wanglab/gogpt-training-data huggingface dataset:
Protein: Translocation protein SEC62 (Translocation protein 1) (TP-1) (hTP-1) (Q99442)
Organism: Homo sapiens (Human)
Function: Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein transport protein Sec61 subunit alpha isoform 1
- Translocation protein SEC63 homolog
- Protein transport protein Sec61 subunit gamma
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit alpha isoform 2
- Serine/threonine-protein kinase OSR1
- STE20/SPS1-related proline-alanine-rich protein kinase
- Reticulophagy regulator 1
- Cell cycle progression protein 1
- Reticulon-3
Sequence:
MAERRRHKKRIQEVGEPSKEEKAVAKYLRFNCPTKSTNMMGHRVDYFIASKAVDCLLDSKWAKAKKGEEALFTTRESVVDYCNRLLKKQFFHRALKVMKMKYDKDIKKEKDKGKAESGKEEDKKSKKENIKDEKTKKEKEKKKDGEKEESKKEETPGTPKKKETKKKFKLEPHDDQVFLDGNEVYVWIYDPVHFKTFVMGLILVIAVIAATLFPLWPAEMRVGVYYLSVGAGCFVASILLLAVARCILFLIIWLITGGRHHFWFLPNLTADVGFIDSFRPLYTHEYKGPKADLKKDEKSETKKQQKSDSEEKSDSEKKEDEEGKVGPGNHGTEGSGGERHSDTDSDRREDDRSQHSSGNGNDFEMITKEELEQQTDGDCEEDEEEENDGETPKSSHEKS
Protein: Proton-coupled zinc antiporter SLC30A9, mitochondrial (GRIP1-associated coactivator 63) (GAC63) (Solute carrier family 30 member 9) (Zinc transporter 9) (ZnT-9) (Q5IRJ6)
Organism: Mus musculus (Mouse)
Function: Acts as a zinc transporter involved in intracellular zinc homeostasis (By similarity). Functions as a secondary coactivator for nuclear receptors by cooperating with p160 coactivators subtypes. Plays a role in transcriptional activation of Wnt-responsive genes.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:Q6PML9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6PML9}. Nucleus {ECO:0000269|PubMed:11906820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6PML9}. Note=Partial co-localization with endoplasmic reticulum. Linked to mitochondrial ribosomes. {ECO:0000250|UniProtKB:Q6PML9}.
Interaction partners:
- Proton-coupled zinc antiporter SLC30A5
- Zinc transporter 6
- Zinc transporter ZIP11
- Zinc transporter 7
- Zinc transporter SLC39A7
- Zinc transporter ZIP9
- Probable proton-coupled zinc antiporter SLC30A4
- Proton-coupled zinc antiporter SLC30A1
- Proton-coupled zinc antiporter SLC30A2
- Probable proton-coupled zinc antiporter SLC30A3
Sequence:
MFPGLAAAAAAHRCSWAALCRLGGGRAATRGRSQGWKNVMTFESFTYVVPDIHPHLSIINQVKLYSTNVQKGGQGSQTPKADKVPSLTQTVENIGAELKAPLKQDPLQVRVKAVLKKRDYGSKYTKNNFITGVRAINEFCLKSSDLEQLRKIRRRSPHDDTESFTVFLRSDVEAKALEVWGSLEALAREKKLRKEAEIEYRERLFRNQRILREYGDFLGNTKPRSRAVSVFLKGPGKVVMVAICINGLNCFFKFLAWIYTGSASMFSEAIHSLSDTCNQGLLALGISKSVQTPDPSHPYGFSNMRYISSLISGVGIFMMGAGLSWYHGIMGLLHPQPMESLLWAYCILAGSLVSEGATLLVAINELRRSAQAKGTTFYKYVMESRDPSTNVILLEDTAAVLGVIIAATCMGLTSITGNPLYDSLGSLGVGTLLGVVSAFLIYTNTEALLGRSIQPEQVQRLTELLESDPSVRAIHDVKATDLGLGKVRFKAEVDFDGRVVTRSYLEKQDFDQMMQEIQEVKTPEQLEAFMLKHGENIIDTLGAEVDRLEKELKKRNPEVRHVDLEIL
Protein: DBF2 kinase activator protein MOB1 (MPS1 binder 1) (Maintenance of ploidy protein MOB1) (P40484)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as an activator subunit for the DBF2 protein kinase. Binds to DBF2, which is required for the phosphorylation and activation of DBF2 by the upstream kinase CDC15 in late anaphase. DBF2-MOB1 is part of the mitotic exit network (MEN) signaling cascade, which regulates release from the nucleus and activity of phosphatase CDC14. Required for inactivation of mitotic cyclin-dependent kinase for exit from mitosis, cytokinesis and G1 gene transcription.
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Bud neck. Chromosome, centromere. Note=Localizes predominantly to the cytoplasmic surface of the spindle pole body during anaphase and to a ring at the bud neck during cytokinesis. Translocates to the nucleus during mitosis and associates with centromere DNA.
Interaction partners:
- Serine/threonine-protein kinase DBF20
- Cell cycle protein kinase DBF2
- Nucleolar protein NET1
- Cell division control protein 15
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Tyrosine-protein phosphatase CDC14
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Protein TEM1
- Serine/threonine-protein kinase CBK1
Sequence:
MSFLQNFHISPGQTIRSTRGFKWNTANAANNAGSVSPTKATPHNNTINGNNNNANTINNRADFTNNPVNGYNESDHGRMSPVLTTPKRHAPPPEQLQNVTDFNYTPSHQKPFLQPQAGTTVTTHQDIKQIVEMTLGSEGVLNQAVKLPRGEDENEWLAVHCVDFYNQINMLYGSITEFCSPQTCPRMIATNEYEYLWAFQKGQPPVSVSAPKYVECLMRWCQDQFDDESLFPSKVTGTFPEGFIQRVIQPILRRLFRVYAHIYCHHFNEILELNLQTVLNTSFRHFCLFAQEFELLRPADFGPLLELVMELRDR
Protein: S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) (F4K7D6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MATQGQVITCKGTFILDPRTLTISAVAYEPNKPLVIEDVQVAPPQAGEVRIKILYTALCHTDAYTWSGKDPEGLFPCILGHEAAGIVESVGEGVTEVQAGDHVIPCYQAECRECKFCKSGKTNLCGKVRSATGVGIMMNDRKSRFSVNGKPIYHFMGTSTFSQYTVVHDVSVAKIDPTAPLDKVCLLGCGVPTGLGAVWNTAKVEPGSNVAIFGLGTVGLAVAEGAKTAGASRIIGIDIDSKKYETAKKFGVNEFVNPKDHDKPIQEVIVDLTDGGVDYSFECIGNVSVMRAALECCHKGWGTSVIVGVAASGQEISTRPFQLVTGRVWKGTAFGGFKSRTQVPWLVEKYMNKEIKVDEYITHNLTLGEINKAFDLLHEGTCLRCVLDTSK
Protein: Beta-defensin 126 (Beta-defensin 26) (DEFB-26) (Defensin, beta 126) (Epididymal secretory protein 13.2) (ESP13.2) (HBD26) (Q9BYW3)
Organism: Homo sapiens (Human)
Function: Highly glycosylated atypical beta-defensin involved in several aspects of sperm function. Facilitates sperm transport in the female reproductive tract and contributes to sperm protection against immunodetection; both functions are probably implicating the negative surface charge provided by its O-linked oligosaccharides in the sperm glycocalyx. Involved in binding of sperm to oviductal epithelial cells to form a sperm reservoir until ovulation. Release from the sperm surface during capacitation and ovaluation by an elevation of oviductal fluid pH is unmasking other surface components and allows sperm to penetrate the cumulus matrix and bind to the zona pellucida of the oocyte (By similarity). In vitro has antimicrobial activity and may inhibit LPS-mediated inflammation.
Subcellular location: Secreted {ECO:0000305}. Note=Secreted by epididymal cells and is absorbed to the surface of sperm during transit through the epididymis (By similarity). Mainly located on the sperm acrosome. {ECO:0000250|UniProtKB:Q9BEE3, ECO:0000269|PubMed:26832966}.
Interaction partners:
- Defensin beta 118
- Beta-defensin 127
- Beta-defensin 114
- Beta-defensin 129
- Beta-defensin 128
- Beta-defensin 106
- Beta-defensin 125
- Beta-defensin 113
- Beta-defensin 1
- Beta-defensin 121
Sequence:
MKSLLFTLAVFMLLAQLVSGNWYVKKCLNDVGICKKKCKPEEMHVKNGWAMCGKQRDCCVPADRRANYPVFCVQTKTTRISTVTATTATTTLMMTTASMSSMAPTPVSPTG
Protein: Rrp4p homologue (Q95Z16)
Organism: Trypanosoma brucei
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSVPTCITGDTICGSAGPSKLDYVEDHVFLRGYNTYEGNNPNGAAAAQEGGGEIIASINGMVEVTDRVVSVKGMSSRYVAEVGDIVVGRVKEVCGNRWRVDVGAFQDAVMPLANVTEPGGILRRRGRSDELTMRNIFDEGELVVAEVQRVSQDGLISLHTRSGEKYGKLSDFGLLVLISPALVKRVKHHFMCLEFIHVNLVLGTNGAIWVSPATATTATESAKSAYDRFDADIRRAVTRVANCIRVMGNARFPVFDKSIEAAVKASIDFVLGPFEILYPGNQNLITTTVLDTINTRKRTIY
Protein: Beta-amylase 2, chloroplastic (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) (Beta-amylase 9) (O65258)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low beta-amylase activity. Interacts poorly with starch or other alpha-1,4-glucan.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:18431481}.
Interaction partners:
- 4-alpha-glucanotransferase DPE2
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Isoamylase 3, chloroplastic
- alpha-D-xyloside xylohydrolase
- Alpha-amylase 3, chloroplastic
- Alpha-glucan phosphorylase 1
- Probable alpha-amylase 2
- Isoamylase 2, chloroplastic
- Alpha-amylase 1
- Alpha-glucan phosphorylase 2, cytosolic
Sequence:
MAIRLNHSVIPVSVKLGAPTRVSARSSLPFSVGDWRGVSTFSGARPLVLAKVKLRAESTEEDRVPIDDDDDSTDQLVDEEIVHFEERDFAGTACVPVYVMLPLGVIDMNSEVVEPEELLDQLRTLKSVNVDGVMVDCWWGIVESHTPQVYNWSGYKKLFQMIRELGLKIQVVMSFHECGGNVGDDVHIQIPEWVREIGQSNPDIYFTDSAGRRNTECLTWGIDKQRVLRGRTALEVYFDYMRSFRVEFDEFFEEKIIPEIEVGLGPCGELRYPSYPAQFGWKYPGIGEFQCYDKYLMNSLKEAAEVRGHSFWGRGPDNTETYNSTPHGTGFFRDGGDYDSYYGRFFLNWYSRVLIDHGDRVLAMANLAFEGTCIAAKLSGIHWWYKTASHAAELTAGFYNSSNRDGYGPIAAMFKKHDAALNFTCVELRTLDQHEDFPEALADPEGLVWQVLNAAWDASIPVASENALPCYDREGYNKILENAKPLTDPDGRHLSCFTYLRLNPTLMESQNFKEFERFLKRMHGEAVPDLGLAPGTQETNPE
Protein: LD17594p (Q95RP4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MECIIQVFPDEFHLKTLDPFLKSCAQLETGVNVKNIIISLIERLAAYNQRSGKTSGNAIDAIIPAEVELFEVFSVQVANIVQTRMDMPLEDTISLQVALLSLAQKVYPDRVDYVDKVLGTTAQILQRMNMNNISHLLSVNQELSRLLRICIDFYNNALTIIQLQNFCPLLEKFDYTSRKSLALYLVMNILDNETLVPTADQADSLLTIITPLIKDDDTNKENGAAAGNTTPDAEEFAEEQGVVARFIHLMRSDEPDMQYKMLQTARKHLGNGGGQRLKHVLPPLVFAAYQLAFKYKAIAEQDENWDKKCQKIVQYCHSTISALAKADLADLALRLYLQGALVIGEIGYTNHETVAYEFMTQAFSLYEDEISDSKAQLAAITLIMSTFEQMSCFGEENAEPLRTNCALAASKLLKKPDQCRGVVACAALFWSGKQNGEEMRDEKRTLDCLKKGARIASQCLDTGVQVQLYVELLNHYLFYFERGNSLITVAMLNQLIAKVNEELPNLEPSEETKQIESHYKNTLAHIRSRMESNDSSLEVSFAGITLN
Protein: Heat shock 70 kDa protein 4L (Heat shock 70-related protein APG-1) (Heat shock protein family H member 3) (Heat-shock protein family A member 4-like protein) (HSPA4-like protein) (Osmotic stress protein 94) (O95757)
Organism: Homo sapiens (Human)
Function: Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=May translocate to the nucleus after heat shock. {ECO:0000250}.
Interaction partners:
- DnaJ homolog subfamily B member 1
- Heat shock cognate 71 kDa protein
- Hsp70-binding protein 1
- BAG family molecular chaperone regulator 2
- BAG family molecular chaperone regulator 1
- Heat shock protein 105 kDa
- Endoplasmic reticulum chaperone BiP
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Heat shock 70 kDa protein 12A
Sequence:
MSVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRTRAIGNAAKSQIVTNVRNTIHGFKKLHGRSFDDPIVQTERIRLPYELQKMPNGSAGVKVRYLEEERPFAIEQVTGMLLAKLKETSENALKKPVADCVISIPSFFTDAERRSVMAAAQVAGLNCLRLMNETTAVALAYGIYKQDLPPLDEKPRNVVFIDMGHSAYQVLVCAFNKGKLKVLATTFDPYLGGRNFDEALVDYFCDEFKTKYKINVKENSRALLRLYQECEKLKKLMSANASDLPLNIECFMNDLDVSSKMNRAQFEQLCASLLARVEPPLKAVMEQANLQREDISSIEIVGGATRIPAVKEQITKFFLKDISTTLNADEAVARGCALQCAILSPAFKVREFSITDLVPYSITLRWKTSFEDGSGECEVFCKNHPAPFSKVITFHKKEPFELEAFYTNLHEVPYPDARIGSFTIQNVFPQSDGDSSKVKVKVRVNIHGIFSVASASVIEKQNLEGDHSDAPMETETSFKNENKDNMDKMQVDQEEGHQKCHAEHTPEEEIDHTGAKTKSAVSDKQDRLNQTLKKGKVKSIDLPIQSSLCRQLGQDLLNSYIENEGKMIMQDKLEKERNDAKNAVEEYVYDFRDRLGTVYEKFITPEDLSKLSAVLEDTENWLYEDGEDQPKQVYVDKLQELKKYGQPIQMKYMEHEERPKALNDLGKKIQLVMKVIEAYRNKDERYDHLDPTEMEKVEKCISDAMSWLNSKMNAQNKLSLTQDPVVKVSEIVAKSKELDNFCNPIIYKPKPKAEVPEDKPKANSEHNGPMDGQSGTETKSDSTKDSSQHTKSSGEMEVD
Protein: T cell receptor delta, constant region (A0A0G2JEU3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XSQPPAKPSVFIMKNGTNVACLVKDFYPKEVTISLRSSKKIVEFDPAIVISPSGKYSAVKLGQYGDSNSVTCSVQHNSETVHSTDFEPYANSFNNEKLPEPENDTQISEPCYGPRVTVHTEKVNMMSLTVLGLRLLFAKTIAINFLLTVKLFF
Protein: Adenosine 5'-monophosphoramidase HINT2 (EC 3.9.1.-) (HINT-3) (HIT-17kDa) (Histidine triad nucleotide-binding protein 2, mitochondrial) (HINT-2) (PKCI-1-related HIT protein) (Q9BX68)
Organism: Homo sapiens (Human)
Function: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Hydrolyzes adenosine 5'-O-p-nitrophenylphosphoramidate (AMP-pNA). Hydrolyzes fluorogenic purine nucleoside tryptamine phosphoramidates in vitro. May be involved in steroid biosynthesis. May play a role in apoptosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16762638, ECO:0000269|PubMed:18653718}.
Interaction partners:
- Adenosine 5'-monophosphoramidase HINT3
Sequence:
MAAAVVLAAGLRAARRAVAATGVRGGQVRGAAGVTDGNEVAKAQQATPGGAAPTIFSRILDKSLPADILYEDQQCLVFRDVAPQAPVHFLVIPKKPIPRISQAEEEDQQLLGHLLLVAKQTAKAEGLGDGYRLVINDGKLGAQSVYHLHIHVLGGRQLQWPPG
Protein: Lysine-specific demethylase JMJ28 (EC 1.14.11.-) (Jumonji domain-containing protein 28) (AtJMJ28) (Protein JUMONJI 28) (Lysine-specific histone demethylase JMJ28) (Protein B160) ([histone H3]-trimethyl-L-lysine monodemethylase JMJ28) (Q8H1S7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function as histone H3 lysine demethylase and be involved in regulation of gene expression (By similarity). Regulates flowering time by promoting CONSTANS (CO) and CONSTANS-LIKE genes (e.g. COL2 and COL5) expression via interaction with FBH transcription factors (FBH1, FBH2, FBH3 and FBH4) at their loci to remove H3K9me2 repressive histone marks. Modulates also the expression of several develpmental genes such as MYB30, TFS1, AGL6 and RVE2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:33604650}.
Interaction partners:
- E3 ubiquitin-protein ligase JMJ24
- Lysine-specific demethylase JMJ26
- Histone H3-lysine
- Histone-lysine N-methyltransferase ATX4
- Histone-lysine N-methyltransferase ATX2
- Histone-lysine N-methyltransferase ATX3
- Histone-lysine N-methyltransferase ATX5
- Transcription factor bHLH103
- Subtilisin-like protease SBT3.1
- Pentatricopeptide repeat-containing protein At4g21170
Sequence:
MSENEIVPDEFRCNRSDGKQWRCKRRALEGKKMCESHHSQQSLKRSKQKVAESSKLVRSRRGGGDEVASSEIEPNESRIRSKRLGKSKRKRVMGEAEAMDEAVKKMKLKRGDLQLDLIRMVLKREVEKRKRLPNSNNKKKSNGGFSEFVGEELTRVLPNGIMAISPPSPTTSNVSSPCDVKVGEEPISMIKRRFRSKNIEPLPIGKMQVVPFKGDLVNGRKEKKMRCHWCGTRGFGDLISCLSCEREFFCIDCIEKRNKGSKEEVEKKCPVCRGSCRCKVCSVTNSGVTECKDSQSVRSDIDRVLHLHYAVCMLLPVLKEINAEHKVEVENDAEKKEGNPAEPQIHSSELTSDDRQPCSNGRDFAVVDLQRMCTRSSSVLRLNSDQDQSQESLSRKVGSVKCSNGIKSPKVCKRKEVKGCSNNLFLSLFPLELTSKLEISAEEVVSCYELPEILDKYSGCPFCIGMETQSSSSDSHLKEASKTREDGTGNFLYYPTVLDFHQNNLEHFQTHWSKGHPVIVRSVIKSGSSLNWDPVALFCHYLMNRNNKTGNTTDCMDWFEVEIGVKQFFLGSLRGKAETNTCQERLKLEGWLSSSLFKEQFPNHYAEILNILPISHYMDPKRGLLNIAANLPDTVQPPDFGPCLNISYRSGEEYAQPDSVKKLGFETCDMVDILLYVTETPVSTNQICRIRKLMKNIGRVRSKNPAKGRESRFDKGKKRDRLDDYSSSDSESSQHCLGAKCRGSEFEGEERESCNYSCEEESLSNTYGAQWDVFQKQDVSKLLEYIKNHSLELESMDSSKKKVSHPLLEQSYYLDEYHKARLKEEFDVEPWSFDQCVGEAVILPAGCPYQIRKNKSCVNAVLKFLSPEHVSESIKRVKELNQLPQSVKSKANKIEVKKMAIHKISEAVKEIRELTSSDSTGALRLYN
Protein: WIZ protein (WIZ zinc finger) (B9EGQ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDLGSPSLPKKSLPVPGALEQVASRLSSKVAAEVPHGSKQELQDLKAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP
Protein: Small ribosomal subunit protein uS14c (30S ribosomal protein S14, chloroplastic) (P0C465)
Organism: Oryza sativa (Rice)
Function: Binds 16S rRNA, required for the assembly of 30S particles.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MAKKSLIQRERKRQKLEQKYHLIRRSSKKKIRSKVYPLSLSEKTKMREKLQSLPRNSAPTRLHRRCFLTGRPRANYRDFGLSGHILREMVYACLLPGATRSSW
Protein: THO complex subunit MFT1 (Mitochondrial fusion target protein 1) (P33441)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:11060033, ECO:0000269|PubMed:14562095}.
Interaction partners:
- THO complex subunit HPR1
- THO complex subunit 2
- THO complex subunit THP2
- ATP-dependent RNA helicase SUB2
- Protein TEX1
- Nuclear cap-binding protein subunit 2
- RNA annealing protein YRA1
- Small ribosomal subunit protein eS1B
- Mitochondrial import receptor subunit TOM20
- CTD kinase subunit alpha
Sequence:
MPLSQKQIDQVRTKVHYSEVDTPFNKYLDILGKVTKLTGSIINGTLSNDDSKIEKLTEQNISQLKESAHLRFLDLQSSIDTKKVADENWETCQQETLAKLENLKDKLPDIKSIHSKLLLRIGKLQGLYDSVQVINREVEGLSEGRTSLVVTRAEWEKELGTDLVKFLIEKNYLKLVDPGLKKDSSEERYRIYDDFSKGPKELESINASMKSDIENVRQEVSSYKEKWLRDAEIFGKITSIFKEELLKRDGLLNEAEGDNIDEDYESDEDEERKERFKRQRSMVEVNTIENVDEKEESDHEYDDQEDEENEEEDDMEVDVEDIKEDNEVDGESSQQEDNSRQGNNEETDKETGVIEEPDAVNDAEEADSDHSSRKLGGTTSDFSASSSVEEVK
Protein: Acylphosphatase (EC 3.6.1.7) (Q57ZA8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Aldehyde dehydrogenase
- Acetyl-coenzyme A synthetase
Sequence:
MPQTVDQVASSAQNNEGMIVRCHVFVRGRVQGVFFRKHTQKAAEEFGVRGWVRNLPDGRVELMAEGPKQQVANLVKWCNEGSPKSRVEGVDSTTEAEGIEYSFDTFEILR
Protein: Leukotriene B4 receptor 1 (LTB4-R 1) (LTB4-R1) (Chemoattractant receptor-like 1) (G-protein coupled receptor 16) (P2Y purinoceptor 7) (P2Y7) (Q15722)
Organism: Homo sapiens (Human)
Function: Receptor for extracellular ATP > UTP and ADP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. May be the cardiac P2Y receptor involved in the regulation of cardiac muscle contraction through modulation of L-type calcium currents. Is a receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Leukotriene B4 receptor 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Leukotriene A-4 hydrolase
- Retinoic acid receptor responder protein 2
- Guanine nucleotide-binding protein G
- Hematopoietic SH2 domain-containing protein
- Polyunsaturated fatty acid 5-lipoxygenase
- Interleukin-8
- G protein-coupled receptor kinase 5
Sequence:
MNTTSSAAPPSLGVEFISLLAIILLSVALAVGLPGNSFVVWSILKRMQKRSVTALMVLNLALADLAVLLTAPFFLHFLAQGTWSFGLAGCRLCHYVCGVSMYASVLLITAMSLDRSLAVARPFVSQKLRTKAMARRVLAGIWVLSFLLATPVLAYRTVVPWKTNMSLCFPRYPSEGHRAFHLIFEAVTGFLLPFLAVVASYSDIGRRLQARRFRRSRRTGRLVVLIILTFAAFWLPYHVVNLAEAGRALAGQAAGLGLVGKRLSLARNVLIALAFLSSSVNPVLYACAGGGLLRSAGVGFVAKLLEGTGSEASSTRRGGSLGQTARSGPAALEPGPSESLTASSPLKLNELN
Protein: Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2) (Q8N3U4)
Organism: Homo sapiens (Human)
Function: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Subcellular location: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Double-strand-break repair protein rad21 homolog
- Sister chromatid cohesion protein PDS5 homolog A
- Structural maintenance of chromosomes protein 1A
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 1B
- Sister chromatid cohesion protein PDS5 homolog B
- Cohesin subunit SA-1
- Meiotic recombination protein REC8 homolog
- Separin
Sequence:
MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKGGNGGGKPPSGPNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGMMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTKITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCTHYVILWQLAKITESSSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDNNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGISSRGSTVRSKKSKPSTGKRKVVEGMQLSLTEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQTEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF
Protein: Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Sporulation-specific protein 9) (O59703)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of ypt7 and rhb1. May be involved in vesicle trafficking and protein sorting. Required for forespore membrane formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Isopentenyl-diphosphate delta-isomerase
- Diphosphomevalonate decarboxylase
- Farnesyl pyrophosphate synthase
- Squalene synthase
- Dehydrodolichyl diphosphate synthase complex subunit SPAC4D7.04c-farnesyl diphosphate specific))
- Decaprenyl-diphosphate synthase subunit 1
- Protein farnesyltransferase subunit beta
- Dehydrodolichyl diphosphate synthase complex subunit nus1
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MVNDFNEKNGIKKRLLDFFPVVLEGIREILESMQYFPEETEKLLYSIKRNTLGGKNNRGLAVLQSLTSLINRELEEAEFRDAALLGWLIEILQGCFLMADDIMDQSIKRRGLDCWYLVVGVRRAINESQLLEACIPLLIRKYFRNMPYYVDLLDTFREVTFLTELGQQEDLLSSRDGEASLRSFDLMKYDFIITYKTSFYSFYLPIKCALLLSRNSNQKAYDTTIKLSKLLGYYFQVQDDYLDCFGDYTVLGKVGMDIQDNKCTWLVCYAEKFASADQLNLLRAHYGKAGSENIAVIKQLYHELQIPELYHKFEDDMVDSISKEIDLIDESTGLKKCIFTKFFQLIYKRSR