wanglab/gogpt-training-data huggingface dataset:
Protein: Slit homolog 2 protein (Slit-2) (Q9WVC1)
Organism: Rattus norvegicus (Rat)
Function: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal cord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal cord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. Seems to be involved in regulating leukocyte migration (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Roundabout guidance receptor 2
- Roundabout homolog 1
- Roundabout homolog 4
- Roundabout homolog 4
- Roundabout homolog 3
- Netrin-1
- Adhesion G protein-coupled receptor L2
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
Sequence:
MSGIGWQTLSLSLALVLSILNKVAPHACPAQCSCSGSTVDCHGLALRIVPRNIPRNTERLDLNGNNITRITKTDFAGLRHLRILQLMENKISTIERGAFHDLKELERLRLNRNNLQLFPELLFLGTAKLYRLDLSENQIQAIPRKAFRGAVDIKNLQLDYNQISCIEDGAFRALRDLEVLTLNNNNITRLSVASFNHMPKLRTFRLHSNNLYCDCHLAWLSDWLRQRPRVGLYTQCMGPSHLRGHNVAEVQKREFVCSDEEEGHQSFMAPSCSVLHCPIACTCSNNIVDCRGKGLTEIPTNLPETITEIRLEQNSIRVIPPGAFSPYKKLRRLDLSNNQISELAPDAFQGLRSLNSLVLYGNKITELPKSLFEGLFSLQLLLLNANKINCLRVDAFQDLHNLNLLSLYDNKLQTVAKGTFSALRAIQTMHLAQNPFICDCHLKWLADYLHTNPIETSGARCTSPRRLANKRIGQIKSKKFRCSGTEDYRSKLSGDCFADLACPEKCRCEGTTVDCSNQKLNKIPDHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINLSNNKITDIEEGAFEGASGVNEILLTSNRLENVQHKMFKGLESLKTLMLRSNRISCVGNDSFTGLGSVRLLSLYDNQITTVAPGAFGTLHSLSTLNLLANPFNCNCHLAWLGEWLRRKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDDGNDDNSCSPLSRCPSECTCLDTVVRCSNKGLKVLPKGIPRDVTELYLDGNQFTLVP
Protein: Protein Jade-3 (Jade family PHD finger protein 3) (PHD finger protein 16) (Q92613)
Organism: Homo sapiens (Human)
Function: Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity.
Interaction partners:
- Histone acetyltransferase KAT7
- Chromatin modification-related protein MEAF6
- Inhibitor of growth protein 4
- Inhibitor of growth protein 5
Sequence:
MKRHRPVSSSDSSDESPSTSFTSGSMYRIKSKIPNEHKKPAEVFRKDLISAMKLPDSHHINPDSYYLFADTWKEEWEKGVQVPASPDTVPQPSLRIIAEKVKDVLFIRPRKYIHCSSPDTTEPGYINIMELAASVCRYDLDDMDIFWLQELNEDLAEMGCGPVDENLMEKTVEVLERHCHENMNHAIETEEGLGIEYDEDVICDVCRSPDSEEGNDMVFCDKCNVCVHQACYGILKVPEGSWLCRSCVLGIYPQCVLCPKKGGALKTTKTGTKWAHVSCALWIPEVSIACPERMEPITKISHIPPSRWALVCNLCKLKTGACIQCSIKSCITAFHVTCAFEHGLEMKTILDEGDEVKFKSYCLKHSQNRQKLGEAEYPHHRAKEQSQAKSEKTSLRAQKLRELEEEFYSLVRVEDVAAELGMPTLAVDFIYNYWKLKRKSNFNKPLFPPKEDEENGLVQPKEESIHTRMRMFMHLRQDLERVRNLCYMISRREKLKLSHNKIQEQIFGLQVQLLNQEIDAGLPLTNALENSLFYPPPRITLKLKMPKSTPEDHRNSSTETDQQPHSPDSSSSVHSIRNMQVPQESLEMRTKSYPRYPLESKNNRLLASLSHSRSEAKESSPAWRTPSSECYHGQSLGKPLVLQAALHGQSSIGNGKSQPNSKFAKSNGLEGSWSGNVTQKDSSSEMFCDQEPVFSPHLVSQGSFRKSTVEHFSRSFKETTNRWVKNTEDLQCYVKPTKNMSPKEQFWGRQVLRRSAGRAPYQENDGYCPDLELSDSEAESDGNKEKVRVRKDSSDRENPPHDSRRDCHGKSKTHPLSHSSMQR
Protein: FHA domain-containing protein (Q584H2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIVGQMRRASVAGSSDSVLAIRSCFDNRDAVLFIQPGDGALLVADGHRYVQVILHFHGVTRFPSLIVLPWEQHRFSVRVNNVLYDDGPISLDVGDEIELMDSRSRLTADRCVFRVELLTTGCGPYVSELLANGNRTDNAVPAHKPYKVGQGSCWAEFVNHRVGKLDKVLSRVKR
Protein: Limostatin, isoform C (A0A0B4K7D0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTTTMAAPQQQEVPHALLDIETPNQFNYSPSPLAQPDSLRSKPYFDFLSTLYAHDTAKSNLFRPYSVRQRRDADVQKLSRPRRAIVFRPLFVYKQQEIRKQEIRDRNAQRRHDLNRLQRV
Protein: CDKN1A interacting zinc finger protein 1 (F6XWQ4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XRVQPQTQMTAPKQTQTPDRLPEPPEVQMLPRIQPQALQIQTQPKLLRQAQTQTSPEHLAPQQDQVEPQVPTQAQSQEQTSEKTQDQPQTWPQGSVPPPEQASGPACATEPQLSSHAAEAGSDPDKALPEPVSAQSSEDRSREASAGGLDLGECEKRAGEMLGMWGAGSSLKVTILQSSNSRAFNTTPLTSGPRPGDSTSATPAIASTPSKQSLQFFCYICKASSSSQQEFQDHMSEAQHQQRLGEIQHSSQTCLLSLLPMPRDILEKEAEDPPPKRWCNTCQVYYVG
Protein: Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) (P19620)
Organism: Sus scrofa (Pig)
Function: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane.
Interaction partners:
- Protein S100-A10
- Tissue-type plasminogen activator
- PDZ domain-containing protein.
- PDZ domain-containing protein
- Protein S100
- Annexin A1
- Cellular tumor antigen p53
- Plasminogen
- Protein S100-A11
- Galectin.
Sequence:
MSTVHEILCKLSLEGDHSTPASAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIXIMVSRSEVDMLKIRSEFKRKYGKSLYNYIQQDTKGDYQKALLYLCGGDD
Protein: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein (A8MQX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Defensin-like protein 204
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Disease resistance protein-like
- Uncharacterized protein
- Transmembrane protein
- Uncharacterized protein
- Uncharacterized protein
- STAY-GREEN-like protein
- Glycine-rich protein homolog
- Uncharacterized protein
Sequence:
MASKNMTTIMALFLTFNLVFLGFTSAQPVCPLNQSELGICVNVLGLISITTSNAAQCCSILAGLNNVSLVSVCACEAVRLNILNLLGITVNLNLRLNGLLGLCRLPVQPGFNCLL
Protein: Tropomyosin alpha-1 chain (A0A060W8G0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Troponin T type 2b
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Troponin T2d, cardiac
- Troponin T2e, cardiac
- Troponin T2e, cardiac
- Uncharacterized protein
- Troponin I, slow skeletal muscle
Sequence:
MDAIKKKMQMLKLDKENALDRAEGAEGDKKAAEDKSKQLEDEISELEKKLRITEDERDKVLDEFQAAEEKFLNAEEVATKLEDDLVALQKKLKGTEDELDKYSESLKDAQEKLEVAEKTATDAEADVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRASKDEEKMELQDIQLKEAKHIAEEADRKYEEVARKLVIIESDLERTEERAELSEGKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEASYSSTAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDNALNDMTSM
Protein: Doublesex- and mab-3-related transcription factor A2 (Doublesex- and mab-3-related transcription factor 5) (Q5UU75)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May be involved in sexual development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
Interaction partners:
Sequence:
MDLRPEIPPASQAGSQVHPGAAAAAAAAASIPVSMAGSLLRAPPLLLRATEKYPRTPKCARCRNHGVVSALKGHKRYCRWKDCMCAKCTLIAERQRVMAAQVALRRQQAQEENEARELQLLYGTAEGLALAAANGIIPPRQNYEVFGPVSNESNSGESNIQKFELFPKTPLPGTVTPHQAAGKSVSTDTESVPGMSSPDMRHGSGSENGDRESIVSSPIAKPLKDGEETPGSISPIGSDSGSDTDKDEQEPSPSSAASRQMNAIDILTRVFPNHKRSVLELVLQGCGKNVVQAIEQILNNSGQAKGPEETWTAERMLQSVQPTMSSTPRPMLPGTMTLSNRSAFSPLQPNAPHFGSDPSTYPLSTHLGLNPLRLAYSAHSRGLAFMAPYSTTGLMPTLGFRPPMDYAFSDLIRDRTLLHKDQSYTNGLYGPLVNNTQEKQ
Protein: Rho guanine nucleotide exchange factor 26 (F6TAL7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
XVYQQRTLQKLLATNPSFKEVLSRIESHEDCRNLPMISFLILPMQRVTRLPLLMDTICQKTPKDSPKYEVCKRALKEVSKLVRLCNEGARKMERTEMMYTINSQLEFKIKPFPLVSSSRWLVKRGELTAYVEDTVLFSKRMSKQQVYFFLFNDVLIITKKKSEESYNVNDYSLRDQLLVESCDNEELNSSPGKNPSTMLYSRQSSATHLFTLTVLSNHASEKVDMLLGAETQSERARWITALGHSSGKQPPDRTSWY
Protein: Prostate tumor-overexpressed gene 1 protein (PTOV-1) (Activator interaction domain-containing protein 2) (Q86YD1)
Organism: Homo sapiens (Human)
Function: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:16639697}. Nucleus {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644}. Cell membrane {ECO:0000269|PubMed:15713644}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11313889}. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase (PubMed:12598323). Also localizes to lipid rafts (PubMed:15713644). {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644}.
Interaction partners:
- Flotillin-1
- Flotillin-2
- Kelch domain-containing protein 2
- CREB-binding protein
Sequence:
MVRPRRAPYRSGAGGPLGGRGRPPRPLVVRAVRSRSWPASPRGPQPPRIRARSAPPMEGARVFGALGPIGPSSPGLTLGGLAVSEHRLSNKLLAWSGVLEWQEKRRPYSDSTAKLKRTLPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNSQLAQFHFTNRDCDSLKGLCRIMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVSAIRQVITTRKQAVGPGGVNSGPVQIVNNKFLAWSGVMEWQEPRPEPNSRSKRWLPSHVYVNQGEILRTEQWPRKLYMQLIPQQLLTTLVPLFRNSRLVQFHFTKDLETLKSLCRIMDNGFAGCVHFSYKASCEIRVLMLLYSSEKKIFIGLIPHDQGNFVNGIRRVIANQQQVLQRNLEQEQQQRGMGG
Protein: Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial (EC 2.3.1.234) (Glycoprotease 1) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein GCP1) (tRNA threonylcarbamoyladenosine biosynthesis protein GCP1) (O22145)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance (By similarity). May have a role in embryonic development in plants.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:19694617}; Peripheral membrane protein {ECO:0000269|PubMed:19694617}.
Interaction partners:
- At4g34412
- non-specific serine/threonine protein kinase
- Transmembrane protein
- non-specific serine/threonine protein kinase
- Threonylcarbamoyl-AMP synthase
- Threonylcarbamoyl-AMP synthase
- Tryptophan synthase alpha chain, chloroplastic
- Glycoprotease 2
Sequence:
MVRLFLTLSPAISRFNLYPGISILARNNNSLRLQKHHKLKTKTPTFSLISPSSSPNFQRTRFYSTETRISSLPYSENPNFDDNLVVLGIETSCDDTAAAVVRGNGEILSQVISSQAELLVQYGGVAPKQAEEAHSRVIDKVVQDALDKANLTEKDLSAVAVTIGPGLSLCLRVGVRKARRVAGNFSLPIVGVHHMEAHALVARLVEQELSFPFMALLISGGHNLLVLAHKLGQYTQLGTTVDDAIGEAFDKTAKWLGLDMHRSGGPAVEELALEGDAKSVKFNVPMKYHKDCNFSYAGLKTQVRLAIEAKEIDAKCPVSSATNEDRRNRADIAASFQRVAVLHLEEKCERAIDWALELEPSIKHMVISGGVASNKYVRLRLNNIVENKNLKLVCPPPSLCTDNGVMVAWTGLEHFRVGRYDPPPPATEPEDYVYDLRPRWPLGEEYAKGRSEARSMRTARIHPSLTSIIRADSLQQQTQT
Protein: Alpha-2,8-sialyltransferase 8B (EC 2.4.3.-) (Polysialic acid synthase) (Sialyltransferase 8B) (SIAT8-B) (Sialyltransferase St8Sia II) (ST8SiaII) (Sialyltransferase X) (STX) (O35696)
Organism: Mus musculus (Mouse)
Function: May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92186}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q92186}. Secreted {ECO:0000250|UniProtKB:Q92186}. Cell membrane {ECO:0000250|UniProtKB:Q92186}. Note=Also trafficks to the cell surface. {ECO:0000250|UniProtKB:Q92186}.
Interaction partners:
- Neural cell adhesion molecule 1
- Syntaxin-2
Sequence:
MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSPPAVADRSNESLKHNIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFQTCAIVGNSGVLLNSGCGQEIDTHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHGLNGSILWIPAFMARGGKERVEWVNALILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCNQIYLYGFWPFPLDQNQNPVKYHYYDSLKYGYTSQASPHTMPLEFKALKSLHEQGALKLTVGQCDGAT
Protein: Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Rotamase A) (Q54SM3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10575348}.
Interaction partners:
- Ran-specific GTPase-activating protein homolog
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-processing factor 19
- Protein snwA
- Probable ATP-dependent RNA helicase ddx41
- Crooked neck-like protein 1
- Protein BUD31 homolog
- WD40 repeat-containing protein
- Nuclear pore protein
- Pre-mRNA-splicing factor SYF2
Sequence:
MTTVKPTSPENPRVFFDITIGGVEAGKVVMELYANTVPKTAENFRALCTGEKGIGKSGKPLSYKGSSFHRVITNFMCQGGDFTMGNGTGGESIYGNKFADENFKLKHFGQGTLSMANAGANTNGSQFFICVAPTDWLDGKHVVFGFVTEGMDVVKKMEAAGSQSGKTTKPVVIANCGQL
Protein: Protocadherin beta-12 (PCDH-beta-12) (Q9Y5F1)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin beta-7
Sequence:
MENGGAGTLQIRQVLLFFVLLGMSQAGSETGNFLVMEELQSGSFVGNLAKTLGLEVSELSSRGARVVSNDNKECLQLDTNTGDLLLREMLDREELCGSNEPCVLYFQVLMKNPTQFLQIELQVRDINDHSPVFLEKEMLLEIPENSPVGAVFLLESAKDLDVGINAVKSYTINPNSHFHVKIRVNPDNRKYPELVLDKALDYEERPELSFILTALDGGSPPRSGTALVRVVVVDINDNSPEFEQAFYEVKILENSILGSLVVTVSAWDLDSGTNSELSYTFSHASEDIRKTFEINQKSGDITLTAPLDFEAIESYSIIIQATDGGGLFGKSTVRIQVMDVNDNAPEITVSSITSPIPENTPETVVMVFRIRDRDSGDNGKMVCSIPEDIPFVLKSSVNNYYTLETERPLDRESRAEYNITITVTDLGTPRLKTEHNITVLVSDVNDNAPAFTQTSYALFVRENNSPALHIGSISATDRDSGTNAQVNYSLLPSQDPHLPLASLVSINADNGHLFALRSLDYEALQGFQFRVGATDHGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPWAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAAPVGRCSVPEGPFPGHLVDVSGTGTLSQSYHYEVCVTGGSRSNKFKFLKPIIPNFLPQSTGSEVEENPPFQNNLGF
Protein: Folic acid synthesis protein fol1 [Includes: Dihydroneopterin aldolase (DHNA) (EC 4.1.2.25) (7,8-dihydroneopterin aldolase) (FASA) (FASB); 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) (EC 2.7.6.3) (2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (PPPK) (FASC); Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase) (FASD)] (Q4LB35)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes three sequential steps of tetrahydrofolate biosynthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable dihydrofolate synthetase
- Probable folylpolyglutamate synthase
- GTP cyclohydrolase 1
- Putative aminodeoxychorismate synthase
- Putative aminodeoxychorismate lyase
- Alkaline phosphatase
- Branched-chain-amino-acid aminotransferase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, mitochondrial
- Multifunctional tryptophan biosynthesis protein
Sequence:
MKSLVNLWGIYPFIRNNSLHGFAKIPRIVSTIPRQLRFSSLRHPTRQMDLIHDTVVVENLNTFAVVGQDQWKRKEPQPVQIDVYMRNNVQLAGEKDELKSTIHYGIASKLLRKEIEGSFFTTPKDLVNKIASLCFEDVIDTSHVSIKLTLPKCVLRSKNGLHYYAERERNSTSNFVDRIEFSDLELATILGIHAFERQEKQRVCLNISFANTEVEALEIARAIAEYVEQSAFLTIEALVVNLSKYLCFTKNLDDISIKAEKPSAITFANASAVQIYRTRSYFLQESLHKYESTKNKIAYLSFGSNIGDKFEQIQTALSMLHKIEGIRVLDVSPLYETEPMYYKDQPSFLNGVCKIETRMSPINLLRACQSIEQEMGRIKTILKGPRCIDLDIVLYEDCVYESEVLTIPHLGLQEREFVLRPLLALSPDLVHPYTHQPLQEALDKLPSQGIRLYSSFDNKKIINGALTMGILNVTPDSFSDGGKVSQNNILEKAKSMVGDGASILDIGGQSTKPGADPVSVEEELRRVIPMISLLRSSGITVPISIDTYYSKVAKLAIEAGANIINDVTGGMGDEKMLPLAASLQVPICIMHMRGTPETMKALSIYEKDIVEEVAVELSSRVEAAVQSGVHRYNIILDPGFGFAKTPKQSAGLLGRLHELMKKPQFKDMHWLSGPSRKGFTGYFTGDASPKDRIWGTSACVTASVLQGVSIVRVHDTKEMSKVVGMANAIRYVP
Protein: Transcription factor PRE5 (Basic helix-loop-helix protein 164) (AtbHLH164) (bHLH 164) (Protein PACLOBUTRAZOL RESISTANCE 5) (bHLH transcription factor bHLH164) (Q9LJX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical and probable non DNA-binding bHLH transcription factor that integrates multiple signaling pathways to regulate cell elongation and plant development. May have a regulatory role in various aspects of gibberellin-dependent growth and development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor IBH1
- Auxin-responsive protein SAUR15
- Expansin-A8
- Transcription factor PIF4
- Transcription factor HBI1
- Steroid
Sequence:
MSNRRSRQTSNASRISDDQMIDLVSKLRQFLPEIHERRRSDKVSASKVLQETCNYIRKLHREVDNLSDRLSQLLDSVDEDSPEAAVIRSLLM
Protein: Glycogenin-1 (GN) (EC 2.4.1.186) (H2KYQ5)
Organism: Caenorhabditis elegans
Function: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for gsy-1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13280}. Nucleus {ECO:0000250|UniProtKB:P13280}. Note=Localizes to glycogen granules (glycosomes) in the cytoplasm. {ECO:0000250|UniProtKB:C4R941}.
Interaction partners:
- Glycogen [starch] synthase
- 1,4-alpha-glucan branching enzyme
- UTP--glucose-1-phosphate uridylyltransferase
- glycogenin glucosyltransferase
- Protein phosphatase 1 regulatory subunit
- phosphoglucomutase
- Glycogen debranching enzyme
- Serpentine Receptor, class T
- Alpha-1,4 glucan phosphorylase
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MSEAWITLATNDNYAQGALVLVHSLRTAGTTRKIHCLISNEVSAPVRKQLEEHFDDVSIVDVFNSNDSDNLRLIERPDLGVTFTKLHCWRLTQYTKCVFLDADTLVLRNADELFTRPDFSAASDIGWPDSFNSGVFVYVPNNETYRQLVDFAVTHGSYDGGDQGLLNDFFSNWRDLPSEHRLPFIYNMTAGAFYTYAAAYKRYGANTKIVHFIGSVKPWHGSAAVHTGEHFQQWQKIYHAHVNHTSRTNEHAAVFPSHHHTPEHRSHSADHPKIERKDSIVREIGNFVMHVVQSVNILPSYDTDANTSDSHRNNEPHKHDQQREEHHELPHNKFQTPHEESQDIVGSTDCFGSQMPKYNADSETDREVEQITNNTPCPAFVPFERREEYQAASPSTEERRAAWEAGQPDYLGRDAFVHIQEALNRALNE
Protein: Homer protein homolog 2 (Zgc:111960) (Q502P2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MGEQPIFTTRAHVFQIDPTTKKNWVPASKQAVTVSYFYDSARNSYRIISVDGTKVIINSTITPNMNFTKTSQKFGQWADSRANTVFGLGFASEQQLSKFAEKFLEVKEAAKLAREKSQDKMETSSDQSQESGRDTPSGNQPSSINGTDDEKISHSGPETAALKAESSAESRKTQATRSLEENNQLRSKIAELELQCKELSVERERNAQLTVRIQELEADLQDKQQELENLRKQAEIIPQLMAECESLSGKLQAAELSSSGLRERVELLQGEAQHRQQQQNSLKTELKLLMEQLDGKIDELHEVRQGISKLGIDN
Protein: Coenzyme F420:L-glutamate ligase (EC 6.3.2.31) (EC 6.3.2.34) (Coenzyme F420-0:L-glutamate ligase) (Coenzyme F420-1:gamma-L-glutamate ligase) (F420:glutamyl ligase) (Q58178)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the GTP-dependent successive addition of two L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2), with a gamma-linkage between the two glutamates. Cannot use F420-2 as substrate to add more glutamates. Exhibits maximum activity with GTP, compared with UTP (66%) and dGTP (25%); with ATP, only F420-1 is observed as the product; CTP and TTP support no activity.
Interaction partners:
- 2-phospho-L-lactate transferase
- 2-phospho-L-lactate guanylyltransferase
- 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
- Coenzyme gamma-F420-2:alpha-L-glutamate ligase
- 5,10-methylenetetrahydromethanopterin reductase
- F420-dependent NADP reductase
- Shikimate dehydrogenase
- Dihydroneopterin aldolase
- Beta-ribofuranosylphenol 5'-phosphate synthase
Sequence:
MIKEKRKVEVIGLELPIFKGGEQINLSELIAQYPIEDGDIIVIAETLISKLEGGVIDRDKIIPSKEAIELAKKTGKDPKVVQVILDEAKEIVKVGKNFIITETKHGFVCANSGVDESNIYKGIKILPKNPDESAEKIRKEIEKLTGKRVGVIISDSVGRPFRKGAVGIAIGVSGILALWDRKGEKDLFGRELKTTEVAIADELASMANVVMGEADEGIPVVIIRGANVPFGNGKGRDLIRPKEEDVFRN
Protein: Adenylosuccinate synthetase isozyme 2 (AMPSase 2) (AdSS 2) (EC 6.3.4.4) (Adenylosuccinate synthetase, acidic isozyme) (Adenylosuccinate synthetase, liver isozyme) (L-type adenylosuccinate synthetase) (IMP--aspartate ligase 2) (D4AEP0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03127}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
- Trifunctional purine biosynthetic protein adenosine-3
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- AMP deaminase 1
- GMP reductase 1
- GMP reductase
- Argininosuccinate synthase
- Inosine triphosphate pyrophosphatase
Sequence:
MSISESSPAATSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRCQGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGLDGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLRMCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQQLKGYMERIKPMVRDGVYFLYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAYTTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALALTKLDILDMFTEIKVGVAYKLDGETIPHFPANQEVLNKVEVQYKTLPGWNTDISNARTFKELPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Protein: Calcium-binding tyrosine phosphorylation-regulated protein (Calcium-binding protein 86) (Cancer/testis antigen 88) (CT88) (Fibrousheathin II) (Fibrousheathin-2) (FSP-2) (Testis-specific calcium-binding protein CBP86) (O75952)
Organism: Homo sapiens (Human)
Function: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform 4 probably does not bind calcium.
Subcellular location: Cytoplasm, cytoskeleton. Cell projection, cilium, flagellum. Note=Localized to fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.; SUBCELLULAR LOCATION: [Isoform 5]: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.
Interaction partners:
- A-kinase anchor protein 3
- Fibrous sheath CABYR-binding protein
- Ropporin-1A
- Sperm surface protein Sp17
- Ropporin-1-like protein
- A-kinase anchor protein 1, mitochondrial
- Rhophilin-1
- A-kinase anchor protein 4
- cAMP-dependent protein kinase type II-alpha regulatory subunit
Sequence:
MISSKPRLVVPYGLKTLLEGISRAVLKTNPSNINQFAAAYFQELTMYRGNTTMDIKDLVKQFHQIKVEKWSEGTTPQKKLECLKEPGKTSVESKVPTQMEKSTDTDEDNVTRTEYSDKTTQFPSVYAVPGTEQTEAVGGLSSKPATPKTTTPPSSPPPTAVSPEFAYVPADPAQLAAQMLGKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVAAPLVCSGKVLEVQVVNQTSVHVDLGSQPKENEAEPSTASSVPLQDEQEPPAYDQAPEVTLQADIEVMSTVHISSVYNDVPVTEGVVYIEQLPEQIVIPFTDQVACLKENEQSKENEQSPRVSPKSVVEKTTSGMSKKSVESVKLAQLEENAKYSSVYMEAEATALLSDTSLKGQPEVPAQLLDAEGAIKIGSEKSLHLEVEITSIVSDNTGQEESGENSVPQEMEGKPVLSGEAAEAVHSGTSVKSSSGPFPPAPEGLTAPEIEPEGESTAE