wanglab/gogpt-training-data huggingface dataset:
Protein: 25S rRNA (uridine(2634)-N(3))-methyltransferase (EC 2.1.1.313) (Base methyltransferase of 25S RNA 5) (P40493)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2634 (m3U2634) in 25S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:24335083}.
Interaction partners:
- 25S rRNA
- Uncharacterized protein YCR016W
- 25S rRNA
- Protein-lysine N-methyltransferase EFM2
- Putative methyltransferase YGR283C
- Protein arginine N-methyltransferase SFM1
- Regulator of rDNA transcription protein 14
- Putative RNA-binding protein involved in heterochromatin assembly
- 25S rRNA
- Putative methyltransferase YMR310C
Sequence:
MARKLKGKIGSKGLKGALLRHKAKVKLVRNIESKQKHELRKKNSSANNKTVKRNQEFQKLNQGKVMPFEKDETLMLCGEGDFSFARSIVEQNYIESDNLIITSYDNSVNELKLKYPHTFEENYQYLKDLNIPIFFQIDVTKLVKSFKISKNNTWFKIINRLSDHRWGNKPLQNIVFNFPHNGKGIKDQERNIREHQDLIFNFFQNSLQLFNLINTKIQNDTLRYTQGYDLNEDTPQAKKLTAEGYGNIILSLFDGEPYDSWQIKLLAKKNGLTLSRSSKFQWENFPGYHHRRTNSEQDTTKPAKERDARFYIFSKYVSNSSKHNRKSKKDTDSDSD
Protein: P2X purinoceptor 4 (P2X4) (ATP receptor) (Purinergic receptor) (Q99571)
Organism: Homo sapiens (Human)
Function: Receptor for extracellularly released ATP acting as a ligand-gated ion channel that plays multiple role in immunity and central nervous system physiology. Plays a key role in initial steps of T-cell activation and Ca(2+) microdomain formation (By similarity). Participates also in basal T-cell activity without TCR/CD3 stimulation (By similarity). Promotes the differentiation and activation of Th17 cells via expression of retinoic acid-related orphan receptor C/RORC. Upon activation, drives microglia motility via the PI3K/Akt pathway (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10515189, ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F8W463}. Lysosome membrane {ECO:0000269|PubMed:24817123}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- P2X purinoceptor 7
- P2X purinoceptor 6
- P2X purinoceptor 3
- P2X purinoceptor 5
- P2X purinoceptor 1
- P2X purinoceptor 2
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 2D
Sequence:
MAGCCAALAAFLFEYDTPRIVLIRSRKVGLMNRAVQLLILAYVIGWVFVWEKGYQETDSVVSSVTTKVKGVAVTNTSKLGFRIWDVADYVIPAQEENSLFVMTNVILTMNQTQGLCPEIPDATTVCKSDASCTAGSAGTHSNGVSTGRCVAFNGSVKTCEVAAWCPVEDDTHVPQPAFLKAAENFTLLVKNNIWYPKFNFSKRNILPNITTTYLKSCIYDAKTDPFCPIFRLGKIVENAGHSFQDMAVEGGIMGIQVNWDCNLDRAASLCLPRYSFRRLDTRDVEHNVSPGYNFRFAKYYRDLAGNEQRTLIKAYGIRFDIIVFGKAGKFDIIPTMINIGSGLALLGMATVLCDIIVLYCMKKRLYYREKKYKYVEDYEQGLASELDQ
Protein: Putative chloroplast RNA binding protein (RNA-binding (RRM/RBD/RNP motifs) family protein) (O82299)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic
- Pentatricopeptide repeat-containing protein At1g01970
- Chloroplast stem-loop binding protein of 41 kDa b, chloroplastic
- Probable membrane metalloprotease ARASP2, chloroplastic
- Mitochondrial transcription termination factor family protein
- Peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic
- At2g27680/F15K20.22
- Pentatricopeptide repeat-containing protein At2g17033
- Peptidyl-prolyl cis-trans isomerase FKBP17-2, chloroplastic
- Protein CURVATURE THYLAKOID 1C
Sequence:
MAVLEASLSIFSFSSSSSSSKPYLFSKRSSSLKLTALSLRIPSNLSPVFSLRSGSDNSRRLVSVLCSVAEKETSADEETSQEEKTEETQNSNLKRKLFVFNLPWSMSVNDISELFGQCGTVNNVEIIRQKDGKNRGFAFVTMASGEEAQAAIDKFDTFQVSGRIISVSFARRFKKPTPKSPNDLPSPAPGDTRHKLYVSNLAWKARSTHLRELFTAADFNPVSARVVFADPEGRSSGYGFVSFATREEAENAITKLNGKEIMGRPITLKFSLRSASESEDGDSVEANNASEDGDTVEDKNTSEENIVE
Protein: UBX domain-containing protein 1 (Suppressor of high-copy PP1 protein) (P34223)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. Direct or indirect positive regulator of GLC7 activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell division control protein 48
- Protein DOA1
- Ubiquitin thioesterase OTU1
- DER1-like family member protein 1
- E4 ubiquitin-protein ligase UFD2
- Ubiquitin fusion degradation protein 1
- UBX domain-containing protein 7
- UBX domain-containing protein 2
- UBX domain-containing protein 4
- UBX domain-containing protein 5
Sequence:
MAEIPDETIQQFMALTNVSHNIAVQYLSEFGDLNEALNSYYASQTDDQKDRREEAHWNRQQEKALKQEAFSTNSSNKAINTEHVGGLCPKPGSSQGSNEYLKRKGSTSPEPTKGSSRSGSGNNSRFMSFSDMVRGQADDDDEDQPRNTFAGGETSGLEVTDPSDPNSLLKDLLEKARRGGQMGAENGFRDDEDHEMGANRFTGRGFRLGSTIDAADEVVEDNTSQSQRRPEKVTREITFWKEGFQVADGPLYRYDDPANSFYLSELNQGRAPLKLLDVQFGQEVEVNVYKKLDESYKAPTRKLGGFSGQGQRLGSPIPGESSPAEVPKNETPAAQEQPMPDNEPKQGDTSIQIRYANGKREVLHCNSTDTVKFLYEHVTSNANTDPSRNFTLNYAFPIKPISNDETTLKDADLLNSVVVQRWA
Protein: Siroheme decarboxylase NirG subunit (EC 4.1.1.111) (P95414)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in heme d1 biosynthesis. Catalyzes the decarboxylation of siroheme into didecarboxysiroheme (By similarity).
Interaction partners:
- Pre-heme d1 synthase
- Siroheme decarboxylase NirL subunit
- Siroheme decarboxylase NirH subunit
- Protein NirF
- Dihydro-heme d1 dehydrogenase
- Cytochrome c55X
- Nitrite reductase
- Siroheme decarboxylase NirD subunit
- Cytochrome c-551
- uroporphyrinogen-III C-methyltransferase
Sequence:
MDEFDRRLLNRLQHGLPLEPHPYALLAAELDCREEDILRRLDDLLDDGTLTRFGPLFDIEPLGGAFTLAAMSVPEARFEEIAALLAGWPQVAHNYRREHALNMWLVVACDSPAEVAETLARLERESGLAVLDLPKEATYHVGLHFPL
Protein: 3',5'-cyclic-nucleotide phosphodiesterase 1 (PDEase 1) (EC 3.1.4.17) (3':5'-CNP) (Low-affinity cAMP phosphodiesterase) (P22434)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Controls the level of cAMP in yeast cells, together with the high-affinity cAMP phosphodiesterase (PDE2).
Interaction partners:
- 3',5'-cyclic-nucleotide phosphodiesterase 2
- Adenylate cyclase
- cAMP-dependent protein kinase regulatory subunit
- Adenosine kinase
- GMP synthase
- Guanylate kinase
- Golgi apyrase
- AMP deaminase
- Adenine phosphoribosyltransferase 1
- Adenine phosphoribosyltransferase 2
Sequence:
MVVFEITILGANGGPTEYGTQCFILKPARTEDPELIAVDGGAGMYQLREMLVQGRNENEGDDELVPSFYEHDREPIEFFIDSKLNIQKGLSKSLLQSLKRQGEHFESANTMKKTYEVFQGITDYYITHPHLDHISGLVVNSPSIYEQENSKKKTIWGLPHTIDVLQKHVFNDLIWPDLTAERSRKLKLKCLNPKEVQKCTIFPWDVIPFKVHHGIGVKTGAPVYSTFYIFRDRKSKDCIIVCGDVEQDRRESEESLLEEFWSYVAENIPLVHLKGILVECSCPLSSKPEQLYGHLSPIYLINELSNLNTLYNSSKGLSGLNVIVTHVKSTPAKRDPRLTILEELRFLAEERNLGDLRISIALEGHTLFL
Protein: Zinc finger matrin-type protein 3 (Zinc finger protein WIG-1) (p53-activated gene 608 protein) (O08781)
Organism: Rattus norvegicus (Rat)
Function: Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus.
Subcellular location: Nucleus {ECO:0000269|PubMed:12196512, ECO:0000269|PubMed:9250682}. Nucleus, nucleolus {ECO:0000269|PubMed:12196512, ECO:0000269|PubMed:9250682}.
Interaction partners:
Sequence:
MILLQQVWLPLPNRPSTSPPMSVAARSTGTLQLPPQKAFGQEASLPLAGEEDLAKRGEPDSALEELCKPLFCKLCNVTLNSAQQAQAHYQGKNHGKKLRNYYAANSCPPPARMSSVAEPVATPLVPVPPQVGSCKPGGRVILATENDYCKLCDASFSSPAVAQAHYQGKNHAKRLRLAEAQSHSFSDSAEAGQRRTRKEGSEFKMVTTRRNMYTVQSNSGPYFNARSRQRIPRDLAMCVTPSGQFYCSMCNVGAGEEVEFRQHLESKQHKSKVSEQRYRSEMENLGYVQ
Protein: Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) (K(+) channel subunit beta-2) (Kv-beta-2) (P62483)
Organism: Rattus norvegicus (Rat)
Function: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity. Promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore. Modulates the functional properties of KCNA4. Modulates the functional properties of KCNA5 (By similarity). Enhances KCNB2 channel activity (By similarity). Binds NADPH and has NADPH-dependent aldoketoreductase activity. Has broad substrate specificity and can catalyze the reduction of methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21357749}. Membrane {ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:9334400}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:23318870}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:9334400}. Synapse, synaptosome {ECO:0000269|PubMed:21357749}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21357749}. Note=Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits. Associates with microtubules when unphosphorylated (PubMed:21357749). {ECO:0000269|PubMed:21357749, ECO:0000305}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 2
- Potassium voltage-gated channel subfamily A member 1
- Potassium voltage-gated channel subfamily A member 5
- Potassium voltage-gated channel subfamily A member 6
- Potassium voltage-gated channel subfamily A member 4
- Potassium voltage-gated channel subfamily A member 3
- Potassium voltage-gated channel subfamily B member 1
- Voltage-gated potassium channel KCNC1
- Voltage-gated potassium channel KCNC3
- Potassium voltage-gated channel subfamily A member 10
Sequence:
MYPESTTGSPARLSLRQTGSPGMIYSTRYGSPKRQLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPYSKKDYRS
Protein: AcrIIA5 (A0A220GHA5)
Organism: Streptococcus phage D4276
Interaction partners:
Sequence:
MAYGKSRYNSYRKRSFNRSNKQRREYAQEMDRLEKAFENLDGWYLSSMKDSAYKDFGKYEIRLSNHSADNKYHDLENGRLIVNIKASKLNFVDIIENKLDKIIEKIDKLDLDKYRFINATNLEHDIKCYYKGFKTKKEVI
Protein: Transcription elongation factor, mitochondrial (J3KTG7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGSVLFTAGERWRCFLTPSRSSLYWALHNFCCRKKSTTPKKITPNVTFCDENAKEPENALDKLFSSEQQASILHVLNTASTKELEAFRLLRGRRSINIVEHRENFGPFQNLESLMNVPLFKYKSTVQVCNSILCPKTGREKRKSPENRFLRKLLKPDIERERLKAVNSIISIVFGTRRIAWAHLDRKLTVLDWQQSDRWSLMRGIYSSSVYLEEVRQLHLQIPTC
Protein: Early phosphoprotein p84 [Cleaved into: p20; p26; p28] (P17151)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Promotes efficient viral DNA replication. Recruits the DNA polymerase processivity factor to pre-replication foci.
Subcellular location: Host nucleus {ECO:0000269|PubMed:16501081, ECO:0000269|PubMed:2824853}. Virion {ECO:0000269|PubMed:2824853}. Note=Found in subnuclear structures known as promyelocytic leukemia oncogenic domains (PODs) or nuclear domain 10 (ND10) during the early stages of viral infection (PubMed:16501081).; SUBCELLULAR LOCATION: [p20]: Virion {ECO:0000269|PubMed:19656965}.; SUBCELLULAR LOCATION: [p26]: Virion {ECO:0000269|PubMed:19656965}.; SUBCELLULAR LOCATION: [p28]: Virion {ECO:0000269|PubMed:19656965}.
Interaction partners:
Sequence:
MDLPTTVVRKYWTFANPNRILHQSVNQTFDVRQFVFDTARLVNCVDGDGKVLHLNKGWLCATIMQHGEASAGAKTQQGFMSIDITGDGELQEHLFVRGGIVFNKSVSSVVGSSGPNESALLTMISENGNLQVTYVRHYLKNHGESSSGGGGCGAASTASAVCVSSLGGSGGTRDGPSAEEQQRRRQEQRHEERRKKSSSSAGGGGGGGAGGGGGGGGSGGQHSSDSANGLLRDPRLMNRQKERRPPPSSENDGSPPLREAKRQKTTAQHEGHGGGGKNETEQQSGGAGGGGGGGSGRMSLPLDTSEAVAFLNYSSSSSAVSSSSNNHHHHHHHHNAVTDVAAGTDGALLLPIERGAVVSSPSSTSPSSLLSLPRPSSAHSAGETVQESEAAATAAAAGLMMMRRMRRAPAEAAEAPPQSEEENDSTTPVSNCRVPPNSQESAAPQPPRSPRFDDIIQSLTKMLNDCKEKRLCDLPLVSSRLLPETSGGTVVVNHSSVARTAAAVSAAGVGPPAAACPPLVTTGVVPSGSVAGVAPVAAAIETPAAPPRPVCEIKPYVVNPVVATAAAASNSSSSSSAPLPPPPPPSGGRRGRARNNTRGGGGGGGGRNSRRQAASSSSSSSRRSRRRNNRHEDEEDNDPLLRLSQVAGNGRRRGPSFLEDGLEIIDPSEEAAIAAASIAAFFDD
Protein: Isochorismate pyruvate lyase (IPL) (EC 4.2.99.21) (Chorismate mutase) (CM) (EC 5.4.99.5) (Salicylate biosynthesis protein) (Q51507)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the incorporation of salicylate into the siderophore pyochelin. Catalyzes the elimination of the enolpyruvyl side chain from isochorismate to yield salicylate and pyruvate via a rare pericyclic hydrogen transfer mechanism from C2 to C5. PchB also catalyzes the nonphysiological Claisen rearrangement of chorismate to prephenate in which the pyruvylenol tail is transferred from a C3 ether linkage to a C1-C9 linkage.
Interaction partners:
- Pyochelin synthase PchD
- Pyochelin biosynthetic protein PchC
- Salicylate biosynthesis isochorismate synthase
- Pyochelin synthetase PchE
- Pyochelin biosynthetic protein PchG
- Pyochelin synthetase PchF
- Fe
- Probable ATP-binding component of ABC transporter
- Probable ATP-binding component of ABC transporter
- Uncharacterized protein PA4219
Sequence:
MKTPEDCTGLADIREAIDRIDLDIVQALGRRMDYVKAASRFKASEAAIPAPERVAAMLPERARWAEENGLDAPFVEGLFAQIIHWYIAEQIKYWRQTRGAA
Protein: UMP-CMP kinase (EC 2.7.4.14) (Deoxycytidylate kinase) (CK) (dCMP kinase) (Nucleoside-diphosphate kinase) (EC 2.7.4.6) (Uridine monophosphate/cytidine monophosphate kinase) (UMP/CMP kinase) (UMP/CMPK) (P30085)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:10462544, ECO:0000269|PubMed:11912132}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:10462544, ECO:0000269|PubMed:11912132}. Note=Predominantly cytoplasmic, less than 15% nuclear. {ECO:0000269|PubMed:11912132}.
Interaction partners:
- Thymidylate kinase
- UMP-CMP kinase 2, mitochondrial
- Nucleoside diphosphate phosphatase ENTPD5
- Uridine-cytidine kinase 2
- Nucleoside diphosphate kinase, mitochondrial
- 5'
- Uridine 5'-monophosphate synthase
- Alpha-enolase
- Deoxyguanosine kinase, mitochondrial
- Deoxycytidine kinase
Sequence:
MKPLVVFVLGGPGAGKGTQCARIVEKYGYTHLSAGELLRDERKNPDSQYGELIEKYIKEGKIVPVEITISLLKREMDQTMAANAQKNKFLIDGFPRNQDNLQGWNKTMDGKADVSFVLFFDCNNEICIERCLERGKSSGRSDDNRESLEKRIQTYLQSTKPIIDLYEEMGKVKKIDASKSVDEVFDEVVQIFDKEG
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase 5 (Protein mannosyltransferase 5) (EC 2.4.1.109) (Q5ACU3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Protein mannosyltransferase (PMT) involved in hyphal morphogenesis and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Required for biofilm formation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase 6
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
Sequence:
MTKELPSGYFQGPFRPYKTFQPSLTERPLSKFEQFAVFSILLISLIRLYKLYIPDRVVFDEIHLIKYIKNYYDGSIFVDIHPPLGKLIYFYITKLFSFDKDFQIDIIGDLYPEDFPYLWLRLFSGICGIGHVLLTFFTLRITCNSVISIVITILICLENSMVTVSRLILLEGPSLFVQSLVIYNYKAFTTRIPFTGCWYFNLFVTGIALGLNISLKISGLFTFAWVGILTCVQLWEILGDLRISIWQFIKHLVLRVVAFIMVPLTIYCSVFYIHFENLPNEGPGSGFLTPHFRSTLDDYQQQPLQVLYGSTITIKHNALEKYLHSHDLTYPRGSNLQQVTLYDFPDVNNEWVIETKQKYNEEKLMTDQREVKDGDVVRLYHKATGHYLHVNDIRPPISEHEYSYEVNGNETRGLLGNEDYEFKIRMLVKKPHAENDLPLIKLRTTETIFQLIHQATRCNLMSHEQKLPDWGEYQNEVLCVKEPTIPNTLWYVESSSHPLLKDTKKLKTFPKFSFWSKLIETHKVMFNLNKGFTNPHPYASKPLDWPLLSRGIAFFSNYNLKSIDEESSLIYYLGNVAIYYSVFFVGLIAIFKCAIYSFIKLNPYASPPSSSKSSPYANFYNNSWPYLVGWFINYIPYCLMSRNLYLHHYLSALNFGILLLSQYLNYRVAKNKIIGGIITATIFVSAIYCFYEFIPITYGLPWTLDQCNSHKWFPNWDIDCMTYTG
Protein: Interleukin-7 (IL-7) (P10168)
Organism: Mus musculus (Mouse)
Function: Hematopoietic cytokine that plays an essential role in the development, expansion, and survival of naive and memory T-cells and B-cells thereby regulating the number of mature lymphocytes and maintaining lymphoid homeostasis. Mechanistically, exerts its biological effects through a receptor composed of IL7RA subunit and the cytokine receptor common subunit gamma/CSF2RG. Binding to the receptor leads to activation of various kinases including JAK1 or JAK3 depending on the cell type and subsequently propagation of signals through activation of several downstream signaling pathways including the PI3K/Akt/mTOR or the JAK-STAT5.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P13232}.
Interaction partners:
- Cytokine receptor common subunit gamma
- Interleukin-7 receptor subunit alpha
- Interleukin-9
- Interleukin-4
- Tyrosine-protein kinase JAK3
- Interleukin-5
- Interleukin-2
- Interleukin-10
- Interleukin-6
- Interleukin-3
Sequence:
MFHVSFRYIFGIPPLILVLLPVTSSECHIKDKEGKAYESVLMISIDELDKMTGTDSNCPNNEPNFFRKHVCDDTKEAAFLNRAARKLKQFLKMNISEEFNVHLLTVSQGTQTLVNCTSKEEKNVKEQKKNDACFLKRLLREIKTCWNKILKGSI
Protein: Homeobox protein CDX-1 (Caudal-type homeobox protein 1) (P47902)
Organism: Homo sapiens (Human)
Function: Plays a role in transcriptional regulation. Involved in activated KRAS-mediated transcriptional activation of PRKD1 in colorectal cancer (CRC) cells. Binds to the PRKD1 promoter in colorectal cancer (CRC) cells. Could play a role in the terminal differentiation of the intestine. Binds preferentially to methylated DNA.
Subcellular location: Nucleus.
Interaction partners:
- Lymphoid enhancer-binding factor 1
Sequence:
MYVGYVLDKDSPVYPGPARPASLGLGPQAYGPPAPPPAPPQYPDFSSYSHVEPAPAPPTAWGAPFPAPKDDWAAAYGPGPAAPAASPASLAFGPPPDFSPVPAPPGPGPGLLAQPLGGPGTPSSPGAQRPTPYEWMRRSVAAGGGGGSGKTRTKDKYRVVYTDHQRLELEKEFHYSRYITIRRKSELAANLGLTERQVKIWFQNRRAKERKVNKKKQQQQQPPQPPMAHDITATPAGPSLGGLCPSNTSLLATSSPMPVKEEFLP
Protein: GDP-D-glucose phosphorylase 1 (EC 2.7.7.78) (Metabolite control phosphorylase 1) (Q5ZR76)
Organism: Caenorhabditis elegans
Function: Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21507950}.
Interaction partners:
Sequence:
MEPFPRILDDRLPRNMRRPRPIDKMPMRKIVMLGANARTQRSVSSIQLPAEYSPSASSAPYFNYSPDDFILDLRSHQSDEIYENGNSNHEKDEKKALKELLHERWENAKQYNAFNYPLNCMYRCLDGKYDLSMQLNIERGELRRKPMHFKNIKEPFNHLRFNFAKLHDHEILFYLKCDTDPISNDLLDRHLVAVNASPLERDHSLIVPSVNKCSPQVLTLQAVRIAVDLMLLVDDDMFHILFNSLLGQASVNHLHLHAMYWPYDSDLINRKCEPLHDVPNVYVIRPPVWICPAIVFQLDSLDNYEQFKMNIYKCVEHLTESNQAHNLFLARAQPIRTTGAEKEEDRRGERPQLVTCYVFPRMNMIGAKPPSNFNPAANELAGNLTSYTIRFFESANEQSVIRIIEEEASLDDDTFRSLCFDLADVLIGRSVGTSRPQDLDTLAGLTSPEIDELRDSFQSFMPRSPSIRHRSSTRAQSDEGSK
Protein: Phenoloxidase-activating factor 1 (EC 3.4.21.-) (Prophenoloxidase-activating factor I) (Serine protease PPAF-1) [Cleaved into: Phenoloxidase-activating factor 1 light chain; Phenoloxidase-activating factor 1 heavy chain] (O97366)
Organism: Holotrichia diomphalia (Korean black chafer)
Function: Serine endopeptidase which, by cleaving prophenoloxidase PPO1 and PPO2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products.
Subcellular location: Secreted {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}.
Interaction partners:
Sequence:
MKQVHFFILWFFVLNLYSIKAQAGCRTPNGENARCVPINNCKILYDSVLTSDPEVIRFLRASQCGYNGQPLVCCGSSASYQPPPTSASIRNRRPELLPNDCGYQVEADKILNGDDTVPEEFPWTAMIGYKNSSNFEQFACGGSLINNRYIVTAAHCVAGRVLRVVGALNKVRLGEWNTATDPDCYGAVRVCVPDKPIDLGIEETIQHPDYVDGSKDRYHDIALIRLNRQVEFTNYIRPVCLPQPNEEVQVGQRLTVVGWGRTETGQYSTIKQKLAVPVVHAEQCAKTFGAAGVRVRSSQLCAGGEKAKDSCGGDSGGPLLAERANQQFFLEGLVSFGATCGTEGWPGIYTKVGKYRDWIEGNIRP
Protein: Potassium channel tetramerisation domain-containing 12.2 (Righton) (Q561T3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- A kinase
- Ca++-dependent secretion activator 2.
- POU domain protein.
Sequence:
MDKTRADASSPRFSEIIELNVGGQVYVTRHSTLLSVPNSLLWTMFSQKKPAELTTDSKGRFFLDRDGFLFRYILDYLRDQTLVLPDYFKEKASLLKEAEYFQLQDLAKRLKPAVSKENSISEEVCQSDPEEAALAGTSMTCTGPRSPSLDARKTGFITIGYRGSYTIGRDLQQDAKFRRVARITVCGKTSLAKEVFGETLNESRDPDRPPERYTSRYYLKYNFLEQAFDRLAEVGFHMVACSSTGTCAYASNDPNEDKIWTSYTEYVFCRE
Protein: Gibberellin 2-beta-dioxygenase 3 (EC 1.14.11.13) (Gibberellin 2-beta-hydroxylase 3) (Gibberellin 2-oxidase 3) (GA 2-oxidase 3) (OsGA2ox3) (Q8S0S6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins, leading to the homeostatic regulation of their endogenous level. Catabolism of gibberellins (GAs) plays a central role in plant development. In vitro, converts GA1, GA20, and GA29 to the corresponding 2-beta-hydroxylated products GA8, GA29-catabolite, respectively.
Interaction partners:
- Gibberellin 20 oxidase 1
- Gibberellin 20 oxidase 3
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 3-beta-dioxygenase 1
- Os05g0257800 protein
- Os04g0517600 protein
Sequence:
MVVLAGPPAVDHIPLLRSPDPGDVFSGVPVVDLGSPGAARAVVDACERYGFFKVVNHGVATDTMDKAESEAVRFFSQTQPDKDRSGPAYPFGYGSKRIGFNGDMGWLEYLLLALDDASLADACTVPSCAVFRAALNEYISGVRKVAVRVMEAMSEGLGIAQADALSALVTAEGSDQVFRVNHYPPCRALQGLGCSVTGFGEHTDPQLVSVLRSNGTSGLQIALRDGQWVSVPSDRDSFFVNVGDSLQVLTNGRFKSVKHRVVANSLKSRVSFIYFGGPPLAQRIAPLPQLLGEGEQSLYKEFTWDEYKKAAYKSRLGDNRLAQFEKK
Protein: Neuralized E3 ubiquitin protein ligase 4 (A0A1L4AAD6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable E3 ubiquitin-protein ligase HERC2
- GEO11166p1
- Centriolar coiled coil protein 110kDa, isoform B
Sequence:
MTGREAQSFHTRCGRSIRLYNNNRMAQRSMRDFSHALVFSAEPLEDDVLFEVVIEKKNTYWGGSIEIGVTAESPDDLELVACATAMRNGTWVMSGIDVRKDGRRLFEFYGTDLETLNENDRVGVMRTSGNDLVFYVNGESQGVAAKNMPKPLWALVDLYGRCVQVSLCPRDGSGSGELLDSPLQQPLQQVVQNLDVAMNVNIVVDSDAWMQGNGSVSGADDRLCFHTRCGSLVKLSPNFRSAERRRPLDEFNNGVVMTHRPLRDNELFEIRIDKLVDKWSGSIEVGVTTHNPAVLHFPATMTNMRSGTIMMSGCGILTNGKGTRRQYGEFNLDELREGDRVGMMRKANGNLHNYINGQDQGVAATRAPSTLWGVIDLYGMTIKVTIVDRDEREQQNLVTRRNNIVAGMTACSSGAGAQHTQHQQHSGTPTLSLLSPESEMNAAGAAGGLSETISSTRAIARNDDRLTFHHICGTHATVTQSGRTALRPNAADDFNNGVVLTRRPLRPNELFQVRLERVVTKWAGSVEMGVTTHSADELDFPFTMTNVRSGTWMMTGNGVMQNGVTVIEQYGQNLDRLQVGDRVGVVRKDDGTLHFWVNGVDQGPAANNVPERVYGVIDLYGQAAQASIVDTSECGSPDTGNSTISNTTLYSEVPLRFHSIHGANAGISNSGLTASRPNSLAEFNDAIVFSNRPLRQRELFEVELETMVRHWSGNIEIGVTGTRPEDIQLAPNATDLEASDTIILCGPMIFHNRKTIRTNILLDLDTLGPSTRVGVMRNGDFIHFFVDGMDQGPACECHAPNIWAIIDLYGQCAQVSLTQTQLDIRAPYATSENSQSCQATSVIQHPAMETKHRWTCVSGNVSLTKDWTEASRFTGAAAPLSHCLVFSEHPLSVGSPFEIKLTSVNSMFAGCLSIGVTDLNLSDESVRKKLPTSIRRIPANVWYVSGNEVCFNSSCLQRSLASLEWLRVDDRITLERVENSLNILLNSENVNIHFHNVPNDVYVVAELRGSTMGIQVISAQGPASPLRPCSLRLQDSMDFGVDPLNKQDSSMLESIDSEALNYEFLDVSQKNARLSDDRRSVTRIKSYNQSIVCLNKPLCKGESISIKVDALNNKWKGTVGLGVLSASPQTVPISLLDFKRSCWLATHDYVNINGQVMPSKYGDALEQIQVGTVITLTLTHAGMLIIMIGSTNLEDLASGLPNHVYPVFDVYGKCEKITLITGNDAGRTGNANGTPILEAPEALELDNGMPQQCEKAHLEMHEKEKDTEQVCESGPSTSGAPSNAMTRSVMESVSENLLLNISIKNRTLEQQRNELGGSSSTCCLRESLQLQHNTNLNIQRSQSTQRFQNSLNTSATAAGSSGTSGCTANTQHLSNSGVYDTNKEYDDLPNPPNPLVNSVDEASGAITSVSTTIDHSENNAEALELSASNEREMSGEPALNDNVLEDDEIDYMNHLLLLQQLQQNEYTRHHLMPDQASLLNLDLPSLNSMESDTNSVGQTRPSGGTDSLRSTATGASVEQNDCEYLRQVRRFCASLVLPQAFFDSRLEPVCFCLKCSGPSIGGNGDKLEGWVYFKLNQQTVNVLSTSTSTASAGGGASSATAPQVHFDLNGDWLPFYYMTRVDKIRAILDRGQPLPLETDPDEEPAAAALKDEPGTRLELYYSPNATVIEPVLPQHHFASEQGLHRISTSFEVYVRRQSISGVTTGKAAAEAKRRSLGSTDHDHGGTGQGADGVGVTPSATLNESSVHLLNDLCWFTKEAGACIINALIIKLDRIEESESH