wanglab/gogpt-training-data huggingface dataset:
Protein: Gametogenetin (Q86UU5)
Organism: Homo sapiens (Human)
Function: May be involved in spermatogenesis.
Interaction partners:
- E3 ubiquitin-protein ligase FANCL
Sequence:
MGNLQSEPSAGGGSRKVQPSDRAPDSRRTSLVEPEMTSQAMRLTRGLGVWFPGSATPPGLMVPREPQASPSTLPLTLERPSPVMPPPEEAAAVSAPPPAPAGTLLPGPSKWQKPAGTPVPRIRRLLEASHRGQGDPPSLRPLKPPPPPRQLSVKDTVPRAPSQFPPPLETWKPPPPLPSERQPADRRITPALATPASPPTESQAGPRNQGQTAGRARGGAPPHAGEGEMAQPADSESGLSLLCKITFKSRPSLAPPAASSSLAAKASLGGGGGGGLFAASGAISYAEVLKQGPLPPGAARPLGEVSRGAQEAEGGDGDGEGCSGPPSAPASQARALPPPPYTTFPGSKPKFDWVSAPDGPERHFRFNGAGGGIGAPRRRAAALSGPWGSPPPPPEQIHSAPGPRRPAPALLAPPTFIFPAPTNGEPMRPGPPGLQELPPLPPPTPPPTLQPPALQPTPLPVAPPLTPGLGHKESALAPTAAPALPPALAADQAPAPSPAPAPTVAEPSPPVSAPAPAAAPIKTRTRRNKGSRAARGATRKDGLHGDGPRERATATVPDSSGGGGGGSGASQTGAANTRAARHWLPFQVLNSCPCKCYCHHQPRHRRLPRNVSAWLSTSTNHLGEPPWVATIKLSGSLVAKLEHYDLQATHSN
Protein: Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Mitochondrial assembly protein 1) (Processing enhancing protein) (PEP) (P10507)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. Preferentially, cleaves after an arginine at position P2 (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:3044780}.
Interaction partners:
- Cytochrome c oxidase subunit 4, mitochondrial
- Mitochondrial-processing peptidase subunit alpha
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Bud site selection protein 22
Sequence:
MFSRTASKFRNTRRLLSTISSQIPGTRTSKLPNGLTIATEYIPNTSSATVGIFVDAGSRAENVKNNGTAHFLEHLAFKGTQNRSQQGIELEIENIGSHLNAYTSRENTVYYAKSLQEDIPKAVDILSDILTKSVLDNSAIERERDVIIRESEEVDKMYDEVVFDHLHEITYKDQPLGRTILGPIKNIKSITRTDLKDYITKNYKGDRMVLAGAGAVDHEKLVQYAQKYFGHVPKSESPVPLGSPRGPLPVFCRGERFIKENTLPTTHIAIALEGVSWSAPDYFVALATQAIVGNWDRAIGTGTNSPSPLAVAASQNGSLANSYMSFSTSYADSGLWGMYIVTDSNEHNVQLIVNEILKEWKRIKSGKISDAEVNRAKAQLKAALLLSLDGSTAIVEDIGRQVVTTGKRLSPEEVFEQVDKITKDDIIMWANYRLQNKPVSMVALGNTSTVPNVSYIEEKLNQ
Protein: Insulin-like growth factor 2 (Insulin-like growth factor II) (I3PGL3)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
LQFVCGDRGFYFSRPSSRINRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSASTTVLPDDVTAYPVGKFFQYDIWKQSTQRLRRGLPAFLRARRGRTLAKELEALREAKSHRPLIALPTQDPATHGGASSKASSD
Protein: Friend leukemia integration 1 transcription factor (Proto-oncogene Fli-1) (Transcription factor ERGB) (Q01543)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcriptional activator. Recognizes the DNA sequence 5'-C[CA]GGAAGT-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:28255014}.
Interaction partners:
- F-box/WD repeat-containing protein 7
- Tripeptidyl-peptidase 1
- Endothelial transcription factor GATA-2
- Runt-related transcription factor 1
- RNA-binding protein EWS
- T-cell acute lymphocytic leukemia protein 1
- Runt-related transcription factor 2
- Transcription factor PU.1
- Transcriptional activator Myb
- Palmitoyl-protein thioesterase 1
Sequence:
MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLPPQQEWINQPVRVNVKREYDHMNGSRESPVDCSVSKCSKLVGGGESNPMNYNSYMDEKNGPPPPNMTTNERRVIVPADPTLWTQEHVRQWLEWAIKEYSLMEIDTSFFQNMDGKELCKMNKEDFLRATTLYNTEVLLSHLSYLRESSLLAYNTTSHTDQSSRLSVKEDPSYDSVRRGAWGNNMNSGLNKSPPLGGAQTISKNTEQRPQPDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSANASCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHPTESSMYKYPSDISYMPSYHAHQQKVNFVPPHPSSMPVTSSSFFGAASQYWTSPTGGIYPNPNVPRHPNTHVPSHLGSYY
Protein: Deazaflavin-dependent nitroreductase (EC 1.-.-.-) (F420H(2)-dependent quinone reductase Ddn) (Fqr) (EC 1.1.98.-) (P9WP15)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in a F420-dependent anti-oxidant mechanism that protects M.tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. In vitro, catalyzes the reduction of both benzoquinone and naphthoquinone analogs; since menaquinone is the sole quinone electron carrier in the respiratory chain in M.tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidation is therefore likely to be the endogenous menaquinone found in the membrane fraction of M.tuberculosis. Is able to use F420 species with two and five glutamate residues in its polyglutamate tail. Cannot use NADH or NADPH instead of F420H(2) as the electron donor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16000731}; Peripheral membrane protein {ECO:0000269|PubMed:16000731}.
Interaction partners:
- F420-dependent glucose-6-phosphate dehydrogenase
- Phosphoenolpyruvate transferase
- Bifunctional F420 biosynthesis protein FbiB
- FO synthase
- Phosphoenolpyruvate guanylyltransferase
- F420-dependent hydroxymycolic acid dehydrogenase
- Large ribosomal subunit protein uL3
- HTH-type transcriptional regulator MmpR5
- Steroid 3-ketoacyl-CoA thiolase
- F420H
Sequence:
MPKSPPRFLNSPLSDFFIKWMSRINTWMYRRNDGEGLGGTFQKIPVALLTTTGRKTGQPRVNPLYFLRDGGRVIVAASKGGAEKNPMWYLNLKANPKVQVQIKKEVLDLTARDATDEERAEYWPQLVTMYPSYQDYQSWTDRTIPIVVCEP
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FMM8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MSDAFEEVCDALKASFTDDKEDSLTLVTMIDTLSEEVDEGFEVKEKEQFLELLLNLLEADTELVSAVGWDLPRTLLRFCNAKNIKNSDRLRKCKVVTICMAIFNLLALHAKPQECLVTTLELLSELNFKNIVEECHQLSEDGSDNNTAEEDNDAVEDYMKDRDQPEIIFGVKSYALFELAGSLIRRVATLHPSKYLEEAVTAIRKYVTNNTEVVEDVKFILRRVFAFCRGYIPPEPPRQLIVDLKMNHEEYDEIMNSEIELQVRLLRNLCTFSVAYCVKFLNDKTEVVYFHKLINKDLQLPEFYRSVHDIISRYYQIAFSFDIDLNDEFNDILRETRGIYEDVIKRINETNNTDKNAKSDILLKAGYYYEVQKTAREKEINPDTKGIILLSGFNYIENGDHLIDIDIADALYLYLRFASESLFSPTCHNVTIEGVARYWIWAALTTTDNNILKEKLAELSPLVLHSVLNLLLVKNCHQVNEEIRMITFTLITRILCLLPENCSYEFLMDELDNCAVVFGKSCVLGILRDLVIKVDHSVSSNNTDTEDLSESMAQLKINNEKRAKKTFITLDPKRAGEIEDLAIKTLKETKKSMKKDYILLVLNYIKFFSTFAHKWNKSKLNEFTTLVATNFSDSKMLPEINAIIDANEKLRSLTE
Protein: Neural cell adhesion molecule 1 (N-CAM-1) (NCAM-1) (CD antigen CD56) (P13591)
Organism: Homo sapiens (Human)
Function: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted.; SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Major prion protein
- Low affinity immunoglobulin gamma Fc region receptor III-B
- Low affinity immunoglobulin gamma Fc region receptor III-A
- Neural cell adhesion molecule L1
- B-lymphocyte antigen CD19
- Neurocan core protein
- Cadherin-2
- Alpha-2,8-sialyltransferase 8B
- GDNF family receptor alpha-1
Sequence:
MLQTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQKLMFKNAPTPQEFREGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTIQARQNIVNATANLGQSVTLVCDAEGFPEPTMSWTKDGEQIEQEEDDEKYIFSDDSSQLTIKKVDKNDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEVQYAPKLQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDQVEPYSSTAQVQFDEPEATGGVPILKYKAEWRAVGEEVWHSKWYDAKEASMEGIVTIVGLKPETTYAVRLAALNGKGLGEISAASEFKTQPVQGEPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPANGSPTSGLSTGAIVGILIVIFVLLLVVVDITCYFLNKCGLFMCIAVNLCGKAGPGAKGKDMEEGKAAFSKDESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPEKGPVEAKPECQETETKPAPAEVKTVPNDATQTKENESKA
Protein: Argininosuccinate lyase (ASAL) (EC 4.3.2.1) (Arginosuccinase) (P11447)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Acetylglutamate kinase
- Argininosuccinate synthase
- N-acetyl-gamma-glutamyl-phosphate reductase
- Ornithine carbamoyltransferase subunit F
- Amino-acid acetyltransferase
- Acetylornithine deacetylase
- Ornithine carbamoyltransferase subunit I
- Acetylornithine/succinyldiaminopimelate aminotransferase
- Biodegradative arginine decarboxylase
- Adenylosuccinate lyase
Sequence:
MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESDAEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARLG
Protein: NAD-dependent dihydropyrimidine dehydrogenase subunit PreA (DPD) (EC 1.3.1.1) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) (P25889)
Organism: Escherichia coli (strain K12)
Function: Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT).
Interaction partners:
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreT
- D-phenylhydantoinase
- Probable pyruvate-flavodoxin oxidoreductase
- Putative oxidoreductase UacF
- Glutamate synthase small chain
- Putative oxidoreductase AegA
- Thymidine phosphorylase
- NAD
- Malate dehydrogenase
- Purine nucleoside phosphorylase DeoD-type
Sequence:
MLTKDLSITFCGVKFPNPFCLSSSPVGNCYEMCAKAYDTGWGGVVFKTIGFFIANEVSPRFDHLVKEDTGFIGFKNMEQIAEHPLEENLAALRRLKEDYPDKVLIASIMGENEQQWEELARLVQEAGADMIECNFSCPQMTSHAMGSDVGQSPELVEKYCRAVKRGSTLPMLAKMTPNIGDMCEVALAAKRGGADGIAAINTVKSITNIDLNQKIGMPIVNGKSSISGYSGKAVKPIALRFIQQMRTHPELRDFPISGIGGIETWEDAAEFLLLGAATLQVTTGIMQYGYRIVEDMASGLSHYLADQGFDSLQEMVGLANNNIVPAEDLDRSYIVYPRINLDKCVGCGRCYISCYDGGHQAMEWSEKTRTPHCNTEKCVGCLLCGHVCPVGCIELGEVKFKKGEKEHPVTL
Protein: DNA replication ATP-dependent helicase/nuclease DNA2 (DNA replication ATP-dependent helicase-like homolog) [Includes: DNA replication nuclease DNA2 (EC 3.1.-.-); DNA replication ATP-dependent helicase DNA2 (EC 3.6.4.12)] (Q6ZQJ5)
Organism: Mus musculus (Mouse)
Function: Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair: recruited by BLM and mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P51530}. Mitochondrion {ECO:0000250|UniProtKB:P51530}.
Interaction partners:
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Exonuclease 1
- WD repeat and HMG-box DNA-binding protein 1
- Flap endonuclease 1
- Replication protein A 70 kDa DNA-binding subunit
- RecQ-like DNA helicase BLM
- DNA topoisomerase 3-alpha
- RecQ-mediated genome instability protein 1
- ATP-dependent DNA helicase PIF1
- DNA polymerase epsilon catalytic subunit A
Sequence:
MEPLDELDLLLLEEDGGAEAVPRVELLRKKADALFPETVLSRGVDNRYLVLAVETSQNERGAEEKRLHVTASQDREHEVLCILRNGWSSVPVEPGDIVHLEGDCTSEPWIIDDDFGYFILYPDMMISGTSVASSIRCLRRAVLSETFRGSDPATRQMLIGTILHEVFQKAISESFAPERLQELALQTLREVRHLKEMYRLNLSQDEILCEVEEYLPSFSKWAEDFMRKGPSSEFPQMQLSLPSDGSNRSSPCNIEVVKSLDIEESIWSPRFGLKGKIDVTVGVKIHRDCKMKYKVMPLELKTGKESNSIEHRSQVVLYTLLSQERREDPEAGWLLYLKTGQMYPVPANHLDKRELLKLRNWLAASLLHRVSRAAPGEEARLSALPQIIEEEKTCKYCSQIGNCALYSRAVEEQGDDASIPEAMLSKIQEETRHLQLAHLKYFSLWCLMLTLESQSKDNRKTHQSIWLTPASELEESGNCVGNLVRTEPVSRVCDGQYLHNFQRKNGPMPATNLMAGDRIILSGEERKLFALSKGYVKKMNKAAVTCLLDRNLSTLPATTVFRLDREERHGDISTPLGNLSKLMESTDPSKRLRELIIDFREPQFIAYLSSVLPHDAKDTVANILKGLNKPQRQAMKRVLLSKDYTLIVGMPGTGKTTTICALVRILSACGFSVLLTSYTHSAVDNILLKLAKFKVGFLRLGQSHKVHPDIQKFTEEEICRSRSIASLAHLEELYNSHPIVATTCMGINHPIFSRKTFDFCIVDEASQISQPVCLGPLFFSRRFVLVGDHQQLPPLVVNREARALGMSESLFKRLERNESAVVQLTVQYRMNRKIMSLSNKLTYAGKLECGSDRVANAVLALPNLKDARLSLQLYADYSDSPWLAGVLEPDNPVCFLNTDKVPAPEQVENGGVSNVTEARLIVFLTSTFIKAGCSPSDIGVIAPYRQQLRIISDLLARSSVGMVEVNTVDKYQGRDKSLILVSFVRSNEDGTLGELLKDWRRLNVALTRAKHKLILLGSVSSLKRFPPLGTLFDHLNAEQLILDLPSREHESLSHILGDCQRD
Protein: Coiled-coil domain-containing protein lobo (Lost boys protein) (Q4V516)
Organism: Drosophila melanogaster (Fruit fly)
Function: Key component of the nexin-dynein regulatory complex (N-DRC), essential for N-DRC integrity. Involved in the regulation of flagellar motility (By similarity). Involved in sperm motility. Required for the sperm to enter in the coiled storage seminal receptacle (SR) tubule.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:21289096}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8JAM0}. Note=Detected as regular puncta along the flagellum. {ECO:0000269|PubMed:21289096}.
Interaction partners:
- Dynein regulatory complex subunit 4
Sequence:
MPKVLFQKYKKVVSNIDPSRYSAKFKEIDEQRRSQGSESDFADEMEGEFEAEMEEMGSSEFSLSEGEPSLNIGKIDLSFPETVEEFENSPQCYPPSYYTLSPKERLLLLYAENFRKQLVLSYPKRRAMVLALPNECKVQKFVCTTIRPTAFIYTQLISSVEEIAKFVADFIQYEPLQDPINLPNRLISPETLLRKRKGNSYEMATLLVSMLIGAGHPALVVSGVAREETILNDQLAVPYPYPIVEVEVEEVKPKVEKPGQKYKLRGLPDLKSHLEEDMAEVHRQKEAEEKRIQDEIIRKQMEDLELLAVDRYHYRRSHAWVVIINNAPWSVKPKTTYTDVNGDVVEAPPTAIFIEPSTGFICETGCKQYILVDSIWNEYNYYVCKQKHQRVSELRWDLRDTKDWEHMLPGEPPEMRIYKMASDENVADEERDISEEKHLDCIGSWVERLHIGLADFEQRFPSSEKKIQYKGAIHERFSPYSQRDGKVMQLTIFNNDECTIPKVRYEYYENRSDLMRHVKYTYATDQFEEIFNKGRNDSLKSIEYFSDPSQQRKVHFFSASRIDSLELMVVEPGSLILHYKDRSDKCWYKEFEFTPAGNVLKKVTEKFLKASANDVCSNDIATRTFLFQQNKIVLKFHYTFGALTATVVEFTKPPRPDYGKELIYDEKLTKIYKANPLDPTRTNLELYRLLCEQLQYEDHLRKNFEKIFEDINNVFDLRKSEKAEPKLKFSIFDPLRNGAARAIRMRQFEEEEELKKEIASKPADFLAPYLVPYKHQEELTPEQSQNAYNACLNDLKSRFVSLLNNLQRHYEDLTSESKSLNRFLNKFENQFNNYDYKRLVQQSKDLELNKRMVQQRLTLTHEESQKKYEVVKNSLLKDPRLNFKKDDLARRASETSK
Protein: NK-tumor recognition protein (NK-TR protein) (Natural-killer cells cyclophilin-related protein) (Peptidyl-prolyl cis-trans isomerase NKTR) (PPIase) (EC 5.2.1.8) (Rotamase) (P30414)
Organism: Homo sapiens (Human)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Component of a putative tumor-recognition complex involved in the function of NK cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8421688}.
Interaction partners:
- Arginine/serine-rich protein PNISR
- Activator of 90 kDa heat shock protein ATPase homolog 1
- Serine/arginine-rich splicing factor 11
- Dual specificity protein kinase CLK1
- Stress-induced-phosphoprotein 1
- Interleukin-2 receptor subunit beta
- Prostaglandin E synthase 3
Sequence:
MGAQDRPQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGGESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVIDCGVLATKSIKDVFEKKRKKPTHSEGSDSSSNSSSSSESSSESELEHERSRRRKHKRRPKVKRSKKRRKEASSSEEPRNKHAMNPKGHSERSDTNEKRSVDSSAKREKPVVRPEEIPPVPENRFLLRRDMPVVTAEPEPKIPDVAPIVSDQKPSVSKSGRKIKGRGTIRYHTPPRSRSCSESDDDDSSETPPHWKEEMQRLRAYRPPSGEKWSKGDKLSDPCSSRWDERSLSQRSRSWSYNGYYSDLSTARHSGHHKKRRKEKKVKHKKKGKKQKHCRRHKQTKKRRILIPSDIESSKSSTRRMKSSCDRERSSRSSSLSSHHSSKRDWSKSDKDVQSSLTHSSRDSYRSKSHSQSYSRGSSRSRTASKSSSHSRSRSKSRSSSKSGHRKRASKSPRKTASQLSENKPVKTEPLRATMAQNENVVVQPVVAENIPVIPLSDSPPPSRWKPGQKPWKPSYERIQEMKAKTTHLLPIQSTYSLANIKETGSSSSYHKREKNSESDQSTYSKYSDRSSESSPRSRSRSSRSRSYSRSYTRSRSLASSHSRSRSPSSRSHSRNKYSDHSQCSRSSSYTSISSDDGRRAKRRLRSSGKKNSVSHKKHSSSSEKTLHSKYVKGRDRSSCVRKYSESRSSLDYSSDSEQSSVQATQSAQEKEKQGQMERTHNKQEKNRGEEKSKSERECPHSKKRTLKENLSDHLRNGSKPKRKNYAGSKWDSESNSERDVTKNSKNDSHPSSDKEEGEATSDSESEVSEIHIKVKPTTKSSTNTSLPDDNGAWKSSKQRTSTSDSEGSCSNSENNRGKPQKHKHGSKENLKREHTKKVKEKLKGKKDKKHKAPKRKQAFHWQPPLEFGEEEEEEIDDKQVTQESKEKKVSENNETIKDNILKTEKSSEEDLSGKHDTVTVSSDLDQFTKDDSKLSISPTALNTEENVACLQNIQHVEESVPNGVEDVLQTDDNMEICTPDRSSPAKVEETSPLGNARLDTPDINIVLKQDMATEHPQAEVVKQESSMSESKVLGEVGKQDSSSASLASAGESTGKKEVAEKSQINLIDKKWKPLQGVGNLAAPNAATSSAVEVKVLTTVPEMKPQGLRIEIKSKNKVRPGSLFDEVRKTARLNRRPRNQESSSDEQTPSRDDDSQSRSPSRSRSKSETKSRHRTRSVSYSHSRSRSRSSTSSYRSRSYSRSRSRGWYSRGRTRSRSSSYRSYKSHRTSSRSRSRSSSYDPHSRSRSYTYDSYYSRSRSRSRSQRSDSYHRGRSYNRRSRSCRSYGSDSESDRSYSHHRSPSESSRYS
Protein: Protein QUA-QUINE STARCH (Q3E7K4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in regulating carbon and nitrogen allocation to starch and protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19154206}.
Interaction partners:
- Nuclear transcription factor Y subunit C-4
- Transmembrane protein
- Protein indeterminate-domain 14
- Senescence-associated and QQS-related protein
- Transmembrane protein
- At1g58243/At1g58243
- At4g12005
- Small EDRK-rich factor-like N-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MKTNREQEIYVERSFKPNNSTIQNLMDIERFILPHTSTSGVARLKMRVISWVGLQFYNY
Protein: Photosystem II reaction center protein L (PSII-L) (Q2LIM1)
Organism: Oryza sp. IRGC 81916
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01317}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01317}.
Interaction partners:
Sequence:
MTQSNPNEQNVELNRTSLYWGLLLIFVLAVLFSNYFFN
Protein: dihydrofolate reductase (EC 1.5.1.3) (Q6IQS4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSRILNCIVAVCPDMGIGKNGNLPWHPIRLSNELKHFQKMTMTPSDEGKKNVVIMGRKTWFSIPAAHRPLKNRINIVLSRELKTAPEGAHYLASDFSSALHLLDSGELEKLVDQVWIIGGSSLYKEVMERSGHRRLFVTRILKQFDCDTFIPNFDMDKYKLLPEFPGVPVGLQEDNGVQYLFEVYESIKH
Protein: Xylulose kinase (XK) (Xylulokinase) (EC 2.7.1.17) (1-deoxy-D-xylulokinase) (EC 2.7.1.-) (P09099)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. Also catalyzes the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. Can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. Has a weak substrate-independent Mg-ATP-hydrolyzing activity.
Interaction partners:
- Xylose isomerase
- L-ribulose-5-phosphate 4-epimerase AraD
- Ribulose-phosphate 3-epimerase
- L-ribulose-5-phosphate 4-epimerase SgbE
- L-ribulose-5-phosphate 4-epimerase UlaF
- D-xylose-binding periplasmic protein
- Xylose operon regulatory protein
- D-xylose-proton symporter
- Xylose import ATP-binding protein XylG
- Ribulokinase
Sequence:
MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLLPLMA
Protein: Leucine-rich-repeats and calponin homology domain protein, isoform C (X2JA56)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAATVYQRLHSVAVGVGSAAGSAIGSGSASLPGSGTGSGSGIGHAGNTSSSTSSALLSHSQLTRSLERILEEAHFSGELILTNRKLKDFPRTGTKYSLTDTVIADLSRNRFAELPEEVTTFAFLETLLLYHNTIRSIPESVKQLSSLTYLDLRSNQLSSLPREICFLPLQVLLVSNNRLTSLPDELGRLDQTLTDLDASYNQLANLPARLGELRSLRSLSLRSNHLLYLPRELTCLSLISLDVSNNKIASLPLEIRHMSTLVELQLENNPLTSPPASLCMRGLVHVFKFLETQATKDEKGSRSGGNYDGYTTLRRAPRHNSSGNVLEASTTGSTNNQRRHQVDSGYNTSDGLDKRWSHDAPTKSKTDSPLHCVSNSTAATLPRTLPSAVHSQADLMDASLTSSTSTIVDESLTLSPTASPCKLSYAHSNSSSNGSSPDQDDDIMLDHQERTVHHANGRSGKGLGNIQTYKEYKEALKQQRNQEISVYKQKHPNANHSPNDDEDLSPSPPSISNGSSSNTLPKSIMKQNSNQIGHNGNGNGSANGNGVDDVVIPKKPIQKVIPSRITEIKPASTSDIRSANSSDCLGYVKPQSPMKNGTSKFNTSNGGGVQTTVGIVSSTTIKSPVSSTTKLGTVKTHRSVTWNHDIPAEKLSFTMRREFDRQREETELMSQLRTIIETRLKMTLPVDIASALTDGVILCHLANYVRPRSVASIHVPSPGVNKLTMARCRRNVDNFLEACRRIGVDEELICSCEDVVPQIEPQQPQLPRADDDYDADVYVQDDGSISRSNDSSHLQCSDDCNSSSNHINRVPNALALLRTVSALIAMDENPYHQQLHHHLQLQLEQQHFEQEQFSEPTTCSQQQEQMLLLQQQQQQLEHVLYENGLPRAENDDGVEDRDDDIGKRQQQLATVGQMLLKAKQKTYEKIKHNLLSAHGQHNFQGNNNNRMLHTIVENEHDVAAAGPAGHYQIIDEKQEEDPYQPKSEDLKDAAALGNATKEAISKRIEFFEQQKSGKPKLEVFSIYLPKEKTKELELEQKIKAKTNEAGSSILKHDSHTLTVILSCVFIATFLWLVFFPLPG
Protein: Transcription factor PIF1 (Basic helix-loop-helix protein 15) (AtbHLH15) (bHLH 15) (Phytochrome-interacting factor 1) (Protein PHYTOCHROME INTERACTING FACTOR 3-LIKE 5) (Transcription factor EN 101) (bHLH transcription factor bHLH015) (Q8GZM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator. Regulates negatively chlorophyll biosynthesis and seed germination in the dark, and lightinduced degradation of PIF1 relieves this negative regulation to promote photomorphogenesis. Binds to the G-box motif (5'-CACGTG-3') found in many light-regulated promoters. Promotes the expression of SOM, and thus modulates responses to abscisic acid (ABA) and gibberellic acid (GA).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15448264, ECO:0000269|PubMed:16359394}.
Interaction partners:
- Phytochrome B
- Phytochrome A
- DELLA protein RGA
- Transcription factor HY5
- Dof zinc finger protein DOF3.7
- DELLA protein GAI
- Gibberellin 3-beta-dioxygenase 1
- B3 domain-containing transcription factor ABI3
- Gibberellin 3-beta-dioxygenase 2
- DELLA protein RGL2
Sequence:
MHHFVPDFDTDDDYVNNHNSSLNHLPRKSITTMGEDDDLMELLWQNGQVVVQNQRLHTKKPSSSPPKLLPSMDPQQQPSSDQNLFIQEDEMTSWLHYPLRDDDFCSDLLFSAAPTATATATVSQVTAARPPVSSTNESRPPVRNFMNFSRLRGDFNNGRGGESGPLLSKAVVRESTQVSPSATPSAAASESGLTRRTDGTDSSAVAGGGAYNRKGKAVAMTAPAIEITGTSSSVVSKSEIEPEKTNVDDRKRKEREATTTDETESRSEETKQARVSTTSTKRSRAAEVHNLSERKRRDRINERMKALQELIPRCNKSDKASMLDEAIEYMKSLQLQIQMMSMGCGMMPMMYPGMQQYMPHMAMGMGMNQPIPPPSFMPFPNMLAAQRPLPTQTHMAGSGPQYPVHASDPSRVFVPNQQYDPTSGQPQYPAGYTDPYQQFRGLHPTQPPQFQNQATSYPSSSRVSSSKESEDHGNHTTG