wanglab/gogpt-training-data huggingface dataset:
Protein: YY1-associated protein 1 (Hepatocellular carcinoma susceptibility protein) (Hepatocellular carcinoma-associated protein 2) (Q9H869)
Organism: Homo sapiens (Human)
Function: Associates with the INO80 chromatin remodeling complex, which is responsible for transcriptional regulation, DNA repair, and replication. Enhances transcription activation by YY1. Plays a role in cell cycle regulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11710830, ECO:0000269|PubMed:12118372}. Nucleus {ECO:0000269|PubMed:14744866, ECO:0000269|PubMed:17541814}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27939641}. Nucleus, nucleolus {ECO:0000269|PubMed:27939641}.
Interaction partners:
- Histone-lysine N-methyltransferase ASH1L
- Transcriptional repressor protein YY1
Sequence:
MEEEASRSAAATNPGSRLTRWPPPDKREGSAVDPGKRRSLAATPSSSLPCTLIALGLRHEKEANELMEDLFETFQDEMGFSNMEDDGPEEEERVAEPQANFNTPQALRFEELLANLLNEQHQIAKELFEQLKMKKPSAKQQKEVEKVKPQCKEVHQTLILDPAQRKRLQQQMQQHVQLLTQIHLLATCNPNLNPEASSTRICLKELGTFAQSSIALHHQYNPKFQTLFQPCNLMGAMQLIEDFSTHVSIDCSPHKTVKKTANEFPCLPKQVAWILATSKVFMYPELLPVCSLKAKNPQDKILFTKAEDNKYLLTCKTARQLTVRIKNLNMNRAPDNIIKFYKKTKQLPVLGKCCEEIQPHQWKPPIEREEHRLPFWLKASLPSIQEELRHMADGAREVGNMTGTTEINSDQGLEKDNSELGSETRYPLLLPKGVVLKLKPVADRFPKKAWRQKRSSVLKPLLIQPSPSLQPSFNPGKTPAQSTHSEAPPSKMVLRIPHPIQPATVLQTVPGVPPLGVSGGESFESPAALPAMPPEARTSFPLSESQTLLSSAPVPKVMMPSPASSMFRKPYVRRRPSKRRGARAFRCIKPAPVIHPASVIFTVPATTVKIVSLGGGCNMIQPVNAAVAQSPQTIPIATLLVNPTSFPCPLNQPLVASSVSPLIVSGNSVNLPIPSTPEDKAHMNVDIACAVADGENAFQGLEPKLEPQELSPLSATVFPKVEHSPGPPPVDKQCQEGLSENSAYRWTVVKTEEGRQALEPLPQGIQESLNNSSPGDLEEVVKMEPEDATEEISGFL
Protein: Beta-defensin 115 (Beta-defensin 15) (DEFB-15) (Defensin, beta 115) (Q30KQ5)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-defensin 127
- Beta-defensin 116
- Beta-defensin 121
- Defensin beta 118
- Beta-defensin 123
- Beta-defensin 110
- Beta-defensin 113
- Beta-defensin 114
- Beta-defensin 128
- Beta-defensin 126
Sequence:
MLPDHFSPLSGDIKLSVLALVVLVVLAQTAPDGWIRRCYYGTGRCRKSCKEIERKKEKCGEKHICCVPKEKDKLSHIHDQKETSELYI
Protein: HMG-Y-related protein A (AtHMGA) (High mobility group A protein) (Q43386)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds A/T-rich DNA with a highly dynamic distribution into the nucleus.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:17114349}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9FYS5}. Note=Follows a highly dynamic speckled distribution pattern throughout the chromatin of interphase nuclei. {ECO:0000269|PubMed:17114349}.
Interaction partners:
- AT3g07170/T1B9_17
- DEAD-box ATP-dependent RNA helicase 46
- Uncharacterized protein At2g34160
- At5g08780
- Winged-helix DNA-binding transcription factor family protein
- Winged helix-turn-helix transcription repressor DNA-binding protein
- Winged-helix DNA-binding transcription factor family protein
- Telomere repeat-binding factor 5
- At5g12410
- Pre-mRNA cleavage factor Im 25 kDa subunit 2
Sequence:
MAFDLHHGSASDTHSSELPSFSLPPYPQMIMEAIESLNDKNGCNKTTIAKHIESTQQTLPPSHMTLLSYHLNQMKKTGQLIMVKNNYMKPDPDAPPKRGRGRPPKQKTQAESDAAAAAVVAATVVSTDPPRSRGRPPKPKDPSEPPQEKVITGSGRPRGRPPKRPRTDSETVAAPEPAAQATGERRGRGRPPKVKPTVVAPVGC
Protein: Regulator of G-protein signaling 19 (RGS19) (G-alpha-interacting protein) (GAIP) (O70521)
Organism: Rattus norvegicus (Rat)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, predominantly to G(i)-alpha-3. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (By similarity).
Subcellular location: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- PDZ domain-containing protein GIPC1
- Vitamin K-dependent protein C
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- Chaperone Ric-8A
Sequence:
MPTPHEAEKQHTGPEEADRPPSMSSHDAAPSGPPSRNPCCLCWCCCCSCSWNQERQRAWQVSRESKLQPLPSCEVCTPPSPEEVQSWAQSFDKLMHSPTGRSVFRAFLRTEYSEENMLFWLACEELKTEADRHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINRKMQEPSPHTFDDAQLQIYTLMHRDSYPRFLTSPTYRSLLLQGAPQSSEA
Protein: Link domain-containing protein (Q585U2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 6-phosphofructo-2-kinase/fructose-2, 6-biphosphatase, putative
Sequence:
MSMDTRMVNFGFTRAALLCGLLLLLTAVCPLHVTAADNGRVIVNVKSYFSMDNFAFAHRGNYFVSYKNAAAYCGDNGAVLPADQTEAAHQSLQSAIKRVITGSDAFSYLGGDAVYSSGEAIEADKRCKPGDAASSRYCVYRWNKGLFAKALPDGQGVAFWRGSYVKYGGAASMNGYPSFWGSEYPKRGQLYTLSWYHTGDDVTTWYDGKDMSGRIKWASDNPDTKTENYVILCEVHDSISTTTTTTTTTTTTTTTTTTAAPASGEVPEPTVTKDEEVTVTTVSLEERSNWHIILIALISVVSLIVLLLFLLRWFCDYDVKKEIIPMTLREVVGEPLFVLEPTPFVPPEGFAAPPLALQYYNQMRTSE
Protein: Protein tesmin/TSO1-like CXC 3 (AtTCX3) (Protein TSO1-like 1) (Protein SOL1) (Q8L548)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in development of both male and female reproductive tissues.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- F-box associated ubiquitination effector family protein
- Retinoblastoma-related protein 1
- Proline-rich spliceosome-associated
- THO complex subunit 4B
- Transcription factor E2FC
- Ras-related protein RABG3d
- Histone-binding protein MSI1
- Transcription factor-like protein DPB
- Protein ALWAYS EARLY 1
- Protein ALWAYS EARLY 3
Sequence:
MDTPEKSETQIGTPVSKLKVEDSPVFSYICNLSPIKTIKPIPITCPLSSLNYASPPSVFTSPHAVSHKESRFRSQKDVSASKEVGEEEALVGSEPEQSYKNDCNTPRVTNDVKDNGCGKDLQVMMDNVKKKSDTPDWETLIAATTELIYGSPRESEAFSCLLKKTSNSEARLRGSITATSVAVTNTDVVNNESESVDALSILHRGVRRRCLDFEVKGNNQQTLGESSSSCVVPSIGLHLNTIAMSSKDKNVANEYSFSGNIKVGVQSSLTPVLHSQHDIVRENESGKDSGQIIEVVPKSLASVDLTPISPKKKRRKSEQSGEGDSSCKRCNCKKSKCLKLYCECFAAGFYCIEPCSCINCFNKPIHKDVVLATRKQIESRNPLAFAPKVIRNSDSIIEVGEDASKTPASARHKRGCNCKKSNCLKKYCECYQGGVGCSINCRCEGCKNAFGRKDGSLFEQDEENETSGTPGTKKTQQNVELFKPAAPPSTPIPFRQPLAQLPISSNNRLLPPQSHFHHGAIGSSSSGIYNIRKPDMSLLSHSRIETITEDIDDMSENLIHSPITTLSPNSKRVSLSHLDSPESTPWRRNGGGRNLIRSFPTFPSLTPHH
Protein: Amine oxidase [flavin-containing] A (EC 1.4.3.21) (EC 1.4.3.4) (Monoamine oxidase type A) (MAO-A) (Q64133)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially oxidizes serotonin. Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P21396}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P21396}; Cytoplasmic side {ECO:0000250|UniProtKB:P21396}.
Interaction partners:
- Catechol O-methyltransferase
- Transmembrane O-methyltransferase homolog
- Aromatic-L-amino-acid decarboxylase
- Dopamine beta-hydroxylase
- Amine oxidase [copper-containing] 3
- Amine oxidase
- Amine oxidase
- E3 ubiquitin-protein ligase parkin
- Diamine oxidase [copper-containing]
- Amine oxidase
Sequence:
MTDLEKPSITGHMFDVVVIGGGISGLAAAKLLSEYKINVLVLEARDRVGGRTYTVRNEHVKWVDVGGAYVGPTQNRILRLSKELGIETYKVNVNERLVQYVKGKTYPFRGAFPPVWNPLAYLDYNNLWRTMDDMGKEIPVDAPWQARHAEEWDKITMKDLIDKICWTKTAREFAYLFVNINVTSEPHEVSALWFLWYVRQCGGTSRIFSVTNGGQERKFVGGSGQISEQIMVLLGDKVKLSSPVTYIDQTDDNIIIETLNHEHYECKYVISAIPPVLTAKIHFKPELPPERNQLIQRLPMGAVIKCMVYYKEAFWKKKDYCGCMIIEDEEAPISITLDDTKPDGSMPAIMGFILARKAERLAKLHKDIRKRKICELYAKVLGSQEALSPVHYEEKNWCEEQYSGGCYTAYFPPGIMTLYGRVIRQPVGRIYFAGTETATQWSGYMEGAVEAGERAAREVLNALGKVAKKDIWVQEPESKDVPALEITHTFLERNLPSVPGLLKITGFSTSVALLCFVLYKFKQPQS
Protein: Uncharacterized protein TRE1 (Transferrin receptor-like protein 1) (Q08919)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Metal homeostatis protein BSD2
- E3 ubiquitin-protein ligase RSP5
- Manganese transporter SMF1
- Protein EAR1
- Protein SSH4
- Ubiquitin ligase-binding protein BUL1
Sequence:
MVNTRGYTTLPNVEEPANNSQDELNSQDFEQAIGMPSEPPVYVEEMGMEEPQAPEAFSEKVQRFRMCFENNVVIPVKKNVVDPLAQMISLASEKFDLFLSKIGNVMVMRRIFYIMMMSIIAALIIASDRLPNGKARGSNGSFSDHDLLLQYARKSIDLSKIERDLEYISSMPHMSGTSGDAAIRHYIKESFDKNGIRLAGEEEFMAYSNYPGNVSLRVYSKDDTEGFDIPLNEENFNPMSHNGQLNNIPVIYANKASLDDMASMQDQGLLNGDFILLVHYGDYVFQQMLTAQEYGAKAIIFISEPYQDNKDVIQMKSVALPQYGTGDALTPEWEGSIRDPIDATEAKCLPKIPSIPISANQGDKILAILSDTGVKFSNNLFSGSLNDCRLDLLVQTAIRERHPVHDIVGKIEGSEQAGRAIVIAAPRNSASYGTMYPSFGTVVLLSLIQLYQEMVYKFDWKPLRNIYFISFGGSEFNEAGATELMEKRTEALKSEIYTIIDVGQIGIWDDSNNLEIQCHPLLVDLFQKNMTSRKFNVKVDNVHQFGDWTPYLAQGIPVAIISSPGVMNREHPIYTVEDKFDFIKDKLRDKKKGEVLSEIMLYLVEKSLELIDDPFIPFSISNYVDFLSTTLKDLQKECPDTVNFDEVFLGTTLWENTKLQFEKWKSEWTELMYGAGTYIEPTIIAINRWSWNYLLSLIGVTQCLEEGLMDRTFYKNVIFGPKLWVDKGDPLRSWTFPEIRDTIAIKDWSSVQVQANTLGTILQNTARYFLENKNLHGINTNEF
Protein: Caffeoylshikimate esterase (EC 3.1.1.-) (Lysophospholipase 2) (LysoPL2) (Q9C942)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Esterase involved in the biosynthesis of lignin. Hydrolyzes caffeoylshikimate into caffeate and shikimate. Together with 4-coumarate--CoA ligase (4CL), acts on an alternative reaction for the formation of caffeoyl-CoA and bypasses the second reaction of shikimate O-hydroxycinnamoyltransferase (HST). Accepts also 4-coumaroylshikimate as substrate, but with lower activity. According to PubMed:20345607 and PubMed:22915575, posseses monoacylglycerol O-acyltransferase, monoacylglycerol lipase and lysophospholipase activities in vitro. With the association of ACBP2, may promote the degradation of lysophosphatidylcholine and detoxify the peroxidized membrane in response to cadmium-induced oxidative stress. However these results require additional confirmation in vivo.
Subcellular location: Cell membrane {ECO:0000305|PubMed:20345607}; Peripheral membrane protein {ECO:0000305|PubMed:20345607}. Note=Colocalizes with ACBP2.
Interaction partners:
- Cytochrome P450 98A3
- Flavone 3'-O-methyltransferase 1
- F5F19.5 protein
- Shikimate O-hydroxycinnamoyltransferase
- Cinnamoyl-CoA reductase 1
- Trans-cinnamate 4-monooxygenase
- 4-coumarate--CoA ligase 4
- 4-coumarate--CoA ligase 1
- Cinnamoyl-CoA reductase 2
- 4-coumarate--CoA ligase 2
Sequence:
MPSEAESSANSAPATPPPPPNFWGTMPEEEYYTSQGVRNSKSYFETPNGKLFTQSFLPLDGEIKGTVYMSHGYGSDTSWMFQKICMSFSSWGYAVFAADLLGHGRSDGIRCYMGDMEKVAATSLAFFKHVRCSDPYKDLPAFLFGESMGGLVTLLMYFQSEPETWTGLMFSAPLFVIPEDMKPSKAHLFAYGLLFGLADTWAAMPDNKMVGKAIKDPEKLKIIASNPQRYTGKPRVGTMRELLRKTQYVQENFGKVTIPVFTAHGTADGVTCPTSSKLLYEKASSADKTLKIYEGMYHSLIQGEPDENAEIVLKDMREWIDEKVKKYGSKTA
Protein: Alkylglycerol monooxygenase (EC 1.14.16.5) (Transmembrane protein 195) (Q6ZNB7)
Organism: Homo sapiens (Human)
Function: Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20643956}; Multi-pass membrane protein {ECO:0000269|PubMed:20643956}.
Interaction partners:
- Aldehyde dehydrogenase family 3 member A2
- Fatty acid 2-hydroxylase
- Diacylglycerol kinase beta
Sequence:
MKNPEAQQDVSVSQGFRMLFYTMKPSETSFQTLEEVPDYVKKATPFFISLMLLELVVSWILKGKPPGRLDDALTSISAGVLSRLPSLFFRSIELTSYIYIWENYRLFNLPWDSPWTWYSAFLGVDFGYYWFHRMAHEVNIMWAGHQTHHSSEDYNLSTALRQSVLQIYTSWIFYSPLALFIPPSVYAVHLQFNLLYQFWIHTEVINNLGPLELILNTPSHHRVHHGRNRYCIDKNYAGVLIIWDKIFGTFEAENEKVVYGLTHPINTFEPIKVQFHHLFSIWTTFWATPGFFNKFSVIFKGPGWGPGKPRLGLSEEIPEVTGKEVPFSSSSSQLLKIYTVVQFALMLAFYEETFADTAALSQVTLLLRVCFIILTLTSIGFLLDQRPKAAIMETLRCLMFLMLYRFGHLKPLVPSLSSAFEIVFSICIAFWGVRSMKQLTSHPWK
Protein: Poly(ADP-ribose) glycohydrolase (EC 3.2.1.143) (O02776)
Organism: Bos taurus (Bovine)
Function: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q86W56}. Note=Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q86W56}.
Interaction partners:
- Poly [ADP-ribose] polymerase
- Poly [ADP-ribose] polymerase 1
- Poly [ADP-ribose] polymerase
- X-ray repair cross complementing 1
- ADP-ribose glycohydrolase MACROD1
- ADP-ribosylhydrolase ARH3
- Mono-ADP ribosylhydrolase 2
- ADP-ribose glycohydrolase OARD1
- Histone PARylation factor 1
- Proliferating cell nuclear antigen
Sequence:
MSAGPGCEPCTKRPRWDAAATSPPAASDARSFPGRQRRVLDSKDAPVQFRVPPSSSGCALGRAGQHRGSATSLVFKQKTITSWMDTKGIKTVESESLHSKENNNTREESMMSSVQKDNFYQHNMEKLENVSQLGFDKSPVEKGTQYLKQHQTAAMCKWQNEGPHSERLLESEPPAVTLVPEQFSNANVDQSSPKDDHSDTNSEESRDNQQFLTHVKLANAKQTMEDEQGREARSHQKCGKACHPAEACAGCQQEETDVVSESPLSDTGSEDVGTGLKNANRLNRQESSLGNSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPGFDEQEDSSSAQTANKPSRFQPREADTELRKRSSAKGGEIRLHFQFEGGESRAGMNDVNAKRPGSTSSLNVECRNSKQHGRKDSKITDHFMRVPKAEDKRKEQCEMKHQRTERKIPKYIPPHLSPDKKWLGTPIEEMRRMPRCGIRLPPLRPSANHTVTIRVDLLRIGEVPKPFPTHFKDLWDNKHVKMPCSEQNLYPVEDENGERAAGSRWELIQTALLNRLTRPQNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKLLTRLHVTYEGTIEGNGQGMLQVDFANRFVGGGVTSAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDRSERDDWQRRTTEIVAIDALHFRRYLDQFVPEKIRRELNKAYCGFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAVAERDVVYFTFGDSELMRDIYSMHTFLTERKLTVGEVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESCTQTTNQPGQRTGA
Protein: Ubiquitin-like domain-containing protein (R9PY16)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Ubiquitin-ribosomal protein eL40 fusion protein
- 40S ribosomal protein S27
- Small ribosomal subunit protein eS25
- 40S ribosomal protein S24
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS26
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEENPPEHQRLIFGGKHLENGRTLSDYNIQKESTIYLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEENPPEHQRLIFGGKHLENGRTLSDYNIQKESTIYLVLRLRGGMQIFVKTLTGKTITLEVEPSDSIENVKARIHDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIKHVKARIHDKDGIPPDHQRLIFAGKQLEDGRTLSDYNIQKESTLHSHFKW
Protein: Homer, isoform B (Q9VM94)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MSADSEQPIFTCQAHVFHIDPKTKRTWITASMKAVNVSFFYDSSRNLYRIISVEGTKAVINSTITPNMTFTQTSQKFGQWSDVRANTVYGLGFASEAELTKFVEKFQEVKEATKNAMKSANGSNAVTPTTSANTSPISGRAVGSMQNDNTAIDPHTVEPPNMSNTNTQNANPDSPSHKLLNTSDVKADIGSATPSPQPTSGVTGGGGVTISSGGSIVGMHTGPGAGATAEQQLKYENERLKMALAQSCANAKKWEIELATLKNNNIRLTSALQESTANVDEWKRQLHTYKEENIRLKRDMEQLCVGGGVVAAAGGGATEDELRREVATLKARTEQLQKELMQQELELKSANISLREKSNDQTLAKLSEVNGVFAKHLSELYGVQKDMESLIQIAKCT
Protein: Transcriptional adapter (A0A024R0Y4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR025024}.
Interaction partners:
Sequence:
MDRLGSFSNDPSDKPPCRGCSSYLMEPYIKCAECGPPPFFLCLQCFTRGFEYKKHQSDHTYEIMTSDFPVLDPSWTAQEEMALLEAVMDCGFGNWQDVANQMCTKTKEECEKHYMKHFINNPLFASTLLNLKQAEEAKTADTAIPFHSTDDPPRPTFDSLLSRDMAGYMPARADFIEEFDNYAEWDLRDIDFVEDDSDILHALKMAVVDIYHSRLKERQRRKKIIRDHGLINLRKFQLMERRYPKEVQDLYETMRRFARIVGPVEHDKFIESHALEFELRREIKRLQEYRTAGITNFCSARTYDHLKKTREEERLKRTMLSEVLQYIQDSSACQQWLRRQADIDSGLSPSIPMASNSGRRSAPPLNLTGLPGTEKLNEKEKELCQMVRLVPGAYLEYKSALLNECNKQGGLRLAQARALIKIDVNKTRKIYDFLIREGYITKG
Protein: Sperm-associated antigen 11A (Antimicrobial-like protein Bin-1b) (EP2 protein) (Q8K4N2)
Organism: Mus musculus (Mouse)
Function: Has antimicrobial activity against E.coli (By similarity). Plays a role in the defense response in the male reproductive tract, contributing to sperm maturation, storage and protection (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Beta-defensin 15
Sequence:
MIPRLLPFFASLLFAALLFPGDIPPGIRNTVCLMQQGHCRLFMCRSGERKGDICSDPWNRCCVPYSVKDRR
Protein: DNAJ protein JJJ1 homolog (AtJJJ1) (Q9C911)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
Interaction partners:
- Cytoplasmic 60S subunit biogenesis factor REI1 homolog 1
- Cytoplasmic 60S subunit biogenesis factor REI1 homolog 2
- 60S ribosomal export protein NMD3
- Nucleolar GTP-binding protein 1
- Eukaryotic translation initiation factor 6-2
- ERBB-3 BINDING PROTEIN 1
- At5g26610
- KIN17-like protein
- Nucleolar GTP-binding protein 1
- At2g32600/T26B15.16
Sequence:
MASSSRSEKRCHYEVLGISKESSPDEIRSSYRRLALQRHPDKLMKAAGLSEAEATAQFQELVHAYEVLSDPKERAWYDSHRSQILFADHSSAGGSKSGGSVPDLFAFFSPTVYSGYSDTGKGFYKVYYDVFNSVYLNEIKFARTLGLRMDSVREAPIMGNLESPYAQVTAFYNYWLGFCTVMDFCWVDEYDVMGGPNRKSRRMMEEENKKSRKKAKREYNDTVRGLAEFVKKRDKRVIDMLVKKNAEMEKKKEEERERKKKMEKERLERAMNYEEPEWAKAHEGEDEGAGLSELEEEDDDAKRKNEQLYCIVCSKKFKSEKQWKNHEQSKKHKEKVAELRESFTDYEEENEEEEIDGPLDSPESVEELHEKLQEELNIDNEERDVKKEVVGEADETDDEYFVAEEDMQGSSESEDEDDEMTLLKKMVSGQKNKQKNVVSKEEDEDETEVEIEGDTAEFSEFDNQKSTGRNKEAKEERNKQNAGNDMADDTSKVQIPGEGGNPDENMNATESASGALADSQKDEANSMEYDNRKSTGRRRRSKKGKDKNNQGELNEKSSEADDTQYVNRDMESQDYKKAPRSKKSTRGMKTKGTTKKNSSNECDRCGEEFESRTKLHKHLADSGHATVKSR
Protein: 40S ribosomal protein S3 (Q5B5U3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 60S ribosomal protein L20
- 60S ribosomal protein L27
- 40S ribosomal protein S30
- 60S ribosomal protein L23
- 40S ribosomal protein S7
- 60S ribosomal protein L35
- 60S acidic ribosomal protein P0
- Large ribosomal subunit protein uL18 C-terminal eukaryotes domain-containing protein
- 40S ribosomal protein S27
- Small ribosomal subunit protein uS7 domain-containing protein
Sequence:
MAAVQGAISKRRKFVADGVFYAELNEFFQRELAEEGYSGVEVRVTPTVTDISTTHTQEVLGEQGRRIRELTSLIQKRFKFPENSVSLYAAKVQNRGLSAVAQCESLRYKLLNGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRAARAKSMKFTDGFMIHSGQPAKEFIDSATRHVLLRQGVLGIKVKIMRGSDPEGKAGPQKTLPDSVTIIEPKEEQPVLQPISQDYGAKAIAAQQAAEQQRLAEQQAAEGQEGGAAETYAQE
Protein: GON-4-like protein (A5JYS9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEDTAEENNESIDDQPSTSTATDPNQTRETEKEKGDDEMFRLLQATDEILENKAKSMNLSSLNVRSILHHLIKYPSTIDVLLGIRENDDLPSVRNMRSRKKPDDSGASSTVNTPKKFGALRIEDRGPKSFLDLEYEEDDEYDDDYIEENDTSTRNKLNAGSEEDEENDDEEEIEDEGEDEDDEEQDELEEDGEHEITGSEACTSGQNDTMHALLFDETSEDVQNEEDYVLNMTLNDTRAESVAPIPTLDNVDDDGFYRDFVTGINRTEKDNDNLEVLDTEDDPDDEDYNVCADDGLNVEDWDETRQDKTTQIPRHELKALMIDTLLAEKEIPLNAFPEEAINGEEHRKSQKVKDAEVYERINTSISSSSESCSLLKDSLATFRPQELQQLNMQLEQHVQLLTQLVVTCHHDVNLSHVRNSSQLMMNELDDIRQQKIYPTVFDVRNLDAAIESCHDINAFDAVDESFLKYAENTEGYGGIALRPEAAVVLSRSNAIRYPALLPSRQPFFIETPIPFLSEEDLMLAVALLQFAHLPRRGEKEMIDRYTAIQQHCLPARSSYKIRTHLKSMRRSDKNPIHQIMQAAEKGVCKLVLPLKSWQESDTPICQWPPASQPGWYRRFQETFNVTEERKILRKHVSTMVLTPVKNKDRQDQEASEATFESGEEGEDDEFVNMGTAPDGRKIIMGREHIEDLVHQLIKQNEISPSKRRKNPTPMKLSTMIQLEEAEKRIADSQKNSCGGQTISALSNVSGDSNVDNNGTHEKELMPSTSSIDSLESINNQETSKFPRPLPMSDQPTLNTSCHITTTTCSVSYEDVDVGTLKKSYVEITASKYETNSNSCFSYPIPPTPGRRSPDDFDDYFMDLESNSLMWPQTPYAVTDENPQTPRGFSASESSEPIDFSSLGKATSLDTEEIVFQSTSCQRPMGYCSDFGEFSNSSSLPEEIPVPSHQRTPQESAIEDDSSMPGLDMVPLYEEDVEECIIEDIEEEEAPIKQGLVNSRPPLRFKKEVKAGITNLAPSRKRTRIEREAMGSVGLDDEQLHDKQKENIMRKVIEDVNQRLFMHTDTYQRFKEAITDENLTDFEKVTRTIIILANHPELLNLVLLNAPPEAVISDLQCDHNYQSYKVAIEMIMDIERYITAAKLKEPSLKGLFRYIQSFLEDKPNMTDEQATKRFYELFGQDRPLWKKLESRFWCLPYKARPRLENYEYIDLTGLETMSKREKRDWNSIPPRFETVDDIDQVMGSVYRASKNEPPSNLVVKCGEFCIRNDDETYTQLEITERVTLDQKR
Protein: Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Q13584)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSLRTSGTASWSGSLGDLEHVEAHCLAQRPALAHCDDVTDLDVQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNIHGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQ
Protein: Transmembrane alanine and leucine rich protein (O07208)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSDQVPKPHRHHIWRITRRTLSKSWDDSIFSESAQAAFWSALSLPPLLLGMLGSLAYVAPLFGPDTLPAIEKSALSTAHSFFSPSVVNEIIEPTIGDITNNARGEVASLGFLISLWAGSSAISAFVDAVVEAHDQTPLRHPVRQRFFALFLYVVMLVFLVATAPVMVVGPRKVSEHIPESLANLLRYGYYPALILGLTVGVILLYRVALPVPLPTHRLVLGAVLAIAVFLIATLGLRVYLAWITRTGYTYGALATPIAFLLFAFFGGFAIMLGAELNAAVQEEWPAPATHAHRLGNWLKARIGVGTTTYSSTAQHSAVAAEPPS
Protein: Hepatocyte nuclear factor 1-beta (Transcription factor 2) (Q6FHW6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MVSKLTSLQQELLSALLSSGVTKEVLVQALEELLPSPNFGVKLETLPLSPGSGAEPDTKPVFHTLTNGHAKGRLSGDEGSEDGDDYDTPPILKELQALNTEEAAEQRAEVDRMLSEDPWRAAKMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQTVQSSGNMTDKSSQDQLLFLFPEFSQQSHGPGQSDDACSEPTNKKMRRNRFKWGPASQQILYQAYDRQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSSNQTHSLNPLLSHGSPHHQPSSSPPNKLSGVRYSQQGNNEITSSSTISHHGNSAMVTSQSVLQQVSPASLDPGHNLLSPDGKMISVSGGGLPPVSTLTNIHSLSHHNPQQSQNLIMTPLSGVMAIAQSLNTSQAQSVPVINSVAGSLAALQPVQFSQQLHSPHQQPLMQQSPGSHMAQQPFMAAVTQLQNSHMYAHKQEPPQYSHTSRFPSAMVVTDTSSISTLTNMSSSKQCPLQAW
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (P06968)
Organism: Escherichia coli (strain K12)
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:1311056, ECO:0000305|PubMed:9261872}.
Interaction partners:
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Thymidylate synthase
- dCTP deaminase
- Thymidine kinase
- Nucleoid occlusion factor SlmA
- Thymidylate kinase
- Nucleoside diphosphate kinase
- 5'/3'-nucleotidase SurE
- Anaerobic ribonucleoside-triphosphate reductase
- Pyrimidine 5'-nucleotidase YjjG
Sequence:
MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ