wanglab/gogpt-training-data huggingface dataset:
Protein: Septin homolog spn4 (P48009)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in the cell cycle. Involved in a late stage of septum formation leading to the separation of the daughter cells.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:15385632}. Note=Localizes to the medial ring at the cell cortex of dividing cells.
Interaction partners:
- Septin homolog spn2
- Septin homolog spn1
- Septin homolog spn3
- Septin homolog spn7
- Septin homolog spn5
- Septin homolog spn6
- Septin ring organizing protein mid2
- Chromosomal passenger complex protein bir1
Sequence:
MNEEETNFVGIADLPNQRHKIVSRNGVAFTLMLCGESGLGKTTFCNTLFSTTIKSHMGPEKVRAKHAEKTVEIEITKAELEEKNFHLRLTVIDTPGFGDFINNSGCWESVVEFIEDQHESYMRQDQQPDRRKIIDMRIHACLYFLRPVRNGVRPMDLEAMKHISKRVNLIPVIAKADMYTRRDLALYKTRISQVLEYHQVNVYKPNMDEGDPVFHRQIQGIINCMPFAIVGSEDDIRTPDGRVVKGREYPWGIVEIENEEHCDFKQLRNILIRSCMLDLIQTTEEKLYEQYRQEQMKVRQYGEPKLRTIDNAKFKEEEENLRKRFTEQVRVEETRFRQWEQRLIAERDSLNKDLEAQHVQIKQIELEIERLKAATSSRKR
Protein: Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase (EC 2.7.8.33) (UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase) (Undecaprenyl-phosphate GlcNAc-1-phosphate transferase) (P0AC78)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). It is the first lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis, and an acceptor for the addition of subsequent sugars to complete the biosynthesis of O-antigen lipopolysaccharide (LPS) in many E.coli O types. The apparent affinity of WecA for the polyisoprenyl phosphate substrates increases with the polyisoprenyl chain length. WecA is unable to utilize dolichyl phosphate (Dol-P).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000269|PubMed:11700352, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:17237164}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02030}. Note=Localizes to discrete regions in the plasma membrane. {ECO:0000269|PubMed:17237164}.
Interaction partners:
- UDP-N-acetylglucosamine 2-epimerase
- ECA polysaccharide chain length modulation protein
- UDP-N-acetyl-D-mannosaminuronic acid transferase
- UDP-N-acetyl-D-mannosamine dehydrogenase
- Lipid III flippase
- dTDP-4-amino-4,6-dideoxygalactose transaminase
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
- Putative O-antigen transporter
- Probable ECA polymerase
- O-antigen ligase
Sequence:
MNLLTVSTDLISIFLFTTLFLFFARKVAKKVGLVDKPNFRKRHQGLIPLVGGISVYAGICFTFGIVDYYIPHASLYLACAGVLVFIGALDDRFDISVKIRATIQAAVGIVMMVFGKLYLSSLGYIFGSWEMVLGPFGYFLTLFAVWAAINAFNMVDGIDGLLGGLSCVSFAAIGMILWFDGQTSLAIWCFAMIAAILPYIMLNLGILGRRYKVFMGDAGSTLIGFTVIWILLETTQGKTHPISPVTALWIIAIPLMDMVAIMYRRLRKGMSPFSPDRQHIHHLIMRAGFTSRQAFVLITLAAALLASIGVLAEYSHFVPEWVMLVLFLLAFFLYGYCIKRAWKVARFIKRVKRRLRRNRGGSPNLTK
Protein: ATP-dependent 6-phosphofructokinase, liver type (ATP-PFK) (PFK-L) (EC 2.7.1.11) (6-phosphofructokinase type B) (Phosphofructo-1-kinase isozyme B) (PFK-B) (Phosphohexokinase) (P17858)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase, muscle type
- Fructose-bisphosphate aldolase A
- ATP-dependent 6-phosphofructokinase, platelet type
- Fructose-bisphosphate aldolase B
- Transaldolase
- Fructose-bisphosphate aldolase C
- Fructose-1,6-bisphosphatase 1
- Hexokinase-1
- Fructose-1,6-bisphosphatase isozyme 2
Sequence:
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDGSLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQKAMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFSPVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
Protein: Mitochondrial inner membrane protein Mpv17 (Protein Mpv17) (P39210)
Organism: Homo sapiens (Human)
Function: Non-selective channel that modulates the membrane potential under normal conditions and oxidative stress, and is involved in mitochondrial homeostasis. Involved in mitochondrial deoxynucleoside triphosphates (dNTP) pool homeostasis and mitochondrial DNA (mtDNA) maintenance. May be involved in the regulation of reactive oxygen species metabolism and the control of oxidative phosphorylation (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16582907, ECO:0000269|PubMed:16582910}; Multi-pass membrane protein {ECO:0000269|PubMed:16582907, ECO:0000269|PubMed:16582910}.
Interaction partners:
- Deoxyguanosine kinase, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- DNA polymerase subunit gamma-1
- Mpv17-like protein 2
- Mpv17-like protein
- Ribonucleoside-diphosphate reductase subunit M2 B
- Twinkle mtDNA helicase
- MICOS complex subunit MIC60
- Glycogen debranching enzyme
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MALWRAYQRALAAHPWKVQVLTAGSLMGLGDIISQQLVERRGLQEHQRGRTLTMVSLGCGFVGPVVGGWYKVLDRFIPGTTKVDALKKMLLDQGGFAPCFLGCFLPLVGALNGLSAQDNWAKLQRDYPDALITNYYLWPAVQLANFYLVPLHYRLAVVQCVAVIWNSYLSWKAHRL
Protein: Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) (Q9NF11)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364099}.
Interaction partners:
- Purine nucleoside phosphorylase
- AMP deaminase
- Adenylosuccinate synthetase
- Adenine phosphoribosyltransferase
- Probable GMP synthase
- Bifunctional purine biosynthesis protein ATIC
- GMP reductase
- Inosine-5'-monophosphate dehydrogenase
- Adenylosuccinate lyase
- guanylate kinase
Sequence:
MAPTRAVIPDDFELPVDAFDIPICYDGDLSGVVIPEGLVRDRVRRLAKDIHAEIGNKPIALLCVLKGSYKFFTALVEELTNARSSCPEPMTVDFIRVKSYEDQMSTGQIQIMGLSNLDELKGKSVLVVDDISDTGRTLAKLLSTLHETGVEKTWTALLLSKRVKRVVDVPEDFVAFEIPDKFIVGYGLDYNQKFRDLGHICVMSPAGIEKYKSE
Protein: Cyclin-dependent kinase 4 (EC 2.7.11.22) (Cell division protein kinase 4) (PSK-J3) (P35426)
Organism: Rattus norvegicus (Rat)
Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
Interaction partners:
- G1/S-specific cyclin-D1
- Cyclin-dependent kinase inhibitor 1B
- G1/S-specific cyclin-D2
- G1/S-specific cyclin-E1
- Cyclin-dependent kinase 4 inhibitor C
- G1/S-specific cyclin-D3
- Cyclin-dependent kinase 4 inhibitor B
- Cyclin-dependent kinase inhibitor 1
- Retinoblastoma-associated protein
- Cyclin-A2
Sequence:
MATTRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGAAGGGLPVSTVREVALLRRLEAFEHPNVVRLMDVCATSRTDRDIKVTLVFEHIDQDLRTYLDKAPPPGLPVETIKDLMRQFLSGLDFLHANCIVHRDLKPENILVTSNGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPREVSLPRGAFSPRGPRPVQSVVPEMEESGAQLLLEMLTFNPLKRISAFRALQHSYLHKEESDPE
Protein: Ropporin-1-like protein (ROPN1-like protein) (AKAP-associated sperm protein) (Q96C74)
Organism: Homo sapiens (Human)
Function: Important for male fertility. With ROPN1, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9EQ00}. Cell projection, cilium {ECO:0000269|PubMed:27120127}.
Interaction partners:
- Sperm surface protein Sp17
- A-kinase anchor protein 3
- Calcium-binding tyrosine phosphorylation-regulated protein
- Rhophilin-1
- Radial spoke head protein 3 homolog
Sequence:
MPLPDTMFCAQQIHIPPELPDILKQFTKAAIRTQPADVLRWSAGYFSALSRGDPLPVKDRMEMPTATQKTDTGLTQGLLKVLHKQCHHKRYVELTDLEQKWKNLCLPKEKFKALLQLDPCENKIKWINFLALGCSMLGGSLNTALKHLCEILTDDPEGGPARIPFKTFSYVYRYLARLDSDVSPLETESYLASLKENIDARKNGMIGLSDFFFPKRKLLESIENSEDVGH
Protein: Regulatory protein RapF (P71002)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the regulation of genetic competence development. Inhibits the activity of ComA, a transcriptional factor that regulates the development of genetic competence. Acts by binding to ComA, leading to the inhibition of its DNA-binding activity. May also affect transcription independently of ComA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- RapF inhibitor
- Transcriptional regulatory protein ComA
- Competence and sporulation stimulating factor
- Sporulation initiation phosphotransferase F
- RapK inhibitor
- Surfactin synthase subunit 1
- Phosphatase RapH inhibitor
- Phosphatase RapA inhibitor
- Phosphatase RapE inhibitor
Sequence:
MTGVISSSSIGEKINEWYMYIRRFSIPDAEYLRREIKQELDQMEEDQDLHLYYSLMEFRHNLMLEYLEPLEKMRIEEQPRLSDLLLEIDKKQARLTGLLEYYFNFFRGMYELDQREYLSAIKFFKKAESKLIFVKDRIEKAEFFFKMSESYYYMKQTYFSMDYARQAYEIYKEHEAYNIRLLQCHSLFATNFLDLKQYEDAISHFQKAYSMAEAEKQPQLMGRTLYNIGLCKNSQSQYEDAIPYFKRAIAVFEESNILPSLPQAYFLITQIHYKLGKIDKAHEYHSKGMAYSQKAGDVIYLSEFEFLKSLYLSGPDEEAIQGFFDFLESKMLYADLEDFAIDVAKYYHERKNFQKASAYFLKVEQVRQLIQGGVSLYEIEV
Protein: Formyltransferase/hydrolase complex subunit D (Ftr complex) (EC 2.3.1.101) (Formylmethanofuran--tetrahydromethanopterin formyltransferase) (Ftr) (H4MPT formyltransferase) (Q49118)
Organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens)
Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the intermediate formylmethanofuran (formyl-MFR). Catalyzes the transfer of a formyl group from 5-formyl-H(4)MPT to MFR to produce tetrahydromethanopterin (H(4)MPT) and formyl-MFR, which is then hydrolyzed to formate and MFR.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00579}.
Interaction partners:
- Formyltransferase/hydrolase complex Fhc subunit C
- Formyltransferase/hydrolase complex Fhc subunit B
- Formyltransferase/hydrolase complex Fhc subunit A
- Methenyltetrahydromethanopterin cyclohydrolase
- 5,6,7,8-tetrahydromethanopterin hydro-lyase
- Formaldehyde activating enzyme-like protein
- Formaldehyde activating enzyme-like protein
- NAD
- Bifunctional protein MdtA
- Ribofuranosylaminobenzene 5'-phosphate
Sequence:
MSDFTLNGIKVEDTFAEAFDVAGTAIIVTNDTPKWAMIAATVMTGFATSVIGCGAEAGIDAELSPDETPDGRPGVRILLFGFEPNGLKDQLLKRVGQCILTCPGTACFAGVEGPTKIKLGGAIRYFGDGFAVAKRLPDHEGKMRRYWRIPVMDGEFLCEDSVRAVDGAVGGGNLLFLGRKHADTLIVAEIAVEAAKAIPGAILPFPGGIVRSGSKVGGRTKGMMASTNDAYCPTLKGRAGSALPPECGVVLEIVIDALTSAAVAESMRAALHAATEIGAQHGLVAVTAGNYGGNLGRHHYHLRDLLEKPAA
Protein: Nitrogen regulatory protein DAL80 (Regulatory protein UGA43) (P26343)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negative regulator of multiple nitrogen catabolic genes including the allantoin pathway genes.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional activator protein DAL81
- Transcriptional regulator URE2
- Allantoinase
- Protein DAL82
- Ureidoglycolate lyase
- Urea amidolyase
- Allantoicase
- GABA-specific permease
- Transcriptional activator protein UGA3
- General amino-acid permease GAP1
Sequence:
MVLSDSLKLPSPTLSAAAGVDDCDGEDHPTCQNCFTVKTPLWRRDEHGTVLCNACGLFLKLHGEPRPISLKTDTIKSRNRKKLNNNNVNTNANTHSNDPNKIFKRKKRLLTTGGGSLPTNNPKVSILEKFMVSGSIKPLLKPKETVPNTKECSTQRGKFSLDPCEPSGKNYLYQINGSDIYTSNIELTRLPNLSTLLEPSPFSDSAVPEIELTWKLHNEEEVIKLKTKISELELVTDLYKKHIFQLNEKCKQLEVELHSRASVQSHPQH
Protein: Ankyrin repeat domain-containing protein 2 (Skeletal muscle ankyrin repeat protein) (mArpp) (Q9WV06)
Organism: Mus musculus (Mouse)
Function: Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress.
Subcellular location: Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, cytosol. Nucleus. Nucleus, PML body {ECO:0000250}. Note=In the sarcoplasm of differentiated striated muscle cells, where it is cytosolic and enriched in the I band. In nucleus and PML bodies of proliferating and undifferentiated myoblasts. Associates with the euchromatin in the nucleus of myocytes upon muscle stress.
Interaction partners:
- Titin
- Telethonin
- Cysteine and glycine-rich protein 3
- Myopalladin
Sequence:
MEGPEAVQRATELIEQRLAQEEETEKLRRSAPGKLSMDMLVLEEEKRLGVQSPALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAAAQEPPPEPEEITGPVNEETFLKAAVEGKMKVIDKYLADGGSADTCDEFRRTALHRASLEGHMEILEKLLENGATVDFQDRLDCTAMHWACRGGHLEVVRLLQSRGADTNVRDKLLSTPLHVAVRTGHVEIVEHFLSLGLDINAKDREGDSALHDAVRLNRYKIIKLLLLHGADMMAKNLAGKTPTDLVQLWQADTRHALEHPEPESEQNGLERPGSGRETPQPIPAQ
Protein: EG:80H7.2 protein (Pickel, isoform A) (Pickel, isoform C) (O76899)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sinuous
- LD32918p
Sequence:
MRELNKQQSQDTTDSGVEKGDYPRATNGVVFGAIVTFASFFVLMMSFCSPYWIESYEETRASFKNMGLWQYCFKDFVYPKYAFLKQFTGCHNIFSHEYYVIREYLLPGWLMAVQGFVTMSFIIVFLVLALLSLTIIRLPLKAVLQYEWLLVRLSYMGTAISSLFMFLAVCIFGGCAYRRDWMMYPKFNVLGWSYALAVVTFMLLGLAALILQREARQAYDARGEQKNLVMQMEMQEPGYQPPRHHHSQSRSLQGYI
Protein: Ergosteryl-beta-glucosidase (EC 3.2.1.-) (P40566)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ergosteryl beta-glucosidase involved in the ergosteryl beta-glucoside (EG) catabolic pathway and vacuole formation via hydrolysis of EG to generate glucose. Is also able to hydrolyze cholesteryl beta-glucoside and sitosteryl beta-glucoside to generate glucose; and C6-7-nitro-2,1,3-benzoxadiazole (NBD)-GlcCer to generate C6-NBD-ceramide (Cer).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26116408}. Vacuole membrane {ECO:0000269|PubMed:26116408}; Peripheral membrane protein {ECO:0000269|PubMed:26116408}. Note=Localizes in the cytosol until the initial logarithmic phase, then targets to a yet unidentified organelle with a granule structure in the middle logarithmic phase, and finally localizes at the vacuole membranes in the stationary phase. {ECO:0000269|PubMed:26116408}.
Interaction partners:
- Glucan 1,3-beta-glucosidase I/II
- Sporulation-specific glucan 1,3-beta-glucosidase
- UTP--glucose-1-phosphate uridylyltransferase
- Maintenance of telomere capping protein 6
Sequence:
MPAKIHISADGQFCDKDGNEIQLRGVNLDPSVKIPAKPFLSTHAPIENDTFFEDADKVSFINHPLVLDDIEQHIIRLKSLGYNTIRLPFTWESLEHAGPGQYDFDYMDYIVEVLTRINSVQQGMYIYLDPHQDVWSRFSGGSGAPLWTLYCAGFQPANFLATDAAILHNYYIDPKTGREVGKDEESYPKMVWPTNYFKLACQTMFTLFFGGKQYAPKCTINGENIQDYLQGRFNDAIMTLCARIKEKAPELFESNCIIGLESMNEPNCGYIGETNLDVIPKERNLKLGKTPTAFQSFMLGEGIECTIDQYKRTFFGFSKGKPCTINPKGKKAWLSAEERDAIDAKYNWERNPEWKPDTCIWKLHGVWEIQNGKRPVLLKPNYFSQPDATVFINNHFVDYYTGIYNKFREFDQELFIIIQPPVMKPPPNLQNSKILDNRTICACHFYDGMTLMYKTWNKRIGIDTYGLVNKKYSNPAFAVVLGENNIRKCIRKQLSEMQKDAKSMLGKKVPVFFTEIGIPFDMDDKKAYITNDYSSQTAALDALGFALEGSNLSYTLWCYCSINSHIWGDNWNNEDFSIWSPDDKPLYHDTRAKTPTPEPSPASTVASVSTSTSKSGSSQPPSFIKPDNHLDLDSPSCTLKSDLSGFRALDAIMRPFPIQIHGRFEFAEFNLCNKSYLLKLVGKTTPEQITVPTYIFIPRHHFTPSRLSIRSSSGHYTYNTDYQVLEWFHEPGHQFIEICAKSKSRPNTPGSDTSNDLPAECVIS
Protein: Ankyrin repeat and sterile alpha motif domain containing 1A (A0A3B3ITU5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKEQELLEAARTGHLPAVEKLLSGKRLSSGFGGGGGGGSGGGGGGSGGGGGGLGSSSHPLSSLLSMWRGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPSHTRVNEQNALEIKELKKYGPFDPYINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMGSALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALDTVRELPSQKSQQIAALIEDHMTGKRSTKEVDKTPPPQPPLISSMDSISQKSQGDVEKAVTELIIDFDANAEEEGPYEALYNAISCHSLDSMASGRSSDQDSTNKEAEAAGVKPAGVRPRERPPPPAKPPPDEEEEDHIDKKYFPLTASE
Protein: Sarcoplasmic calcium-binding protein, isoform B (Q7KVU4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPTAVVQAVRQYSKKAGAAKLRREVESDSDSDSDDEFERRRQKMDSKRSERGDSAFWRRKMRTLHRILDVNHDGVVSFDDFSLLAKRFSDLGHLTPEVAAEFNDVIKHTWEEQFGEITPYNLVTAEQFLTDLHHRLNDKKMAKRIGRFLPYLFKAVDFDHTGHLDLEQYKLFFRCLGLTEDDAAVSFAVIDKNGDGQLSLKEFVHLGRQFFLTEDDSKISKMFWGPLVADH
Protein: Protein FAM124B (Q9H5Z6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:23285124}.
Interaction partners:
- Chromodomain-helicase-DNA-binding protein 8
Sequence:
MDETQGPLAMTVHLLANSGHGSLLQRTLDQLLDCICPEVRLFQVSERASPVKYCEKSHSKRSRFPGMSVLLFLHESPGEDRLFRVLDSLQHSPWQCYPTQDTRGRLCPYFFANQEFYSLDSQLPIWGVRQVHCGSEILRVTLYCSFDNYEDAIRLYEMILQREATLQKSNFCFFVLYASKSFALQLSLKQLPPGMSVDPKESSVLQFKVQEIGQLVPLLPNPCMPISSTRWQTQDYDGNKILLQVQLNPELGVKNGILGAGMLPLGSRLTSVSAKRTSEPRSQRNQGKRSQGHSLELPEPSGSPTSDRCAGTSWKSPGRSFQVSSPAMGAHLHLSSHHLESGARMKVLNRENSFQKLEAETNVDTGLTIINSEPRQTYFGGFPRDLQTSQPPFCLPASSLGVATSKNNSVLKERVSPLPLAGQRDLGTRKTISECLLHLQVQGEEKEEDEEEFFI
Protein: CHIP (LD25129p) (O18353)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNRRGLNAGNTMTSQANIDDGSWKAVSEGGSMLPASNSAVLNPDGSNQSGFAQGGLPYNSAGNPYPPAGQSSPAGNQSIVFQNSNQPGSNTPQYTSSPAPSGSSTPGPVGAQNIPGNYPQSATAGNFNGPVGGPFGSPSSGLGQFSRPASSGTPFNSGQAGHFSSPTVFSVGGQFNPMPPASPFGHGGNHPMMGGPQQMERIDQGFRRHNSYFSHTEHRVFELNKRLQQRNEESDNCWWDSFTTEFFEDDARLTILFCLEDGPKRYTIGRTLIPRFFRSIYEGGVSDLYFQLKHAKESFHNTSITLDCDQCTVITQHGKPFFTKVCADARLILEFMYDDYMRIKSWHMTIKGHRELIPRSVIGTSLPPDPMLLDQITKNITRAGITNSTLNYLRLCVILEPMQELMSRHKAYALSPRDCLKTTLFQKWQRMVAPPGKKDPQRPPNKRRKRKGSNSGGGNNSNTPPVTNQKRSPSGPSFSLSSQDVMVVGEPTLMGGEFGEEDERLITRLENTQYDGTNAVEHDNHTGFGHADSPISGSNPWSIDRAGAIPASPGNGAAPQNNANISDIDKKSPIVSQ
Protein: Cytochrome c oxidase assembly factor 3, mitochondrial (Coiled-coil domain-containing protein 56 homolog) (P0DKM0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a critical role in the biogenesis and activity of cytochrome c oxidase (COX) (complex IV).
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:22610097}; Single-pass membrane protein {ECO:0000269|PubMed:22610097}.
Interaction partners:
- Dimethyladenosine transferase 1, mitochondrial dimethyltransferase 1)
- NADH dehydrogenase 1 alpha subcomplex subunit 8
Sequence:
MSASEQGPKIKYGESAPKLDKAQLQFMKLIEEQNLDRVQKLKRIRRNNLLTAGALGVSVLAIYGYSIFSVQQEKFLDDFEEPKKVSS
Protein: Nebulin (Q9DEG5)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
QEILSDRLYRTQPDKMKFTSVTDAPDVVQAKINAMQLSNHLYREAWDKDKTQISIPSDTPEMLQSKVNALNISNKHYQKAWDEAKAKNYDLRADAIPIKHAKASRDIASEYKYKEAHEKQKGHYIGCRTAKEDPKLSWAARAMLLQNDRIYRKAYNDSKAHIHMPVDAMSLQAAKECQTLVSDVDYRHYLHQWTCLPDHNDVVHARKAYDLQSDAVYKSDLEWLRGIGWLPNDSLGINHVKHAGDLLNERKYRTKAETLHFTPVADRVDYVTAKKSGEILSDIKYHKDWNEVKSNYTLTDTPQLDMAREAARILNQSLYKESWEKEKATGYLLPPDTVQIRHAKHSNDVQSELKYKADYVKQRGHYVGVASMRDDPKLVWFEHAGEIQNDRLYKSNYHKTKSKIHIPADIMSVVAAKECQALVSDVDYRHYLHQWTCHPDQNDCIQARKAYDLQSDNIYKSDLEWLRGCGWIPLGSVEHKKVKHAQELINKRAYTKDAIENFSKYTSVVDTPDIVLAKINSVNQSDLKYKETFNLEKGQYIGSDDTPELNHARDMSLLYSDKLYKRDWEVCKPIGYTLDAKYIPLVGAKHANYVNSELKYKEIYEKLKGHYLAGKDIGDFPSVVHSLAFQKIRSALAYRKNYEDTKTRVHIPSDMMNHVLAKKCQYILSDLEYRTYLHHWNCSPEEHDVIQARRAQEILSDVVYKDDLNWLKGIGCYVWDTPQILHAKKSYDLQSQIKYTAAGKENFQNFGVVTDTPVYVTAVQSGINASDVKYKEDYHKTKDKYTTVTETADSERVQNLKHLFSNNLYKEAWDRVKATSYIMPSDAVSLARAKELKHNASIVKYREEYDKFKALYTLPRSVEDDPNTARCLRVGKLNIDRLYKETYEKNKAKVHIIPDMVDIIAAKDAQKKISEIDYRTHLHDWICLPDLQINAHVRKVADQISDVVYKDDLNWLKGIGCFVWDTPEILHAKHAYDLRSDIKYKSDADKMKSKYTVVMDTPVYVQNILSGLNASEVIYRGDYLKKVRGKMIPTDKTVDLQR
Protein: Steroid receptor RNA activator 1 (Steroid receptor RNA activator protein) (SRAP) (Q6QGW5)
Organism: Rattus norvegicus (Rat)
Function: Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of steroid receptors ligand-dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9HD15}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD15}.
Interaction partners:
- Cytoplasmic FMR1-interacting protein
- ABI gene family member 3
- Protein BRICK1
- Nck-associated protein 1
- Abl interactor 1
- NCK associated protein 1 like
- Actin-binding protein WASF1
- Abl-interactor 2
- Wiskott-Aldrich syndrome protein family member
- Cytoplasmic FMR1-interacting protein
Sequence:
MAELYVKPGNKERGWNDPPQFSYGLQTQTGGTKRTPLTKRVAAPQDGSPRAPETSGPPPVDHPPPSSKASRPPPMGSCPASGVDPPSSPVIESETLIEDVLRPLEQALEDCRGHTKQVCDDISRRLALLHEQWDGGKLSVPVKKRMALLVQELLHHQWDTADDIHRSLMVDHVTEVSQWMVGVKRLIAEKRSLSSEENKEEKSTVAPENQTIPGFQPSS
Protein: RNA helicase (EC 3.6.4.13) (Q382X0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGPNRQRKPRELARGRGRGGRCGRGRAAAPAPTAPSSILSRAEKDMVIDVLHHAASGGAVPVSEEHFNPNSGSRIKFQRNSPLTPSEILQRLYEGLGFPPDLVTQYVRDLADESKLPVFNSIGELLAEGGPFQSFLVDSCFELFSYMLWYSREEEGTSLTPEEGDSILQEELEAVRALFDDSFIGLKNFGDDDTDDRELQFSFFTQDDKGVMLSIRIPDHYPSDPPNIFIGPRKQQTGGMSTLAVLPLDTKELPAVARRSILDAAVEAINGFVGEGCLIGLLSSICGAISSVSGLGVVEQLPTPAPCESKEVKAVIAAKRQAFASALSASEDPLALPPEEPSSTTCSLPAKVELGTVDHSDDEVGQVRREFLRNNKQLDAKLKEEWQALRANGTLRNSREQLPAYNAREELRQAVARHRVVVVSGETGSGKTTQIPQYLYEFMCEDGKGSSANIVCTQPRRLAATSVALRVAGERDEAVGGVVGYTIRLENCVSSRTQITYCTTGVVLRRIQVDKFLGRVSHIVVDEIHERGVDTDVLLILLRDLLERRDDLTVVLMSATMDSELFARYFGGSPIINIAGRTFPVQVFHLEEIIPMVNYSLDDGSPYAKWEVRKEERRRNTRKQMLDIDINEIEEARELTAGVHGPSTQLSASHRTLDILSRMNPDVINYELIESIVVYIDTKMGVPGAILIFLPGMVEMTSCMEQLKSNPKLLSSCLIYNLHSSLGSAEQQGVFQHPPKGKRKVVIGTNIMETSITIDDAVFVIDCGKVKENRYDARRSLSQLVTVNTSKANCRQRQGRAGRVREGFCFRLFTSTQFESLDDHQLCEMHRVPLESLVLQIYSLNLGDEVEYLRKALSPPDERAVRSSVKALTTLGALTMDKRLTSLGRHLANLPLDVRIGKMVIHGAILQCVDPVLTIAACLAVRTPFLSAMDYQVEVEGVRRALSGDYMSDHLSSWFAYSKWIAMWHKEGPAGASKLCAKYYLSLPALRQIQATKQQYERFLYEAGLIEETPVRMKNNRFLYDPVVTLEDSVYESGGPRFNTNSGSVKCILSCIVAGLYPNVACVKTVRGGKGGNRTNITTLDGSEVLVHPSSVAGKEKAFASPLLVYVDKVKTSATFLREVSMVTPLHVVFFGSGRLEYLPKYGELVVDEATAFRCQSEDAVLLRHLKDQLDSALSQKINDPSKSWESTSSVVVRAILRLLKGDSSTVRGLTVVDRRQPRAPLTAPLLQVESSDDAPKKKDGSADKRTCFVCGEGGHVVNTCPHKAAAAKGGPVTRCFICGEWHHPTDCAVTTPMR