylase complex subunit SAP180) (Retinoblastoma-binding protein 1-like 1) (Q4LE39)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4A. Involved in spermatogenesis, together with ARID4A, where it functions as a transcriptional coactivator for AR (androgen receptor) and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier. Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. Cytoplasm {ECO:0000269|PubMed:11481388, ECO:0000269|PubMed:15247124}. Note=Cytoplasmic in breast cancer cells. {ECO:0000269|PubMed:15247124}.
Interaction partners:
- Sin3 histone deacetylase corepressor complex component SDS3
- Histone deacetylase complex subunit SAP30
- Paired amphipathic helix protein Sin3a
- Paired amphipathic helix protein Sin3b
- Histone deacetylase 1
- Histone deacetylase 2
- Histone-binding protein RBBP4
- PHD finger protein 12
- Inhibitor of growth protein 1
- Histone-binding protein RBBP7
Sequence:
MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDEDEDDRKQIDELLGKVVCVDYISLDKKKALWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTAPKPDAVLKQAFEQALEFHKSRTIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYKKYLYGFEEYCRSANIEFQMALPEKVVNKQCKECENVKEIKVKEENETEIKEIKMEEERNIIPREEKPIEDEIERKENIKPSLGSKKNLLESIPTHSDQEKEVNIKKPEDNENLDDKDDDTTRVDESLNIKVEAEEEKAKSGDETNKEEDEDDEEAEEEEEEEEEEEDEDDDDNNEEEEFECYPPGMKVQVRYGRGKNQKMYEASIKDSDVEGGEVLYLVHYCGWNVRYDEWIKADKIVRPADKNVPKIKHRKKIKNKLDKEKDKDEKYSPKNCKLRRLSKPPFQTNPSPEMVSKLDLTDAKNSDTAHIKSIEITSILNGLQASESSAEDSEQEDERGAQDMDNNGKEESKIDHLTNNRNDLISKEEQNSSSLLEENKVHADLVISKPVSKSPERLRKDIEVLSEDTDYEEDEVTKKRKDVKKDTTDKSSKPQIKRGKRRYCNTEECLKTGSPGKKEEKAKNKESLCMENSSNSSSDEDEEETKAKMTPTKKYNGLEEKRKSLRTTGFYSGFSEVAEKRIKLLNNSDERLQNSRAKDRKDVWSSIQGQWPKKTLKELFSDSDTEAAASPPHPAPEEGVAEESLQTVAEEESCSPSVELEKPPPVNVDSKPIEEKTVEVNDRKAEFPSSGSNSVLNTPPTTPESPSSVTVTEGSRQQSSVTVSEPLAPNQEEVRSIKSETDSTIEVDSVAGELQDLQSEGNSSPAGFDASVSSSSSNQPEPEHPEKACTGQKRVKDAQGGGSSSKKQKRSHKATVVNNKKKGKGTNSSDSEELSAGESITKSQPVKSVSTGMKSHSTKSPARTQSPGKCGKNGDKDPDLKEPSNRLPKVYKWSFQMSDLENMTSAERITILQEKLQEIRKHYLSLKSEVASIDRRRKRLKKKERESAATSSSSSSPSSSSITAAVMLTLAEPSMSSASQNGMSVECR
Protein: GTP binding protein, putative (Q586V0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHTSSLQLRRRGAGIIGLPNVGKSTLFNALTCSQQAKTGNFPFCTIDANLARVPVADDRLRRLATFSGAHKIVDVEIDLADVAGLIEGASKGAGLGNKFLSDIRPCTILLHMVRCFESARDGFGTPTPLEDVCTIVNELVLADLEAMEKILSKQAKIRKVGDPSLVICQRVVSWLQEGKPAADMSLKTDEERQILQQYNLLSAKPMMFVLNTDESTIASGNRYTHMVESALGSERTCRVCASLEEQTSQLNSREERLLFLKEYGVDTPHGELLLRRAYKLLRLQSFFTIGPQMAHGWTTRVGATAKEASGEIHSDMEQHFHRAKIMAWDKFIEQPNLEAAELKMAYVDATYTMQDGDIMIVEHGASR
Protein: Cytoplasmic polyadenylation element binding protein 3, isoform CRA_a (cDNA FLJ61637, highly similar to Homo sapiens cytoplasmic polyadenylation element binding protein 3 (CPEB3), mRNA) (Q5QP71)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQDDLLMDKSKTQPQPQQQQRQQQQPQPESSVSEAPSTPLSSETPKPEENSAVPALSPAAAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPAAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPAPQPAQPAQPPQAQPPQQRRSPASPSQAPYAQRSAAAAYGHQPIMTSKPSSSSAVAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWMEDNAFRTDNGNNLLPFQDRSRPYDTFNLHSLENSLMDMIRTDHEPLKGRMGINFHHPGTDNIMALNSRSSLFPFEDAFLDDSHGDQALSSGLSSPTRCQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRHVPFRWS
Protein: Stromal cell-derived factor 2-like protein (AtSDF2) (SDF2-like protein) (Q93ZE8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. May be involved in the quality control of glycoproteins. Forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:19763086}.
Interaction partners:
- DnaJ protein ERDJ3B
- Calreticulin-3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- UDP-glucose:glycoprotein glucosyltransferase
- Heat shock 70 kDa protein BIP1
- Heat shock 70 kDa protein BIP3
- Calreticulin-1
- DnaJ protein ERDJ2A
- Probable protein S-acyltransferase 12
- LRR receptor-like serine/threonine-protein kinase EFR
Sequence:
MALGFFCLAIFLYLSLDPDSGYTSASAAASGKEGVEITYGSAIKLMHEKTKFRLHSHDVPYGSGSGQQSVTGFPGVVDSNSYWIVKPVPGTTEKQGDAVKSGATIRLQHMKTRKWLHSHLHASPISGNLEVSCFGDDTNSDTGDHWKLIIEGSGKTWKQDQRVRLQHIDTSGYLHSHDKKYQRIAGGQQEVCGIREKKADNIWLAAEGVYLPLNESSK
Protein: ATP-dependent clpX-like chaperone, mitochondrial (EC 3.6.4.10) (ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial) (Caseinolytic mitochondrial matrix peptidase chaperone subunit) (Q9JHS4)
Organism: Mus musculus (Mouse)
Function: ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through up-regulation of heme biosynthesis (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:22710082}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:O76031}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
- Mitochondrial disaggregase
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Lon protease homolog, mitochondrial
- Lon protease homolog 2, peroxisomal
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Mitochondrial inner membrane m-AAA protease component AFG3L1
- 10 kDa heat shock protein, mitochondrial
- 60 kDa heat shock protein, mitochondrial
Sequence:
MSSCGACTCGAAAARLLTTSLTSAQRGISCGRIHVPVLGRLGTTLDAQALRRAPLRTFSETPAYFASKDGANKDGSGDGNKKSVTEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEAEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQMPQEKRGGEVLDSSQDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNVLFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPSKESSEEEYDSGVEEDGWPRQADAANS
Protein: Transmembrane protein 184A (Q1RMW2)
Organism: Bos taurus (Bovine)
Function: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26769966}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26769966}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:26769966}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q3UFJ6}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000250|UniProtKB:Q3UFJ6}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q3UFJ6}. Note=Colocalizes with CAV1. {ECO:0000269|PubMed:26769966}.
Interaction partners:
- Transmembrane protein 190
Sequence:
MTDTPGLLGTPLAWTPPARPAGPQMERAGNGSQGPGPLFLTSPLARGVSGVFVWAALVLTGHQIYLHLRSYTVPHEQRYIIRLLFIVPVYAFDSWLSLLLLGGHQHYIYFDSVRDCYEAFVIYSFLSLCFQYLGGESAIMAEIRGKPVRTSCFHGTCCLRGMTYSIGFLRFCKQATLQFCIVKPIMALVTIVLQAFGKYHDGDFNVRSGYLYITLVYNASVSLALYALFLFYSATRELLQPFEPVLKFLTIKAVIFLSFWQGLLLAILERCGVIPEVQVIDGSTVGAGTVAAGYQNFIICIEMLFASIALRYAFTCQVYSEKTESSPAPSAPMQSISSGLKETMSPQDIVQDAIHNFSPAYQKYTQQATQEAPRPGQGSVPSPRTPTHSPDGGPGGGRKGRNVEKRMLIPAEEL
Protein: DIRAS family, GTP-binding RAS-like 1 (GTP-binding protein Di-Ras1a) (Q803Y2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MPEQSNDYRVVVFGAGGVGKSSLVLRFVKGTFRDTYIPTVEDTYRQVISCDKSVCTLEITDTTGSHQFPAMQRLSISKGYAFILVYSITSRQSLEELKPIYQQVLAIKGNVENIPIMLVGNKSDETQREVETKEGEAQANTWKCAFMETSAKTNTNVKELFQELLNLDKKRDMSLNMRSSKQRRADKLKAKCSVM
Protein: Rab-GAP TBC domain-containing protein (Q38F17)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMTKTYGSKNPSSNVPLHLAGPPPFAFSDGRAPTRGNMRSFPTPSSAGLSSSVHLPPRSQGSDRRSFVLSEISGASDQLLRTLHRELCNLSAHTESGVSRSCRGESTNRDSASPSRANITGHGFDEQAPISQLSSEEVRTALSLIIHKQNLDLKSRHQRLRQLAEENKKGDTMGTSSDGGVLNEPCCLVLHRILAEARRRWMRILSSRVQGLKKELPVREHPQSNDAHTTSGVSNANALDDSISGVDSDEEMEWSVEHLYETLVSGLNSTVTEELIVTEILGGDTTALHDGIDAFGLLTVFRAPVQAMLVQHQEALAPSLSTLRQYFAALHPSAGCPRAHGSASRAAACSAYSQLNDFLNPGGSTPKSVAAALRRGASPSMRRLLYARALQLQLVVLEGGSTNNAPGELHGSNCGDVIGRCVSFGTSRNLESMRRRVHHKYAVKGMEVTVKVLQAVVKVDNMQSVGDSDRYFIFLDETEALGTTLIVDKDVSDVHLKSTLAQLGRPPEQIESYLVYLLHADVPSADAGQQRTQQQHQQTKTQHLLPSGFFPVEKCTLLIAPICYITGDTTEQYSLVVALFGQLWCRLQGPTPELAQCCWIFESLVVRFAAPACLHATRALRYPPLRLALRWMMTAFADVLEPNELLNLWDLVLSYHIEEVFSGHTSLSLPMCACGRSRGSQRLLPAPCALWLLPIVAASIFVYRAPLVERCGTAEEMLLLFTTGHHLRCRPLLQYLLFMAK
Protein: Pleckstrin homology domain containing A7 (A0A1B0GTN9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XPNPHMSKQDRNQRPSSMVSETSTAGTASTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNPNVPVVVRGWLHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKYSFKAVHTGMRALIYNSSTAGSQAEQSGMRTYYFSADTQEDMNAWVRAMNQAAQVLSRSSLKRDMEKVERQAVPQANHTESCHECGRVGPGHTRDCPHRGHDDIVNFERQEQEGEQYRSQRDPLEGKRDRSKARSPYSPAEEDALFMDLPTGPRGQQAQPQRAEKNGMLPASYGPGEQNGTGGYQRAFPPRTNPEKHSQRKSNLAQVEHWARAQKGDSRSLPLDQTLPRQGPGQSLSFPENYQTLPKSTRHPSGGSSPPPRNLPSDYKYAQDRASHLKMSSEERRAHRDGTVWQLYEWQQRQQFRHGSPTAPICLGSPEFTDQGRSRSMLEVPRSISVPPSPSDIPPPGPPRVFPPRRPHTPAERVTVKPPDQRRSVDISLGDSPRRARGHAVKNSSHVDRRSMPSMGYMTHTVSAPSLHGKSLEELSLLLTRLRRHQAKLASVRNFAISQLLQHQLTFPTCQADDTYLQLKKDLEYLDLKMTGRDLLKDRSLKPVKIAESDTDVKLSIFCEQDRVLQDLEDKIRALKENKDQLESVLEVLHRQMEQYRDQPQHLEKIAYQQKLLQEDLVHIRAELSRESTEMENAWNEYLKLENDVEQLKQTLQEQHRRAFFFQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVTSPLQSPTKAKPKVQEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDRELGQCVNGDSRVELRSYVSEPELATLSGDMAQPSLGLVGPESRYQTLPGRGLSGSTSRLQQSSTIAPYVTLRRGLNAESSKATFPRPKSALERLYSGDHQRGKMSAEEQLERMKRHQKALVRERKRTLGQGERTGLPSSRYLSRPLPGDLGSWKREQDFDLQLLERVVQGEKKDKEENGWLKVQAMPVTELDLEPQDYDLDISRELSKPEKVSIPERYVELDPEEPPSLEELQARYRKAEKIRNILARSSMCNLQPTSGQDQNSVADLDLQLQEQERIINISYALASEASQRSKQVAGPVDLSLTLKPRPFVVGSRAHATPACQMGHLVLQELMRSLTHRLIPVCPI
Protein: Sperm protamine alpha isoform 1 (Scombrine alpha-1) (P83264)
Organism: Scomber scombrus (Atlantic mackerel) (Scomber vernalis)
Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:9530815}. Chromosome {ECO:0000269|PubMed:9530815}.
Interaction partners:
Sequence:
MPRRRRRASRPVRRRRRARRSTAVRRRRRVVRRRR
Protein: Golgi reassembly stacking protein (Q54C46)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}.
Interaction partners:
- WD40 repeat-containing protein smu1
- Acyl-CoA-binding protein
- Probable serine/threonine-protein kinase PLK
- FK506-binding protein 5
Sequence:
MGQQQSQSQQIFENNPYNKNGYHVLQVHPNSPSTGKLVPFFDFIVAANQVIFEKEDSRFSDTFKSNIGKSVQLIVYNIKSDTTREVSITPSTTWGGQGLAGISIRYCSWEKTLENVWHVLDVYLNSPAHEAELQTRLDYIVGTPDLILNEQEDFFTLINNNMYRPIQLYVYSSLTEQIRLVTITPNKNWGGSGSLGCDIGFGLLHRIPTKQMLTSPMINHNSQQQQPQQQQPPQIQQQQQSPQPPQIQQQQQQQQQINAQQPIHPSPIHIQQQVQQQNQFLTPQKEDTNPITKNEEQQPIKFDLSEQLLNAPTVVTSNDNQFSKVQL
Protein: Uncharacterized protein (Q57X63)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTRGQNDTLRDVEQDTTRMHTGVKLSKEDERMLDDRINANTLVYPKQALIIVAAIASFQPVYLSHAVNGLDWINPINAFLYLVIATFTAYMLSQAYTVMVESEFWRQQRHYSEVSKGDEKLLHKYRLQVAVGYTLFFVNSVFSLLCTLLHVYILRHSDPRVSFMLSPTLTAALLWLVAQKNEESRQRRMARHK
Protein: Sporozoite and liver stage asparagine-rich protein (Q8IHP9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Transcription initiation factor TFIID subunit 7, putative
- Histone H4
Sequence:
MRKGKPRHVPMFLRSENKRIFFSFFSYFMPKNDLNFIFEHFDIGLIVLTKIHNIRKKYEEERNNMKNEEDKSDGDDMKIFDEKLKNFFLNYKINPNIEESNDTKISKKEKNNNNKKKKRNYPLNNECKQNNVNKKVMNKSNSCPLNKKNEKKQDIIDDKKKNKLHDMNNERDCNINKEINNDIQKMYMYNNEQGKTHNLDIQSYMPYDQQKGKENQEPSLYKCDEILKMNSTTEDRNKKEDVSKGKKKKINNTPQSYNTPQSYNTPQSYNTPQSYNTTQNYNTTQNYNTTQNCNTTQNYNTTQNYNTTQHNNNINENNDDDKIIIDEENCLNTIKHNEREMNNNIQKTKSCEDNQYLINYNGNNEMSYNHKHLTLLDNKNEEQENAFILNNMNKTKNGINIKENIEHIKDNKKDEIKIERETDDIYISMKKKNETYKKFSKRMNRRKISELVNYHDDYCFYITDLCKKGTMLSLKKNELFNQKNDKINILSSVKYFNKPIQFNQINWNLNNLCTINNIYTKLYDEHINDKINTTPNMQTIIKEKYSQTSSVILGNEQIQNGYQTSNLNINSNDIRIINHNKNDDISINHNNNNDISINHNNNNDISINHNNNNDISINHNNNNDISIINHNNNNDISINHNNNNNNYYFMNNYMHNNINNNYYCYYMNNTNHVNNYYNNIYIQNNHDQNNAPILQPINNHLAHINDLCYIHSEKNEYTKISKNHQMNNINPQQSNGKNQNDISNNINKNDEYYNLNEQKILCDKNKSYIKCDIPQKCDNTQDDENSEQNQNYITNPSNGHYKIKEQMNYVQHIPDYEHDNTTNEMINTQNYTNINLDPYIMNNQNDNNVYLNQNYFDTEKKNKEEDINITEANTHYNNVHIYQNNSNHMNKMINLNNNTNSKSTQDYDLYHNNMENFNNTNYNIMKEKIHINDDTSSVINNSSINSQNNLCNNKKTNNDYQNRNIKNDNSIPDSSINMNELKNNIQMNDYYASNIYNNNNNNNNNNFIISNNIISNYNNYMNESNVYPQINSNNYIPYIDPHLNNEPYKHTINNQLNKNCINNNISMDDNVYDSNTISIHISVNDNEYNNSNFTNDMYNNNNNNNNNNNNCNNSSNSNSNSNQVCLYMPNHELYNSNYNITQHMPSSNDVPKIQKHIANNIIMNGHKEEHIIEKKSKEETNKTNEQVYRSINQNNTLILKENEIDENDINTLNQNLNIKNDMNNMDNIINLKNLNNINNIYTPYQNNILKNNEIQFLNNNKEVITKHAYTHSSNEININVYKNIDTQINIRKNENNNDIIINKEQKDISTNNEQNQTYNYITSSVKNEYSILDNSPTDKNYKKNLNLNISSSYNTNDHINNYHDDIDKTNKDNKYEEEKHKDINIYINNINSNGNKNHNFINSYFDLNENEKKKKINIFYHDNKSLKNISNEELTNTNPYKCINNTIDNNNDHKNGYIELNEINNSIMNNDEKIITAYLNNRVVQNGLSHDILNEDVSINTHSNKENKNDNHNNNSNNSNNSSRSNNHNNNNNSNNNYANSYNVKNDLQINNNNYSYIKNEKNVHQTFNENNILYKHYSNHVHNYITKNTIQEQKNIHSDNKYETCSLPEKKNIYEPNSQNSPNSQKLPNSQNLSNSQNLPNSPNLPNSQNLPNSPNLPNCFTYVNNQTDILISNLVVQEQKLNDQKKEMRSNNNINNTKWNNAYNNEVQHVNNNIVNEEINILPYPSKNENNLNEHNSNIYHDKNNQHDIRTYYNDSTKITNKLHIESGNNKLTNDAIHTNNEYTINSRYPICQNYSAITAPEKMNCPQMMANHNFNNIPEYVIQNNHVNVDGNNKNDPIDNNNNNDNDNIEIFNIQQTKQIKYNNNTTDTNNNSLIHNVENNYNTDGLDISNISYNNYTNNNMYNLNNDNINNNYMPQNYYHINYNNIATSENNQLIQINNYNINTNINDININTHVNSYKENDKKNILYNNNINNMNNDNINHDHYKYICNSNSNNNNNNNNNNNNNNNNDHYYYYNCCRNEEYKYNDNNYINIQNKKNNIVNDNTSNIIKSQYNNTNKNMILEQHNINMNEDNYNQINSNLCLLKNDSISTCCDNINNNNNNNNNKYSNNEINSNEYLYYKFDEQYDKKNNVSAMCDNIKNKQHYNNYVAYNTNGSYENMSNFSSNNVYVNNKCPSYNNNNMNNMNNMNNNNCYNYHGYNVMNTKYNKAGNKFSSVQIDTQMDNPIHVDKNKNDDILERNIKGSIINNNNDSNDDNNNDDNNNDNNNNDNASNNNNDTNNINYLMNIKNTNNFDSTNNFDSTNNFDSTNNFDSTNNFDSTNNFNNRNNFNNRNNFNNRNNFEHINNINKIHHIDNENNLCREDENNHNTILTNVKNTTNKEYINICTDHLNLLKNYNLNNYINLLKINKLNDYYYNSIINKSQDGTCNTFLQNSLNNQSNIIQNNNIYENNQRIQLYNYPSFETYNNNIINTWNQKNTNNSYNSYIPLSNVQCNWKNHIFNVTQNNAHINDNKEYNYQKYPYVYNNQILSINHGKKETNTLNYLNCTGENEITYLNDLNSNEQNYNDHNKNNNPYNHDHNIIYNDVYNHMNPSYIYNNICTPTNFIQDLIKTNKINNNSNYLNIFNNMIHLQNMHNENNHLFKKEKCDQAKPYSNTDVLCTLKNNNLNENKNVNIINTIPHTLNNYYNFHILLNILRRKQLYHNSFNQLISKMTKNYNINANNNNNNDNSNLNNNNNNVRYNKRNYSISSVGFSNRSKRWTICPSYICCNSALCRFKLTCNFKFLQFNQAYNTFNIPYAIYNCYKNIMNNYHYFTSTLCPQQTYLSKHSAQEHETIFNVYWHLLNNEKYKYIQNIILFLDSNLYTRAVWLLKKGYNMNDIEVQKAEKKLIKLMLLVFKFTYDYKNDNNKYEYIKSFLYSLRNNHINFEIMNRFLFY
Protein: Plastocyanin major isoform, chloroplastic (DNA-damage-repair/toleration protein DRT112) (P42699)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. Seems to be the major plastocyanin in Arabidopsis.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11034343, ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}; Peripheral membrane protein {ECO:0000269|PubMed:11034343}; Lumenal side {ECO:0000269|PubMed:11034343}. Note=Loosely bound to the chloroplast thylakoid inner membrane surface (PubMed:11034343).
Interaction partners:
- Photosystem I reaction center subunit III, chloroplastic
- Plastocyanin minor isoform
- Photosystem I reaction center subunit psaK, chloroplastic
- Oxygen-evolving enhancer protein 3-1, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Oxygen-evolving enhancer protein 2-1, chloroplastic
- Photosystem I reaction center subunit IV A, chloroplastic
- Cytochrome f
- At2g26500)
- Photosystem I reaction center subunit XI, chloroplastic
Sequence:
MASVTSATVAIPSFTGLKASTIKSSATVRIQTAAVASPKLTVKSSLKNFGVAAVAAAASIALAGNAMAIEVLLGGGDGSLAFIPNDFSIAKGEKIVFKNNAGYPHNVVFDEDEIPSGVDVAKISMDEQDLLNGAGETYEVALTEPGTYSFYCAPHQGAGMVGKVTVN
Protein: Cytochrome c (Q4X0L0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- quinol--cytochrome-c reductase
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 6, mitochondrial
Sequence:
MGKEEGFAPGKHTLIFPFLQCPRFTLIGTCHHSLRNCGVFSWYRNRRISSSQFKIFSNRCLPFPRDAKKGAKLFQTRCAQCHTVESGGPHKVGPNLHGLFGRKTGSAEGYAYTDANKQAGVTWDENTLFSYLENPKKFIPGTKMAFGGLKKAKERNDLITYVFLSKTHSTMVGIAGANFFSPTATSRRTAKHVRPEKSLVSSTLSGKLCRADSPVVKADARHVHRTRHVLYYNLD