wanglab/gogpt-training-data huggingface dataset:
Protein: Cysteine and glycine-rich protein 1 (Cysteine-rich protein 1) (CRP) (CRP1) (P67966)
Organism: Gallus gallus (Chicken)
Function: Heat stable protein, that interacts with zyxin/ZYX. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P21291}. Cytoplasm {ECO:0000269|PubMed:8294495}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8294495}. Note=Associates with the actin cytoskeleton. {ECO:0000269|PubMed:8294495}.
Interaction partners:
- JAC
- Zyxin
Sequence:
MPNWGGGKKCGVCQKAVYFAEEVQCEGSSFHKSCFLCMVCKKNLDSTTVAVHGDEIYCKSCYGKKYGPKGYGYGMGAGTLSTDKGESLGIKYEEGQSHRPTNPNASRMAQKVGGSDGCPRCGQAVYAAEKVIGAGKSWHKSCFRCAKCGKSLESTTLADKDGEIYCKGCYAKNFGPKGFGFGQGAGALIHSQ
Protein: Cyclin-D5-3 (G1/S-specific cyclin-D5-3) (CycD5;3) (Q10QA2)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Retinoblastoma-related protein 2
- Retinoblastoma-related protein 1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase A-1
- Proliferating cell nuclear antigen
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinases regulatory subunit 1
- Os05g0483900 protein
- [RNA-polymerase]-subunit kinase
- Os05g0484000 protein
Sequence:
MGDASASTSAPATPTSTLICREDGNDLFSADPADDDGGGGSGGDWELSIADDDHVLLMDRDDEYLALMLSKERCAGGGGGGERGDEEEEEMVEEWMKNARAWCVGWIVKTNAGFRFSLKTAYVAVTYLDRFLARRCVDRDKEWALQLLSVACLSLAAKVEERRPPRLPEFKLDMYDCASLMRMELLVLTTLKWQMITETPFSYLNCFTAKFRHDERKAIVLRAIECIFASIKVISSVGYQPSTIALAAILIARNKETAPNLDELKSVVGSLWQQLDTGHVYSCYNKMMIQEDRSMQSTTEVASSGVSVAHIGGSEDSAMGGANNATTLEATPDKKRKRLHSPQRQ
Protein: Amidohydrolase-related domain-containing protein (Q8P8H1)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Interaction partners:
- Probable S-methyl-5'-thioinosine phosphorylase
- Polyamine aminopropyltransferase
- Elongation factor P
- Ubiquinone biosynthesis O-methyltransferase
- Secreted protein
Sequence:
MDPLMTNAPPEPCDLLIEAGYVVPIEPHAVVLEDHAVAVSNGVIVAVLPTADARVRFAPARTVSRPDAALMPGLVNAHTHNPMTLLRGVADDLPLMVWLQQHIWPVEAAVIGPEFVADGTTLAIAEMLRGGTTCVNENYFFADVQAAVYKQHGFRALVGAVIIDFPTAWASSDDEYFARAGELHDQWRDDPLISTAFAPHAPYTVNDANFERVRMLADQLDMPVHLHTHETAQEVADSVAQYGQRPLARLDRLGLVNDRLIAVHMTQLTEAEIHLCAERGVSVVHCPESNLKLASGFCPACALQRASVNLAIGTDGCASNNDLDMFSENRTAAILAKAVANDATALDAATTLRAATLGGARALGFGDRIGSIEVGKQADLVCVDLSALETQPLHHVLSQLIYAAGRHQVTDVWIAGKPKLVQRELIDMDTAALVANARQWRDRIRTVRA
Protein: Polypeptide N-acetylgalactosaminyltransferase 12 (EC 2.4.1.41) (Polypeptide GalNAc transferase 12) (GalNAc-T12) (pp-GaNTase 12) (Protein-UDP acetylgalactosaminyltransferase 12) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12) (Q8IXK2)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- C1GALT1-specific chaperone 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Mucin-5AC
- C1GALT1-specific chaperone 1-like protein
- Mucin-1
- DNA polymerase delta catalytic subunit
- Mucin-7
Sequence:
MWGRTARRRCPRELRRGREALLVLLALLALAGLGSVLRAQRGAGAGAAEPGPPRTPRPGRREPVMPRPPVPANALGARGEAVRLQLQGEELRLQEESVRLHQINIYLSDRISLHRRLPERWNPLCKEKKYDYDNLPRTSVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANELSGLPKVRLIRANKREGLVRARLLGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFEYLGNSGEPQIGGFDWRLVFTWHTVPERERIRMQSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVYPELHVPEDRPGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKERML
Protein: Rhamnogalacturonase A (RGase A) (RHG A) (EC 3.2.1.171) (P87160)
Organism: Aspergillus niger
Function: Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MPALPILALALAPLLVNGQLSGSVGPLTSAHSKAATKTCNVLDYGAVADNSTDIGSALSEAWDACSDGGLIYIPPGDYAMDTWVSLSGGKATAIILDGTIYRTGTDGGNMILVENSSDFELYSNSSSGAVQGFGYVYHREGDLDGPRILRLQDVSNFAVHDIILVDAPAFHFVMDDCSDGEVYNMAIRGGNSGGLDGIDVWGSNIWVHDVEVTNKDECVTVKGPANNILVESIYCNWSGGCAMGSLGADTDITDILYRNVYTWSSNQMYMIKSNGGSGTVNNTLLENFIGRGNRYSLDVDSYWSSMTAVDGDGVQLSNITFKNWKGTEADGAERGPIKVVCSDTAPCTDITIEDFAMWTESGDEQTYTCESAYGDGFCLEDSDSTTSYTTTQTVTTAPSGYSATTMAADLTTDFGTTASIPIPTIPTSFYPGLTAISPLASAATTA
Protein: Protein YABBY 1 (OsYABBY1) (OsYAB1) (Protein FILAMENTOUS FLOWER 1) (Q7XIM7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in floral meristem development and maintenance of stamens, rather than in determining polarity in floral organs.
Subcellular location: Nucleus {ECO:0000269|PubMed:15604733}.
Interaction partners:
Sequence:
MSVQFTSEHVCYVNCNYCNTILVVNVPNNCSYNIVTVRCGHCTMVLSMDLAPFHQARTVQDHQVQNRGFQGNNFGSYDIASRNQRTSTAMYPMPTSQQQVSPIRPPEKRQRVPSAYNRFIKEEIQRIKTSNPEISHREAFSAAAKNWAHLPRLHFGLSVADGGGGGGSN
Protein: FNBP1 protein (B7ZL14)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}.
Interaction partners:
Sequence:
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS
Protein: Somatomedin-B and thrombospondin type-1 domain-containing protein (RPE-spondin) (Q8IVN8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20551380}.
Interaction partners:
- Hydroxysteroid dehydrogenase-like protein 2
- Beta-alanine-activating enzyme
Sequence:
MRTLWMALCALSRLWPGAQAGCAEAGRCCPGRDPACFARGWRLDRVYGTCFCDQACRFTGDCCFDYDRACPARPCFVGEWSPWSGCADQCKPTTRVRRRSVQQEPQNGGAPCPPLEERAGCLEYSTPQGQDCGHTYVPAFITTSAFNKERTRQATSPHWSTHTEDAGYCMEFKTESLTPHCALENWPLTRWMQYLREGYTVCVDCQPPAMNSVSLRCSGDGLDSDGNQTLHWQAIGNPRCQGTWKKVRRVDQCSCPAVHSFIFI
Protein: Mitochondrial ribonuclease P catalytic subunit (EC 3.1.26.5) (Mitochondrial ribonuclease P protein 3) (Mitochondrial RNase P protein 3) (Protein mulder) (Protein only RNase P catalytic subunit) (Q9W413)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:27131785}.
Interaction partners:
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Mitochondrial ribonuclease P protein 1 homolog
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P/MRP subunit p21, isoform A
- FI18256p1
- NADH dehydrogenase complex I, assembly factor 6 homolog
- LD06392p
- Endoribonuclease Dcr-2
- Ribonuclease 3
- Transcription initiation factor TFIID subunit 11
Sequence:
MYNLRLLRNLLPIAGHAHPRWLASQHKRRPQPGSLPADRLDQLRSDLFERRHELSGAEWTEVRRSLVDGYKHINGHNVDAVILGVCSAPNQLSLAKSYVEFLRSRGSKPNAATLGRLLRVYNAAYHERPLSEAEQSEILQICRSLQAEHETLDASSCENVIHGLVATSGDDWQRGLPLLEMMKVTSTPSVAAYSALAEKAFSVATPEQELAWRLLEEMATARKPPKCEVYLALLNRLANETAQLPAQLSLLLQFLERHEILVSQRVAIRLQELSSQVPQLLHTRTTHLGGLGKCQSCQQHLQPVAISDEEFRQLSECFLERVLIRRDVFQRSTPEEVARFKKFVEKTAPYDCVIDGLNVAYSTGTKKTPQQLAKLVATVVRHFREQDKRVLVLGREHMRNWSKQAMHYVHCNASLFLTSNLSHDDPFLLYATLRSGQETDFFSRDLMRSHAFHLGTELKPIFRRWQQEHQFSLVTQTQTGQIIVKEPVRHRLCAHQVADTWHVPYCAQYTPHPTDSFEVPANWLCIQMKEQTIPATKTKTKTTR
Protein: Uncharacterized serine-rich protein C2F12.03c (O14338)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- ATP-dependent helicase upf1
- Nonsense-mediated mRNA decay protein 3
- Nonsense-mediated mRNA decay protein 2
- Eukaryotic translation initiation factor 4 gamma
- CENP-A recruiting complex protein mis19
- Telomerase reverse transcriptase
- CENP-A recruiting complex protein mis20
- SWI/SNF chromatin-remodeling complex subunit sol1
Sequence:
MSAIDSCEHTVSWKLCEQKYNEATTLLSKLKKLLGNFKENCTSVVVDGHKKPRSESRKKYDAKKQHQSSHFATPVKGVESSEPTEKKKRNKEALWLRARQKKWKEIFELCQKITSLLGGTILIDVSFSMEKDVLTYLWMRVHYQVISFFKHRIYEASTQHDPELLSSLVTMHIQYLNSTIQFYTTLIAIIGELYHLQCLSPLTSFFTSCVTPKTILESPLRKQGSHNWKTSTNSQSRLAALFSSIFEDSCLEVDSVKRLLSGSPSSSSSPLKKDSSSNSLTYEPALTDHKPQYLVLCVYRSLIYIGDVHRYLAEVRSPNVPDYQVSRRYYVMAANVAPDYGVHFHQLGLIEVADARSSSRKSSSGQSSSLKGNVNVEDKRLIQALPAISFFFLSSISPNNVAASSAKTSLFIALKRCFGKTNDGSNPCLYHKESSAISLFLRLYAIAFSNTDADYIQDSGPLFKRVRFLLSESLKSGLFSESSLLQMTYCALAARVLAPFIGFSDSGEHGESYPNLKLATQTTTMFFEVLSDSVNSQLPLQALTSGVSSKKDGNFDDLVERRQYGSLSSNAVLMPMLLPLCVLTSSCLQNGDVWLTKDIRTGLSQIFNRLSFFLENTNQTAPDDSVLVRCSSKSIGLLFFFPLVKVCGVPRDTLQWLYFSNHYPFNEEGKGPQVDDSDALITIALDSLYVLLNMRAKSTPNSTSFSSPPTPHRSPFSGQAFTGMGLSNYSLMSSSSFPSAQSSPTSPFLSGTPSIANQSSSIASLQFGRMVDSLVGPVQPIPAQTTGCSVHSLQQRTFSNESPRAVDSGFSRTSTPFSESTSSYPLVSGNLSSCETHLNGSPQNGHLQGERVLFRPLRSPALNTFSTPATEPPEHLVLSELLKKMVNISNN
Protein: Sterol 14-alpha demethylase (EC 1.14.14.154) (Cytochrome P450 monooxygenase 51A) (Ergosterol biosynthesis protein cyp51A) (B8N2C8)
Organism: Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Function: Cytochrome P450 monooxygenase involved in the biosynthesis of ergosterol (By similarity). The existence of several duplicated sterol 14-alpha demethylase genes could be a good strategy to modulate the composition and fluidity of the cell membrane (By similarity). Catalyzes C14-demethylation of erburicol to produce 4,4,24-trimethyl cholesta-8,24(28)-dien-3-beta-ol (By similarity). Shows a slight substrate preference toward eburicol over obtusifoliol (By similarity). As a target of azole drugs, plays a crucial role in azole susceptibility.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Delta
- Delta
- Sterol 14-alpha demethylase
- Sterol 14-alpha demethylase
- Farnesyl-diphosphate farnesyltransferase, putative.
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
Sequence:
MIFSRSMASFTLVSAYAAAGLLAIIVLNLLRQLLFRNKTDPPLVFHWIPFLGSTVTYGMDPYAFFFSCRQKYGDIFTFILLGRKITVYLGIQGNEFILNGKLKDVNAEEIYSPLTTPVFGSDIVYDCPNSKLMEQKKFIKFGLTQAALESHVPLIEKEVLDYLKTSPNFKGTSGRVEITDAMAEITIFTAGRALQGEEVRKKLTAEFADLYHDLDRGFTPINFMLPWAPLPRNRKRDAAHARMREIYMDIINERRKNPDRETSDMIWNLMHCTYKNGQPLPDKEIAHMMITLLMAGQHSSSSISSWIMLRLASEPAVMEELYQEQITKLSPDGRTLPPLQYRDLDLLPLHQNLIKETLRLHLSIHSLMRKVKNPMPVPGTPYVVPADHVLLASPGVTALSDEYFPNASRWDPHRWENRVEKEDEEDIVDYGYGTVSKGTSSPYLPFGAGRHRCIGEKFAYVNLGVIVATMARHMKLFNVDGKKGVPATDYSSMFSGPSKPAIIGWERRFPEKS
Protein: Caprin-2 (RNA granule protein 140) (Q5RJ80)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Promotes phosphorylation of the Wnt coreceptor LRP6, leading to increased activity of the canonical Wnt signaling pathway. Facilitates constitutive LRP6 phosphorylation by CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate cells for Wnt signaling. May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons. Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation. May be involved in apoptosis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6IMN6}. Cell membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IMN6}.
Interaction partners:
- Adipolin
- Claudin
Sequence:
MRKTETMVQLSPSRTLETLTPSELTVEKDDGQGSPKPESPRMLSALQLALSSTTVYCGYEKYIEDGLICLKHKIRNIEKKKLKLERYSDKLKKGEKLNEDQLEAVGKYDEVVHNLKFAKELQKTIGSLTQDLLKAQRKAVRQEKQMKTDEEKSRLSLMLQVQYVLHSLQREDVRKNFCNTRQYSCYMSTQDMEGLMDLASLVGCKRDYSISLEDQMRRAAIVYWELLEGNEKPVAGSTYKHMKEKLLRLVDSGFFDNIPLPKSDSQEKTETIKPDSQSRPSGLTTLVKLSSNEVPSKEFLNRRYMPETDERRRGETASPRNWKEDFLAMKEREPPDSWEMEELADPPASSQSPIQKPWKGAAGLIPKTVDIVKRSTTDPKEKRQRKKAEQDSKSMPVAVEVFSSPSPLPKDPVQRRQQLETLMDQISGSFSFMQESLLDGESSPVNTQTKRCRPSPGSSTPIVQRELTKSPSDILPSSQRSTPLRILLSGEGKGCLSNGDRSINGSDLELHSEDKPRKQAEGFNSPPLYRRGSSISVSLENQSTVQAGRQMLCNGVSSSGSAQTFSTPPSRRSISAENPFHNIHSVFNVIGESSGMKADESGFSESIHRSFTSAKTSSVTTASTQTPPELNPPEEDLQIEGQYPLECAVSAGGPVFSSSHSRVGQSCYSRGAVRGGYDAYRVNVRSPGGSFMSQTHREPASALYMARENGYQQNFKRGAGTATQRSSAGWSDSSQVSSPDRDGAYPLDSGLSDTLSIPAMEVPMNPQGPHTLMPVHVYPLTQLRVAFSAARTANFAPGTLDQPIAFDLLHTNLGDMFDTGSGRFTCPATGAYVFIFHILKLAISVPLYINLMRNEEVMVSAYANDGAPDHETASNHAVLQLFQGDQVWLRLHRGAIYGSSWKYSTFSGFLLYQD
Protein: YlmG homolog protein 1-2, chloroplastic (AtYLMG1-2) (YGGT family protein YLMG1-2) (Q9SUE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Not required for the biogenesis and accumulation of native cytochrome b6 in the thylakoid membrane. Not functionally involved in the pathway for covalent binding of the c-type heme to cytochrome b6.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:Q9SRS3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB3, chloroplastic
- Protein TIC 20-I, chloroplastic
- Tetratricopeptide repeat
- AT3g52230/F4F15_340
- Sequence-specific DNA binding transcription factor
- Protein KINASE OF THE OUTER CHLOROPLAST MEMBRANE 1
- Fatty-acid-binding protein 1
- MAR-binding filament-like protein 1
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 16, chloroplastic
Sequence:
MASFTTNSLALRASILANPRLPPPIIRPRLSLPRKLSFNLSLHNARTIVSSAVTSSSPVLSSKPPSQFPFSDSTRSITTLVLLAGVVIKSLIQKLSVAIVNLSPQIQASFRTASPLFFASLRDRPAGYLNTPLTVVAAGLSKWLDIYSGVLMVRVLLSWFPNIPWDRQPLSAIRDLCDPYLNLFRNIIPPVFDTLDVSPLLAFAVLGTLGSILNNSRG
Protein: Threonine--tRNA ligase 2, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase protein 3) (A2RTX5)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BLY2}. Nucleus {ECO:0000250|UniProtKB:Q8BLY2}. Note=Primarily cytoplasmic. Also detected at lower levels in the nucleus. {ECO:0000250|UniProtKB:Q8BLY2}.
Interaction partners:
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- Threonine--tRNA ligase 1, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Threonine--tRNA ligase, mitochondrial
- Glutamine--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MAAEALAAEAVASRLERQEEDIRWLWSEVERLRDEQLNAPYSCQAEGPCLTREVAQLRAENCDLRHRLCSLRLCLAEERSRQATLESAELEAAQEAGAQPPPSQSQDKDMKKKKMKESEADSEVKHQPIFIKERLKLFEILKKDHQLLLAIYGKKGDTSNIITVRVADGQTVQGEVWKTTPYQVAAEISQELAESTVIAKVNGELWDLDRPLEGDSSLELLTFDNEEAQAVYWHSSAHILGEAMELYYGGHLCYGPPIENGFYYDMFIEDRAVSSTELSALENICKAIIKEKQPFERLEVSKEILLEMFKYNKFKCRILNEKVNTATTTVYRCGPLIDLCKGPHVRHTGKIKTIKIFKNSSTYWEGNPEMETLQRIYGISFPDNKMMRDWEKFQEEAKNRDHRKIGKEQELFFFHDLSPGSCFFLPRGAFIYNTLTDFIREEYHKRDFTEVLSPNMYNSKLWEASGHWQHYSENMFTFEIEKDTFALKPMNCPGHCLMFAHRPRSWREMPIRFADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTVEQIEEEIKGCLQFLQSVYSTFGFSFQLNLSTRPENFLGEIEMWNEAEKQLQNSLMDFGEPWKMNPGDGAFYGPKIDIKIKDAIGRYHQCATIQLDFQLPIRFNLTYVSKDGDDKKRPVIIHRAILGSVERMIAILSENYGGKWPFWLSPRQVMVIPVGPTCEKYALQVSSEFFEEGFMADVDLDHSCTLNKKIRNAQLAQYNFILVVGEKEKIDNAVNVRTRDNKIHGEILVTSAIDKLKNLRKTRTLNAEEAF
Protein: Alpha-1-acid glycoprotein (Orosomucoid) (OMD) (P02764)
Organism: Rattus norvegicus (Rat)
Function: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Albumin
- Haptoglobin
- Alpha-1-antiproteinase
- Alpha-2-macroglobulin
- Transthyretin
- Ceruloplasmin
- Alpha-2-HS-glycoprotein
- Hemopexin
- Vitamin D-binding protein
- Protein AMBP
Sequence:
MALHMVLVVLSLLPLLEAQNPEPANITLGIPITNETLKWLSDKWFYMGAAFRDPVFKQAVQTIQTEYFYLTPNLINDTIELREFQTTDDQCVYNFTHLGVQRENGTLSKCAGAVKIFAHLIVLKKHGTFMLAFNLTDENRGLSFYAKKPDLSPELRKIFQQAVKDVGMDESEIVFVDWTKDKCSEQQKQQLELEKETKKETKKDP
Protein: (thale cress) hypothetical protein (A0A178VTR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEMDSTTTIKPETLSTVSSSPPEKIHLRPMTLSDVDDFMVWATDSNVTRFCTWEPYTSREAAIAYLNDALLPHPWLRAICLDNDRPIGSISVTPVDEIRGEIGYVLGSKYWGKGIATEAVRLVAGEIFKEKPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRDMVMFSFLPSDSLH
Protein: Oviduct-specific glycoprotein (Estrogen-dependent oviduct protein) (Oviductal glycoprotein) (Oviductin) (Q62010)
Organism: Mus musculus (Mouse)
Function: Binds to oocyte zona pellucida in vivo. May play a role in the fertilization process and/or early embryonic development.
Subcellular location: Cytoplasmic vesicle, secretory vesicle. Note=Secretory granules.
Interaction partners:
- Zona pellucida sperm-binding protein 3
- Zona pellucida sperm-binding protein 1
- Zona pellucida sperm-binding protein 2
Sequence:
MGRLLLLAGLVLLMKHSDGTAYKLVCYFTNWAHSRPGPASIMPHDLDPFLCTHLIFAFASMSNNQIVAKNLQDENVLYPEFNKLKERNRELKTLLSIGGWNFGTSRFTAMLSTLANREKFIDSVISFLRIHGFDGLDLFFLYPGLRGSPPHDRWNFLFLIEELQFAFEREALLTQHPRLLLSAAVSGIPSIIHTSYDALLLGRRLDFINVLSYDLHGSWEKFTGHNSPLFSLPEDSKSSAYAMNYWRKLGTPADKLIMGFPTYGRNFYLLKESKNGLQTASMGPASPGKYTKQAGFLAYYEVCSFVQRAKKHWIDYQYVPYAFKGKEWLGYDDTISFSYKAMYVKREHFGGAMVWTLDMDDVRGTFCGNGPFPLVHILNELLVQTESNSTPLPQFWFTSSVNASGPGSENTALTEVLTTDTIKILPPGGEAMTTEVHRRYENMTTVPSDGSVTPGGTASPRKHAVTPENNTMAAEAKTMSTLDFFSKTTTGVSKTTTGISKTTTGVSKTTTGVSKATAGISKTIPEISKATAGVSKTTTGVSKTTTGISKTITGVSKTTTGISKTTTGISKTTTGVSKITTGVSKTTTGISKTTTGISQTTTGISKTTTDISKTTTGISKTTPGISKTTPGMTVIVQTQANEAETTATMDHQSVTPTEMDTTLFYLKTMTPSEKETSRKKTMVLEKATVSPREMSATPNGQSKTLKWASLITEVETYSQDG
Protein: N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (DDAH-1) (Dimethylarginine dimethylaminohydrolase 1) (EC 3.5.3.18) (DDAHI) (Dimethylargininase-1) (O08557)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Interaction partners:
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Protein arginine N-methyltransferase 1
- Nitric oxide synthase 3
Sequence:
MAGLSHPSVFGRATHAVVRAPPESLCRHALRRSQGEEVDFARAERQHQLYVGVLGSKLGLQVVQLPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADSLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDMAANCIYLNIPSKGHVLLHRTPEEYPESAKVYEKLKDHLLIPVSNSEMEKVDGLLTCCSVFINKKTDS
Protein: Peptide leucine arginine (pLR) (Q90WP7)
Organism: Lithobates pipiens (Northern leopard frog) (Rana pipiens)
Function: Mast cell degranulating peptide. Antiproliferative activity against human breast and ovarian tumor cell lines in vitro. Inhibits granulopoiesis in rat in vitro. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity against Gram-positive bacteria B.megaterium Bm11, S.lentus and M.luteus, and antifungal activity against C.tropicalis, C.guiller-mondii and P.nicotianae spores. Has hemolytic activity. The mature peptide inserts into the hydrophobic core of the bacterial cell membrane and increases permeability without disrupting membrane integrity. Probably binds to the outer membrane surface before aggregating to form transmembrane pores.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MFTLKKSLLLLFFLGTISSSLCEQERDSDDEDQGEVTEQVVKRLVRGCWTKSYPPKPCFVRG
Protein: Preprofallaxidin-1 [Cleaved into: Fallaxidin-4.1] (B5LUQ4)
Organism: Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax)
Function: Fallaxidin-4.1 shows antibacterial activity against the Gram-positive bacteria L.lactis (MIC=12 uM), M.luteus (MIC=100 uM), S.epidermidis (MIC=100 uM) and S.uberis (MIC=50 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, E.faecalis, L.innocua, S.aureus, or the Gram-negative bacteria E.cloacae and E.coli. Inhibits the formation of NO by neuronal nitric oxide synthase with an IC(50) of 13.3 uM.
Subcellular location: Secreted {ECO:0000269|PubMed:18803332}.
Interaction partners:
Sequence:
MASLKKSLFLVLFLGMVSLSICDKEKREGENEEEEEEHEEESEEKRGLLSFLPKVIGVIGHLIHPPS
Protein: A-kinase-interacting protein 1 (Breast cancer-associated gene 3 protein) (PKA-interacting protein) (Proline-rich protein BCA3) (Q9NQ31)
Organism: Homo sapiens (Human)
Function: Enhances NF-kappa-B transcriptional activity by regulating the nuclear localization of the NF-kappa-B subunit RELA and promoting the phosphorylation of RELA by PRKACA. Regulates the effect of the cAMP-dependent protein kinase signaling pathway on the NF-kappa-B activation cascade.
Subcellular location: Nucleus {ECO:0000269|PubMed:15630084, ECO:0000269|PubMed:18178962}. Note=Locates to punctate spots.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- Transcription factor p65
Sequence:
MDNCLAAAALNGVDRRSLQRSARLALEVLERAKRRAVDWHALERPKGCMGVLAREAPHLEKQPAAGPQRVLPGEREERPPTLSASFRTMAEFMDYTSSQCGKYYSSVPEEGGATHVYRYHRGESKLHMCLDIGNGQRKDRKKTSLGPGGSYQISEHAPEASQPAENISKDLYIEVYPGTYSVTVGSNDLTKKTHVVAVDSGQSVDLVFPV
Protein: Dimethylsulfoniopropionate lyase DddW (DMSP lyase) (EC 4.4.1.3) (Q5LW89)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Function: Able to cleave dimethylsulfonioproprionate (DMSP), releasing dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere.
Interaction partners:
Sequence:
MTAMLDSFATDLTAATSLHQPGNLPHPPHAIDAENVPLSGGTDPTYGEVRWRTLINGTEAAPRDMVLGIAEFGPGHQLRPHRHTPPEFYLGLEGSGIVTIDGVPHEIRAGVALYIPGDAEHGTVAGPEGLRFAYGFASASFEAIEYRFTASA