wanglab/gogpt-training-data huggingface dataset:
Protein: Protein FAM193A (Protein IT14) (P78312)
Organism: Homo sapiens (Human)
Interaction partners:
- Dynactin subunit 2
Sequence:
MKVRLLRQLSAAAKVKAPSGLQGPPQAHQFISLLLEEYGALCQAARSISTFLGTLENEHLKKFQVTWELHNKHLFENLVFSEPLLQSNLPALVSQIRLGTTTHDTCSEDTYSTLLQRYQRSEEELRRVAEEWLECQKRIDAYVDEQMTMKTKQRMLTEDWELFKQRRFIEEQLTNKKAVTGENNFTDTMRHMLSSRLSMPDCPNCNYRRRCACDDCSLSHILTCGIMDPPVTDDIHIHQLPLQVDPAPDYLAERSPPSVSSASSGSGSSSPITIQQHPRLILTDSGSAPTFCSDDEDVAPLSAKFADIYPLSNYDDTEVVANMNGIHSELNGGGENMALKDESPQISSTSSSSSEADDEEADGESSGEPPGAPKEDGVLGSRSPRTEESKADSPPPSYPTQQAEQAPNTCECHVCKQEASGLTPSAMTAGALPPGHQFLSPEKPTHPALHLYPHIHGHVPLHTVPHLPRPLIHPTLYATPPFTHSKALPPAPVQNHTNKHQVFNASLQDHIYPSCFGNTPEWNSSKFISLWGSEVMNDKNWNPGTFLPDTISGSEILGPTLSETRPEALPPPSSNETPAVSDSKEKKNAAKKKCLYNFQDAFMEANKVVMATSSATSSVSCTATTVQSSNSQFRVSSKRPPSVGDVFHGISKEDHRHSAPAAPRNSPTGLAPLPALSPAALSPAALSPASTPHLANLAAPSFPKTATTTPGFVDTRKSFCPAPLPPATDGSISAPPSVCSDPDCEGHRCENGVYDPQQDDGDESADEDSCSEHSSSTSTSTNQKEGKYCDCCYCEFFGHGGPPAAPTSRNYAEMREKLRLRLTKRKEEQPKKMDQISERESVVDHRRVEDLLQFINSSETKPVSSTRAAKRARHKQRKLEEKARLEAEARAREHLHLQEEQRRREEEEDEEEEEDRFKEEFQRLQELQKLRAVKKKKKERPSKDCPKLDMLTRNFQAATESVPNSGNIHNGSLEQTEEPETSSHSPSRHMNHSEPRPGLGADGDAADPVDTRDSKFLLPKEVNGKQHEPLSFFFDIMQHHKEGNGKQKLRQTSKASSEPARRPTEPPKATEGQSKPRAQTESKAKVVDLMSITEQKREERKVNSNNNNKKQLNHIKDEKSNPTPMEPTSPGEHQQNSKLVLAESPQPKGKNKKNKKKKGDRVNNSIDGVSLLLPSLGYNGAILAHCNLRLPGSSDCAASASQVVGITDDVFLPKDIDLDSVDMDETEREVEYFKRFCLDSARQTRQRLSINWSNFSLKKATFAAH
Protein: Putative transcription factor SOX-15 (Sox50E) (P40657)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MEPSYDHEHPHHLLTNYNSKKYPHVSRTPEYSHSTGSDYPEHGGYLTDGRLMHESNSDAGIYHVRQGSEHSSPSLHSPAIQSSGYENEHLNEAVLAAHSHSHSPMPMVSSAYVGGGTASGSLINSNIPLLGGGGNSVLNKFLSHPHAGMVGGGTGQMEDCTSHSPIEAASMWSYDYKGDLCAPNCGYLERHKPLPADLKYRPGGTQSKSAKESRIRRPMNAFMVWAKIERKKLADENPDLHNADLSKMLGKKWRSLTPQDRRPYVEEAERLRVIHMTEHPNYKYRPRRRKQSKLRAMQPGGKEQSESSPNPGTGGSKSNPKLATPPLATASSSYTTPTDESTCNSTNQNHGQSTPGGLYEQPLKPTYSPSSVDCYSNADSTEQIESLAANCPPALLNESSPTGGGYDNSLLLKKLTKPSPSRAAKSRQEKLAKSEEKNKGSQSQGQSQQGIYAATYPLAPTSVAVVAARGMYVTCNNRGLLDHGHSVKGTFYPPVSVSEDDNSTSMRNSISALQQHCNVVTSTPSSSGGTMPTSEMSSYTVSMADNCGNLRLSMNELSGNEYLPSANAYGMQYEDFLRYQSNDMDYSTSAVEHKETTSDSASGQKCLKYPDTNQNYDDYEAEAYSNAMLPATAASYYTQLPYPPTSLAAFPLQLAVPFQQTTSGAYGAQPIQSGYLHYGNYGGYEGMAQSQPQNQAPVHHQQASHSAPPSLSVPPNQTVTSNSAAISMQQHHHHHFGPAPGMVGVGVGVGVGVGVGEMLFEQQQRKDDEISNILAGVRKTCYSN
Protein: Homeobox protein Hox-A6 (Homeobox protein Hox-1.2) (Homeobox protein M5-4) (P09092)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-A7
- Homeobox protein Hox-C4
- Homeobox protein Hox-B5
Sequence:
MSSYFVNPTFPGSLPSGQDSFLGQLPLYPAGYDALRPFPASYGASSLPDKTYTSPCFYQQSNSVLACNRASYEYGASCFYSDKDLSGASPSGNNKQRGPGDYLHFSPEQQYKPDGSVQGKALHEEGTDRKYTSPVYPWMQRMNSCAGAVYGSHGRRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIANALCLTERQIKIWFQNRRMKWKKENKLINSTQASGEDSEAKAGE
Protein: 3',5'-bisphosphate nucleotidase 2 (EC 3.1.3.7) (3',5'-bisphosphonucleoside 3'-phosphohydrolase 2) (3'-phosphoadenosine-5'-phosphate phosphatase 2) (PAP phosphatase 2) (PAPase 2) (DPNPase 2) (Inositol polyphosphate 1-phosphatase 2) (IPPase 2) (Inositol-1,4-bisphosphate 1-phosphatase 2) (EC 3.1.3.57) (Phosphatase SAL2) (O49623)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Prevents both the toxicity of PAP on RNA processing enzymes as well as the product inhibition by PAP of sulfate conjugation. Is also able to hydrolyze inositol 1,4-bisphosphate.
Interaction partners:
- Phosphatase IMPL1, chloroplastic
- Bifunctional phosphatase IMPL2, chloroplastic
- Inositol-tetrakisphosphate 1-kinase 2
- Inositol-tetrakisphosphate 1-kinase 3
- Inositol 1,3,4-trisphosphate 5/6-kinase 4
- Inositol-tetrakisphosphate 1-kinase 1
- Inositol-phosphate phosphatase
- 5'-adenylylsulfate reductase 1, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
Sequence:
MSYEKELAAAKKAVTLAARLSQEVQKTLLQSQVWKKSDRSPVTAADYGSQAVVSLVLERELQPDKLSLVAEEETGDLRKNGSEAFLEDIAKLVKDTLASEESYTSSPLSTDDVLNAIDCGKSEGGCKGSHWVLDPIDGTRGFVRGEQYAVGLALLVEGKVVLGVMACPNLPLASAVCATDNSSQEDVGCLFFATTGSGTYVQSLKGNSLPQKVQVSSNENLDEAKFLESYHKPIPIHGTIAKKLGIKALPVRIDSQAKYAALSRGDAEIYLRFTLNGYRECIWDHAPGSIITTEAGGVVCDATGKSLDFSKGKYLAHKTGIIVTTKKLKPWILKAVRESIEEENLYF
Protein: Ras-related protein Rab-12 (EC 3.6.5.2) (Rab-13) (P35283)
Organism: Mus musculus (Mouse)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy.
Subcellular location: Recycling endosome membrane {ECO:0000269|PubMed:21718402}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:21718402}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P51152}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23357852}.
Interaction partners:
- MICAL-like protein 2
- BICD family-like cargo adapter 2
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- DENN domain-containing protein 3
- MICAL-like protein 1
- Rab GDP dissociation inhibitor alpha
- Tight junction protein 1
- Rab GDP dissociation inhibitor beta
Sequence:
MDPSAALHRRPAGGSLGAVSPALSGGQARRRKQPPRPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREISRQQGEKFAQQITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDVLRNELSNSILSLQPEPEIPPELPPPRPHVRCC
Protein: Mannose-1-phosphate guanyltransferase (EC 2.7.7.13) (GDP-mannose pyrophosphorylase) (GTP-mannose-1-phosphate guanylyltransferase) (O74484)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint. Required for the correct assembly of the septum.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16049679}.
Interaction partners:
- Probable mannose-1-phosphate guanyltransferase
- Phosphomannomutase
- Dolichol-phosphate mannosyltransferase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- Uncharacterized protein C2D10.19c
- Uncharacterized protein PB2B2.11
- Fumarate reductase
- Probable eukaryotic translation initiation factor 2 subunit beta
Sequence:
MKALILVGGFGTRLRPLTLTLPKPLVEFGNKPMILHQVEALAAAGVTDIVLAVNYRPEIMVEALKKYEKEYNVNITFSVENEPLGTAGPLALARDILAKDHSPFFVLNSDVICEYPFADLAAFHKAHGAEGTIVVTKVEEPSKYGVVVHYPNSESLIERFVEKPVEFVSNRINGGIYILNPSVLDRIEPRPTSIEKEVFPAMVNDKQLHSFDLEGYWMDVGQPKDYLTGTCLYLSSLRKHKPEILAPASSNIIGNVLIDPSATIGKNCKIGPNVVIGPNVTIGDGVRLQRCAILKSSRVRDHAWVKSSIVGWNSTLGSWSRLENVSVLGDDVVVNDEIYVNGGSILPHKSISANIEVPGTIVM
Protein: CAAX prenyl protease 2 (EC 3.4.26.1) (Farnesylated proteins-converting enzyme 2) (FACE-2) (G5EEP3)
Organism: Caenorhabditis elegans
Function: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y256}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12487630}.
Interaction partners:
- CAAX prenyl protease 1 homolog
- Protein farnesyltransferase subunit beta
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein-S-isoprenylcysteine O-methyltransferase
- Protein-S-isoprenylcysteine O-methyltransferase
- Ras protein let-60
- Ubiquitin carboxyl-terminal hydrolase
Sequence:
MGAGLVSACLPISYVLLVHLFDRNGTDRNDPESVKRRFKGALLSNFVSIVVTAFYLRDYTDSPMLEMGVRWDNIGQSITYPFILMNAFYLGQFVMMQIDRTLWHYFDWYEWKLCFNSWVWRRDIIVGPITEEIVFRACSSTLMAHVYGPTMTILLNPIPFAASHFHHIWDDQRRGYSLAHSILQRGFQFCYTYLFGAFATWLQLTTRHAIVPIIAHAFCNAQGLPLWLEIPNYPKRRDRLTLYAAYSVGFAAFVHLLYTRNGMPTP
Protein: FAT atypical cadherin 1 (A0A087WPU4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESMHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDAKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNAPIWIRAF
Protein: Pseudouridine synthase 1 (F5H1S9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVAAHTCNLSTSGGQRSKRPGVRDQPGQHHGDLCLQNIKSVFVSFFQRNVGSSQFKTIEDDLVSALVRSGCIPENHGEDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILEKINSHLPSHIRILGLKRVTGGFNSKNRCDARTYCYLLPTFAFAHKDRDVQDETYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPQDPSACRYILEMYCEEPFVREGLEFAVIRVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGTEKVDVPKAPGLGLVLERVHFEKYNQRFGNDGLHEPLDWAQEEGKVAAFKEEHIYPTIIGTERDERSMAQWLSTLPIHNFSATALTAGGTGAKVPSPLEGSEGDGDTD
Protein: Probable histone-arginine methyltransferase CARMER (EC 2.1.1.319) (Coactivator arginine methyltransferase for EcR/Usp) (Protein arginine N-methyltransferase 4) (DART4) (Q9VH48)
Organism: Drosophila melanogaster (Fruit fly)
Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling. Coordinates ecdysone-mediated expression of cell death genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17459088}. Nucleus {ECO:0000269|PubMed:14705965, ECO:0000269|PubMed:17459088}.
Interaction partners:
- Polyadenylate-binding protein
- histone acetyltransferase
- Ecdysone receptor
- Taiman, isoform G
- Protein arginine N-methyltransferase 5
- Protein ultraspiracle
Sequence:
MSSLRPEEARKLATAASVSPLSNCQFCGVVISSIADEQKLEFTNKYKGSCTLLCSYDSQGVVLRVVSDDDRSHVLKEYMIAADTDAAQMGRRSYAVSLDADNLVLRFASEQDQQLFRKVVENVKHLRPKSVFSQRTEESSASQYFQFYGYLSQQQNMMQDYVRTSTYQRAILGNAVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAQYAQQLVESNNVQHKISVIPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKWLKPQGKMYPTHGDLHIAPFSDESLYSEQYNKANFWYQSAFHGVDLTTLHKEGMKEYFRQPIVDTFDIRICMAKSVRHVCDFLNDKEDDLHLISIPLEFHILQTGICHGLAFWFDVEFSGSSQNVWLSTSPTAPLTHWYQVRCLLPMPIFIKQGQTLTGRVLLEANRRQSYDVTIDLHIEGTLISSSNTLDLKNPYFRYTGAPVQAPPGTSTQSPSEQYWTQVDTQGSRNSSSMLNGGISVNGIGEGMDITHGLMHPH
Protein: Vitamin K epoxide reductase complex subunit 1-like protein 1 (VKORC1-like protein 1) (EC 1.17.4.4) (Q6TEK8)
Organism: Takifugu rubripes (Japanese pufferfish) (Fugu rubripes)
Function: Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K, and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:33154105}; Multi-pass membrane protein {ECO:0000269|PubMed:33154105}.
Interaction partners:
Sequence:
MAAPVLRVSTPRWERIARVLVCLLGILLSLYAFHVEREHARDPSYKALCDVSSSISCSKVFGSRWGRGFGLLGSIFGNDSALNQPNSVYGIVFYAFQLLLGMTVSAMAALILMTTSIMSVVGSLYLGYILYFVLKDLCVICVTTYALNFILFVLNYKRLVYLNEAWKQKLQAKQD
Protein: Inositol polyphosphate-5-phosphatase A (EC 3.1.3.56) (Type I inositol 1,4,5-trisphosphate 5-phosphatase) (5PTase) (Q29467)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Phosphatase that specifically hydrolyzes the 5-phosphate of inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate, and inositol 1,3,4,5-tetrasphosphate to inositol 1,3,4-trisphosphate. Plays a crucial role in the survival of cerebellar Purkinje cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14642}; Lipid-anchor {ECO:0000250|UniProtKB:Q14642}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TNC9}.
Interaction partners:
- Kinase
- Phosphoinositide phospholipase C.
- Kinase
- Inositol polyphosphate-5-phosphatase J.
- Inositol polyphosphate-5-phosphatase K.
- Kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Phosphoinositide phospholipase C.
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
Sequence:
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVVHTHKPHFMALHCQEFGGKNYEASMSHVDKFVKELLSSDAMKEYNRARVYLDENFKSQEHFTALGSFYFLHESLKNIYQFDFKAKKYKKVTGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFVRTRWCVADCAFDLVNIHLFHDASNLVAWETSPSVYSGIRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSKSVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVMLQLEKKLFHYFNQEVFRDNNGTALLEFDKELSVFKDRLYELDISFPPSYPYSEDSGQGRQYMNTRCPAWCDRVLMSPSARELILKSESEEKVVTYDHIGPNVCMGDHKPVFLAFRIAPGAGKPHAHVHKCCVVQ
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (P00397)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Multi-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome c oxidase subunit 5B, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFSGFTLDDTWAKAHFAIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVLIMIFMIWEAFASKREVMSVSYASTNLEWLHGCPPPYHTFEEPTYVKVK
Protein: Cell division cycle 45 (Putative cell division cyle protein 45) (Q9LSG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- Minichromosome maintenance 10
- DNA replication licensing factor MCM5
- DNA replication complex GINS protein SLD5
- DNA polymerase epsilon subunit B
- At1g19080
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM6
- Partner of SLD five 1
Sequence:
MVRIKKVESFYAKLRESATSLSSQNPLLIFPSTSDVDSLCALKVITHILESDSIQYSCFPVSSFLEIHKYAGPAGLCSTSLESPPVTILLINWGCHRDLKLVLKLGPSARVFVVDSHRPIHLHNLSDYNEQVVVLHTDDDERQGDLAYDFDVLKLANESFQLRVEDAGEESDEEEEDEEEDEEDDDDDDGDRPSKRRKMGDGVKVFKKLKRDYYKMGTFHGKPSGCLLFELSHMLRKNTNELLWLACVSLTDQFVHERLTDERYQAAVMELEQHINSSGNIDKITSVTLKDGTKVRAPDCSRISYEEEPRLMLLREWTLFDSMLCSSYIATKLKTWSDNGIKKLKLLLARMGFALIECQQKFPYMSLEVKRKMKQEFDRFLPEYGLNDFYYRSFLRLHGYSSRVSAADVVYGITALLESFLGSGGSSASKQFGEAYDALSLNNLDKLRSGMQQAIKVQRAILRQGSAAITKSGCIRSGRKFRWVKIEDSMDAKYLGYPQALTKFCYFLMDALREKGARMKPMLCACASQQPGKILVVGVCGKPRLGAVRGNAFGNAFRKAAQESRADYFHELFESSWIVLDASAVNSFMIRLTEKL
Protein: Transforming acidic coiled-coil containing protein 1 (E7ET87)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTEGSMGVTLEASAEADLKAGNSCPELVPSRRSKLRKPKPVPLRKKAIGGEFSDTNAAVEGTPLPKASYHFSPEELDENTSPLLGDARFQKSPPDLKETPGTLSSDTNDSGVELGEESRSSPLKLEFDFTEDTGNIEARKALPRKLGRKLGSTLTPKIQKDGISKSAGLEQPTDPVARDGPLSQTSSKPDPSQWESPSFNPFGSHSVLQNSPPLSSEGSYHFDPDNFDESMDPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLITGCKVKKHETQSLALDACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSAGAEVKGEPEEDLEYFECSNVPVSTINHAFSSSEAGIEKETCQKMEEDGSTVLGLLESSAEKAPVSVSCGGESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKTD
Protein: Chanoclavine-I dehydrogenase easD (ChaDH) (EC 1.1.1.332) (Ergot alkaloid synthesis protein D) (D4AK45)
Organism: Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes)
Function: Chanoclavine-I dehydrogenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine. The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae. However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet.
Interaction partners:
Sequence:
MASVSSKIFAITGGASGIGAATCRLLAKRGAATLCVGDLCSENMKQLENDIKEINPNTKVHCTVLDVSSSSNVDEWIKDIITTFGDLHGAANIAGIAQGAGLRQAPTILEEDDQQWKKVFQVNLDGVLYSTRAQVRAMKESSSTNPGDRSIVNVASIASMSHMPDVFAYGTSKAGCAYFTTCVSQDVMPFGIRANTVSPEEVEETYKKEGFSVIEADDVARTIVWLLSEDSRPVFGANINVGACMP
Protein: CDKN1A interacting zinc finger protein 1 (F7BM53)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFNPQLQQQQQLQQQQQQLQQQLQQQQLQQQQQQILQLQQLLQQSPPQASLSIPVSRGLPQQSSPQQLLSLQGLHSTSLLNGPMLQRALLLQQLQGLDQFAMPPATYDGASLTMPTATLGNLRAFNVTAPSLAAPSLTPPQMVTPNLQQFFPQATRQSLLGPPPVGVPINPSQLNHSGRNTQKQARTPSSTTPNRKDSSSQTVPLEDREDPTEGSEEATELQMDTC
Protein: HTH-type transcriptional regulator RamB (icl1 and ramB operon repressor protein) (P9WMI1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the control of the glyoxylate cycle. RamB negatively controls the expression of icl expression during growth on acetate as the sole carbon source. Does not regulate the expression of other genes involved in acetate metabolism.
Interaction partners:
- Conserved protein
- Isocitrate lyase
- 2-methylcitrate dehydratase
Sequence:
MSKTYVGSRVRQLRNERGFSQAALAQMLEISPSYLNQIEHDVRPLTVAVLLRITEVFGVDATFFASQDDTRLVAELREVTLDRDLDIAIDPHEVAEMVSAHPGLACAVVNLHRRYRITTAQLAAATEERFSDGSGRGSITMPHEEVRDYFYQRQNYLHALDTAAEDLTAQMRMHHGDLARELTRRLTEVHGVRINKRIDLGDTVLHRYDPATNTLEISSHLSPGQQVFKMAAELAYLEFGDLIDAMVTDGKFTSAESRTLARLGLANYFAAATVLPYRQFHDVAENFRYDVERLSAFYSVSYETIAHRLSTLQRPSMRGVPFTFVRVDRAGNMSKRQSATGFHFSSSGGTCPLWNVYETFANPGKILVQIAQMPDGRNYLWVARTVELRAARYGQPGKTFAIGLGCELRHAHRLVYSEGLDLSGDPNTAATPIGAGCRVCERDNCPQRAFPALGRALDLDEHRSTVSPYLVKQL
Protein: Uncharacterized protein (Q382L9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNRRVPMSIALDCEFVKTKGRVIVSSIAFVPFASFKAPLRQTHSVGHARSGTGVAKAQAHAEQSARPCMITSGGSTILSLDPTEVMRHADVLPCGHCLMPLLQGETAVGSKQSLTAVEPHPSTTGKEKLPRNYEKMLRIVRSEAGLETLCPHSIPNIRRLDKTWLRALHVAAVNSAEFRDASAHLDHLRTYGNGGRQRWAISFLMKQHPQVLQDLLRKNFTTDDAWCQWLSACGDTVESELQRVAQEHRRISSAQSERKAHSKPGDHPLDSCGVQYKECKSLEELPRELSRTWSALISARAHVGGVKFYTYGNMDAKAIKNSLQLCGATANQAAKPPEGTGKGNYHPNEEEEVGCNLLKSPHEAKVVDLTRHPLFAASGFCISSRKAPPLTDALKKAAAVDVSARLLLESNSSHDPLWDAKALACVAVACGVVPFSNPPVQ
Protein: Insulin-like growth factor 2 (Insulin-like growth factor II) (IGF-II) (Somatomedin-A) (T3M-11-derived growth factor) [Cleaved into: Insulin-like growth factor II Ala-25 Del; Preptin] (P01344)
Organism: Homo sapiens (Human)
Function: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver (Probable). Acts as a ligand for integrin which is required for IGF2 signaling. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:16040806}.
Interaction partners:
- Insulin-like growth factor-binding protein 1
- Insulin-like growth factor-binding protein 6
- Insulin-like growth factor-binding protein 2
- Cation-independent mannose-6-phosphate receptor
- Insulin-like growth factor 1 receptor
- Insulin-like growth factor-binding protein 3
- Insulin-like growth factor 1
- Insulin-like growth factor-binding protein 5
- Insulin-like growth factor 2 mRNA-binding protein 2
- Glypican-3
Sequence:
MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK
Protein: Activin receptor type-1C (EC 2.7.11.30) (Activin receptor type IC) (ACTR-IC) (Activin receptor-like kinase 7) (ALK-7) (Q8K348)
Organism: Mus musculus (Mouse)
Function: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Activin receptor type-2B
- Growth/differentiation factor 3
- Activin receptor type-1B
- Activin receptor type-2A
- Embryonic growth/differentiation factor 1
- Mothers against decapentaplegic homolog 2
- Nodal
- Mothers against decapentaplegic homolog 3
- Inhibin beta B chain
- Inhibin beta A chain
Sequence:
MTPARGSALSLALLLVALAADLAAGLKCVCLLCDSSNFTCQTEGACWASVMLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHLPTASPNAPRLGPTELTVVITVPVCLLSIAAMLTIWACQDRQCTYRKTKRHNVEEALAEYSLVNAGKTLKDLIYDATASGSGSGLPLLVQRTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMVKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCDTCAIADLGLAVKHDSIMNTIDIPQNPKVGTKRYMAPEMLDDTMNLSIFESFKRADIYSVGLVYWEIARRCSVGGVVEEYQLPYYDMVPSDPSIEEMRKVVCDQKLRPNLPNQWQSCEALRVMGRIMRECWYANGAARLTALRVKKTISQLCVKEDCKA