wanglab/gogpt-training-data huggingface dataset:
Protein: Septin (C8VB12)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Septin
- Septin B
- Septin-type G domain-containing protein
- Septin
Sequence:
MSSAYNPIKLRRKKNVKKGIQFCLMVCGASGTGRTTFVNTLCGKQVLQGKDADDATNAHLEEGVRIKPVTVELELDDEGTRISLTIVDTPGFGDQIDNEASFGEIVGYLERQYDDILAEESRIKRNPRFRDNRVHVLLYFITPTGHGLRELDIELMKRLSPRVNVIPVIGKADSLTPAELAESKKLIMEDIEHYRIPVYNFPYDIEEDDEDTVEENAELRGLMPFAIVGSDDFVEIDGRKVRARQYPWGVVEVENPRHSDFLAIRSALLHSHLADLKEITHDFLYENYRTEKLSKSVDGAATTGTDSSINPEDLATQSVRLKEEQLRREEEKLREIELKVQREIAEKRQELLARESQLREIEARMAREASQGEAAEAEQ
Protein: Cytochrome P450 11B1, mitochondrial (CYP11B1) (CYPXIB1) (Cytochrome P-450c11) (Cytochrome P450C11) (Steroid 11-beta-hydroxylase, CYP11B1) (EC 1.14.15.4) (P15538)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the biosynthesis of adrenal corticoids. Catalyzes the hydroxylation of carbon hydrogen bond at 11-beta position of 11-deoxycortisol and 11-deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or corticosterone, respectively. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 11-beta-hydroxysteroid dehydrogenase type 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Steroid 21-hydroxylase
- 17-beta-hydroxysteroid dehydrogenase type 3
- 11-beta-hydroxysteroid dehydrogenase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- Aromatase
- Aldo-keto reductase family 1 member C3
Sequence:
MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRPERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQEDIKMVYSFILRPSMFPLLTFRAIN
Protein: Outer membrane protein assembly factor BamA (Omp85) (P0A940)
Organism: Escherichia coli (strain K12)
Function: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01430, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:23882017, ECO:0000269|PubMed:24619089, ECO:0000269|PubMed:24914988, ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:9298646}.
Interaction partners:
- Outer membrane protein assembly factor BamC
- Outer membrane protein assembly factor BamD
- Outer membrane protein assembly factor BamE
- Outer membrane protein assembly factor BamB
- Chaperone SurA
- Regulator of sigma-E protease RseP
- Chaperone protein Skp
- Outer membrane lipoprotein RcsF
- LPS-assembly protein LptD
- Outer membrane protein A
Sequence:
MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYAVGINGTKNDYQTYAELSVTNPYFTVDGVSLGGRLFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNSLRAGLGYVHNSLSNMQPQVAMWRYLYSMGEHPSTSDQDNSFKTDDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVTLDTATYVPIDDDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYFPHQASNYDPDYDYECATQDGAKDLCKSDDAVGGNAMAVASLEFITPTPFISDKYANSVRTSFFWDMGTVWDTNWDSSQYSGYPDYSDPSNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW
Protein: Z band alternatively spliced PDZ-motif protein 66, isoform M (E1JI76)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSPKLHEFAVVLLRDGQATPWGIRLVGGNDLDTPLIITRVQVGSPAHGELLRGDIISKIGEYDARDLSHADAQQLFRGAGNEIRLVVHRDNKIAYTQGATQEAGPGSRSNSTLPPVTPDLMPHRGPSPFLPGPSHFERALQLPVDTLPQTVFPQLNSSGGYEVPSTVFSPKPTRDHQQDVDEEQAAIVNQPYRTTPLVLPGAKVKKDAPTTESYLRHYPNPAVRAHPGHDYHDSIMKQRVADTMLHKVVGSEADTGRVFHKQFNSPIGLYSNNNIEDTIRSTVPFATSESNRLKDSPLHRPLPTKLNGNQYQRQYPGRRTMW
Protein: SNF2 helicase, putative (EC 3.6.4.12) (C6KT82)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- RuvB-like helicase
- RuvB-like helicase
- RuvB-like helicase
- Histone H4
- Histone H2B
- Histone H2B
- PH domain-containing protein, putative
- Histone H2A
- AP2 domain transcription factor AP2-O3, putative
- Actin-like protein, putative
Sequence:
MRIRKTWCTLCRENFEEGDECIQCKQCKKKFHRECLQAEGLMDNEQLKDIKNYVCYQCINEDDDIPENEDRCKICREKSANLILLLCDGCPNSYHVSCLGLAAEPESEKWYCPICKPDDHKNLDVRRMRKGFVLDNMNGEHVNSSTCYVCQRPGKLLGCDFCPNSFHPTCLPDLDFDNISDQWECPCCKNEDPLLNQGHKRWTKNEIQEIMKKRQRELGFWRSKIIKYRNRFLLAHRKDLQPFVNPRVFSNLTKTFKNDYFHTKGSSNNKKSNKYDNDKYNSKKDVDMDSKEFNEFISSLEDEAHQNACKFIESVFLSVYYPNGRKIERRPLVDNVQLKPHQEDGVEWLLKSFLTGGAILADEMGLGKTIQTLCFLSYLKCNKIDGPHLIVVPLSTVGNWLREIHRFTPHLTCIKICGSKNERTHAKEDRLAEKGLYDLYVTTYETVKNEEEFFVETIPKWQCIVLDEAHRIKNQSGAIRHSMDRVVGNMRLLLTGTPLQNNSAELFTLINFMFPDIFKNSEIIEQAFMNASQNNKNKSNNNNNNNNKDEKNNNNDDDDDGGGGGGGANTSGNNTSKVNVNIGNIDLKSAIKEEDLKSIRCLLDKIMLRRLKEQAITLPKKIFHDVWLPLGTLSAHWYKRLLDIRSMVEEKVSVKKLLGLVIKMRIICGHPKGIVSRPSQMEKLFAFFEEESEDIKEQVKNDALKLKNISGEEHIESSSKLIFIDKLLCQLHYENCKYVKNYASSYEKHKKEVAAYNYHKIQEQTNAQKKKREHSGKFKKIEALENSPLFMEIYNKGKFDLKPTSQKEDMLKSFMHSVPVDNECPYKKKRCIYDKVKEYVKNNSNIKHKGRARLISDNNKNNKNDDNSDDEDDDEEEDEVNYYNKRKDKKKKVISDDDDDDDDDENSNDDNKSEDNNNDDNNNDDNKDITKNDNNGNFSDNNNNNNNINDDQNDDNIFSLHDSSKINNNIKEFLKSEKMEMSNNTDKINEDSTVGVTDKGDNKLDDFDMLKREEKEKNDAYMKEEGEEYDEEDVITHKNGTQLNIDNNNNNNNNINNVTDLKLQTDEKKVVINIKNEMNDNDENGEKLGEAKMHKVLIFTQFQLVLDELEEYCKYRCWKYMRLDGSTNKLIRELDIREFNLSDSIYFIYLISTRAGGLGINLTAANHVIMYDEDWNPFIDLQAIDRAHRIGQKREVNVWKLMTEWTVEERMAFRREQKLKLDKLVVQTQDDEDMLDNFEEKLSSDEIRKLMLHGKAAIQNMDVESTNNFPLEFFIERGRQKLPIINGVDLEREEKCAIEEEINKKDDGDDILVSKNDEDDDDDDDNSVDAKYNNNNDDDNAIDIDEVMMDEAEELESRNNNTNNNNNNNDGTGGSGEMINGQFSSSNNQNNNNNNNNNNDISLWRSVRERKKPQILYTPEYWGRKQEVKQIKHEYRCFICNNTKNHKAIVKDRNGNDIEIDYGDMINCFRCPKTYHKLCEGIKDENVKKTWTCSWHECCLCFRKSSQCGNLLIHCATCPTSFCYNCFPPDYVRYYVGEEYYHNLRQRGVNFTPQNWVCFLCSKCKAVEEQKKRRKMTKEERENEKQLQKELRSQLHDSKQEELEAKKRKRAQQLERDKFIIENRKRIDALDQQYEDQLRKAYENVFPNNFVKELVNRIEHAKMLKQKGIVEDNNNNNNNNKETNKKKSTTFLHTKLPSKLLVLCENCKLPCHANYKYPGKCCYPPELDKSYYMSNTSFSQMGRDGFEKRVSEGKNDSCSSHIHFKDKVGEDSNNMKNITNIVDGNKIMNSSPHKGGTKCEPNEGSTTPSRNDGIKKDLMVTSTINNNNSNNNNNSNNNNNNNNSYNFNENKENSSSTNKLMSNKGIEYNKNDDEDYNNNESKDKIMKGVGTTFLSDGSMRFEKDSPENNMNENNNMNNNNNNEKDSPQNNNDNTSKSKTRKFLRAVCSKCGTVQLGKLAHFRKHCDKLTEEEKKEYDEKREKLKELINLLNKKKIKEEHTEEEYKNMSVFKFKSLYSNYQDKADDILEDCIRSMKWDILIADKKKIIKKEKEKENKKIYSKNDDDNNNNNNNNNKKNNNITSMSLKAKLTHFLSNQPLTISSDYSDTKDIIEIRSDLTDDMKEKINDELCTISGKRKKCIVKNIKKVKKKKGNDDNDENNNNSNNNVDGDKKNNNKSNTSSKKKDDKDLKKLNLLINPFHEKLIKDTHNANFIRDSFNEDFLNKAKEFLRVTKSNLINNGNNNNNNKNKKSSSNSKNINKNSSNTKNSSNTKSSSNTKSSSNTKNKNNKNNHNNSFLESATTAEDFLRGITTGNNNIFNLVSSSNSPYDKNKKLKDDEFEKSIIQNYLNKMKNSLKNSSHLDKNTIKEKLKELNYVNSRSNSNTKNNMNTNIINNNNNNNNNQHTISAQENSLRFAKEIFKNGAFDKNGNFKLYANKGNLCNTNKDIVHLLKSNEQIENMNKNSGYSINDFNLDIFNIDKNIKCEDLEKKLLNLCASTNLMNKKNIQHDNNKKEDNKNYMLDSKNKNKQFLFKKDNTQQQEAFLSNISKAKKESSNSRKRVVEDVNVDYDIKKITNTSENSGPNKVQEYILYRRNTSSVMSNVINNNDKSKNVRNDDEDDDDDEDDDEEDDEDKNESSNYNNNKKKKTNTSSRNSSNNNSSNKNKNNKSGNDIHQASNLLYQNLLNNPQSLLQHLNLEDVKNFLKAADRSNNDNLPEIN
Protein: Alkaline ceramidase YDC1 (EC 3.5.1.-) (Acyl-CoA-independent ceramide synthase) (Q02896)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acyl-CoA-independent ceramide synthase that catalyzes the conversion of dihydroceramide and also phytoceramide to dihydrosphingosine or phytosphingosine. Prefers dihydroceramide. Very low reverse hydrolysis activity, catalyzing synthesis of dihydroceramide from fatty acid and dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide. May play a role in heat stress response.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10900202}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ceramide synthase LAG1
- Ceramide synthase LAC1
- Sphingoid long chain base kinase 4
- Sphingoid long chain base kinase 5
- Dihydrosphingosine 1-phosphate phosphatase YSR3
- Dihydrosphingosine 1-phosphate phosphatase LCB3
- Sphingolipid C4-hydroxylase SUR2
- 3-ketodihydrosphingosine reductase TSC10
- Inositol phosphosphingolipids phospholipase C
- Serine palmitoyltransferase 1
Sequence:
MLFSWPYPEAPIEGYWGKPTSLIDWCEENYVVSPYIAEWSNTITNSIFLMTAFYSTYSAWRNKLETRYILIGMGFSLVGIGSWLFHMTLQYRYQLLDELPMLYATIIPSWSIFAETQEILIKDEKKRKESSFRIQMVISFIMCGIVTILTWIYVVVQKPAIFQVLYGILTLLVVVLSGWLTYYHVHDSFAKKNLFITMVMGMIPFVIGFICWQLDIHLCSFWIYIRRTYLALPLGVLLELHAWWHLLTGTGVYIFVVYLQYLRILTHGNPNDFLFIWRWGFFPELVRKGLPIGTSYSLEYLGPIVNTQVDDETKKNN
Protein: Syntaxin-4 (Q3SWZ3)
Organism: Bos taurus (Bovine)
Function: Plasma membrane t-SNARE that mediates docking of transport vesicles (By similarity). Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane (By similarity). In neurons, recruited at neurite tips to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) which promotes neurite tip surface expression of the dopamine transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity). Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q08850}; Single-pass type IV membrane protein {ECO:0000305}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q08850}. Cell projection, stereocilium {ECO:0000250|UniProtKB:P70452}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:Q08850}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Synaptosomal-associated protein
- Vesicle-associated membrane protein 8
- Vesicle-trafficking protein SEC22b
- Vesicle-associated membrane protein 4
- Vesicle-associated membrane protein 1
- Vesicle-associated membrane protein 7
- Synaptosomal-associated protein 29
- Synaptosomal-associated protein 25
- STX6 protein
Sequence:
MRDRTHELRQGDDSSDDEDKERVALVVHPGTARLGSPDDEFFQKVRTIRQTIVKLENKVRELEKQQVTILATPLPEESMKQDLQNLRDEIKQLGRDIRAQLKAIEPQKEEADENYNSVNTRMRKTQHGVLSQQFVELINKCNLMQSEYREKNVERIRRQLKITNAGMVSDKELEQMLDSGQSEVFVSNILKDTQVTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKVALENQKKARKKKVFIAICLSITVLILVVIIVISTLV
Protein: Uncharacterized protein (C8VT43)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MSEFPSLKPAFTIQIELDAPLAVGTGVRDTNLQVIPFSKGVFKTAEGFEPAFEAQVVGTGNDYIHADPDGKHMRLNANGVIKTQDDALIYVNYTGVVTLGEAEQKVLSGTAEEGSTPFGNSFTHLTVETGHERYKDLENRVFVGKGRFNVQKGKPVVVEYRVAQVVHA
Protein: separase (EC 3.4.22.49) (Q9VRN6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein kinase polo
- Bub1-related kinase
- Serine/threonine-protein kinase PLK4
- FI11703p
- Structural maintenance of chromosomes protein
- Protein phosphatase PP2A 55 kDa regulatory subunit
- Aurora kinase B
- Precocious dissociation of sisters 5, isoform A
- Protein wings apart-like
- Cell division cycle protein 20 homolog
Sequence:
MLETGDEAEMLAGFTSSDVGPEAKEYNLLRADEEYRNGNVEHSIYYQVKAQFQSTDLRYLTESAELENQRPTAEELIKSATKLEKKDYKSKKFLQNIIKYLQQMEQEKQPKKPINEIPEYLDFLDDVQDPTEGLTRISEKCNSLPQEWCVLQLCKSFNPATTYSVFNEIIASDGAIYLTLLRHCRSSQLGPICLKISNENTANLFREYSTLVERFRRVVTVDPLNMKGKEAKQKYWEELNGFDTFQQKLLADFRDIISPYSFLFFGKRYDCTVVQKQIKATYTRVDDFCLLNQWGTHQRVLLSQAASHANRLEIADLKLICYELSSNENEIQSAYELLKGLASDWAEVEERQPLASRRFPIILVVDERLDHLHWEQLVTVQEFSRVKSLHCLWRLFQNHKSNIKHGYYTTNIKRGMCVINPDADLVNSGRRLRSFFEYWLSQWQHLFETVPNEEVMVKQALQADCFVYAGHGSGLQYVNGRIICRARVRSVVFLFGCDSTRMLGTGLYSALYGAHDYYHGALCPSIVGTLMPALDGNMDTVSVTILSRWLAPGDNKVIPWTHIDRVPWLKNGIIKGKDETTPTMNDQPNYHLGSLCSILSLVQQGKVEPNIYNCCIYVCRGLPAWNLAVEKLPL
Protein: Beta-defensin 107 (Beta-defensin 7) (BD-7) (DEFB-7) (Defensin, beta 107) (Q8IZN7)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted.
Interaction partners:
- Beta-defensin 105
- Beta-defensin 106
- Beta-defensin 104
- Beta-defensin 103
- Beta-defensin 108B
- Beta-defensin 110
- Beta-defensin 1
- Sperm associated antigen 11B
- Defensin alpha 5
- Beta-defensin 113
Sequence:
MPGAMKIFVFILAALILLAQIFQARTAIHRALISKRMEGHCEAECLTFEVKIGGCRAELAPFCCKNRKKH
Protein: Atypical chemokine receptor 1 (Duffy antigen/chemokine receptor) (CD antigen CD234) (Q9QUI6)
Organism: Mus musculus (Mouse)
Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1 and TARC. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels (By similarity).
Subcellular location: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via caveolae. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}.
Interaction partners:
- C-C motif chemokine 2
- C-C motif chemokine 5
- Growth-regulated alpha protein
- CD82 antigen
- C-X-C motif chemokine 5
- Atypical chemokine receptor 4
- Atypical chemokine receptor 2
Sequence:
MGNCLYPVETLSLDKNGTQFTFDSWNYSFEDNYSYELSSDYSLTPAAPCYSCNLLDRSSLPFFMLTSVLGMLASGSILFAILRPFFHWQICPSWPILAELAVGSALFSIAVPILAPGLHSAHSTALCNLGYWVWYTSAFAQALLIGCYACLNPRLNIGQLRGFTLGLSVGLWGAAALSGLPVALASDVYNGFCTFPSSRDMEALKYTHYAICFTIFTVLPLTLLAAKGLKIALSKGPGPWVSVLWIWFIFWWPHGMVLIFDALVRSKTVLLYTCQSQKILDAMLNVTEALSMLHCVATPLLLALFCHQTTRRSLSSLSLPTRQASQMDALAGKS
Protein: Uncharacterized protein Rv1417 (P9WLY1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase
- Riboflavin biosynthesis protein RibBA
- Probable transmembrane protein
- Putative lipoprotein LprH
- Integration host factor
- Small ribosomal subunit protein uS19
- Exported repetitive protein
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
Sequence:
MTAAPNDWDVVLRPHWTPLFAYAAAFLIAVAHVAGGLLLKVGSSGVVFQTADQVAMGALGLVLAGAVLLFARPRLRVGSAGLSVRNLLGDRIVGWSEVIGVSFPGGSRWARIDLADDEYIPVMAIQAVDKDRAVAAMDTVRSLLARYRPDLCAR
Protein: Erbb2 interacting protein (M0R9T2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Receptor tyrosine-protein kinase erbB-2
- Nucleotide-binding oligomerization domain-containing protein 2
- Plakophilin 4
- Adhesion G protein-coupled receptor L2
- ARVCF, delta catenin family member.
- Desmoglein 1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L1
Sequence:
MTQLVLEQLSGLREFWMDGNRLTFIPGFIGSLRQLTYLDVSKNNIEMVEEGISTCENLQDFLLSSNSLQQLPETIGSLKNVTTLKIDENQLMYLPDSIGGLRSIEELDCSFNEIEALPSSIGQLTNIRTFAADHNYLQQLPPEIGNWKNVTVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPALWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEESGRDLKQHEDQQVVNKDKGVKPSESITTKSKLDEREKYMNSVPKTSEPEAETNAGNSPVTTNRKSSGNMKHLVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDAKDTDSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTALCSPAKQIPIDSNSKIRQEDENFNSLLQNGVNLNNSPEEKFKINDKKDFKLPEYDLNIEEQLVLIEKDVDSKATSEDSHQLDHINMNLNKLVTNNIFQPEIMERSKMQDIVLGTGFLSIHSKSEAEHIENGNKFLNSESINKVNGLSEDTAQSPGRIEPQNTSPADVGISKSTEDLSPQRSGPAGSVVKSHSITNMETGGLKIYDILSDDGPQPPGATVKVASTMDGKNIVRSKSATLLYDQPLQVFTASSSSSELLSGTKAVFKFDSNHNPEDPDIIRASIVPGPQSIPQLYGPPQYNVQYSGSAAMKDTLWHPKQNPQIDPVSFPPQRLPRSESAENHSYTKHSANMNFSNHNNVRANTAYHLHQRLAPTRHGEMWAVSPNDRLVPAVSRTTVQRQSSVSSTASVNLGDPGPTRRTEGDYLSYRELHSMGRTPVTSGSQRPLSARAFSIDGPSTSRPQSARPSISEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPHDWREQVLRHIEAKKLEKSMLSRSFSSNLTAVSSSHYGSSRDLHGSQGSLALNVADGRGSGGHSFRHPQTSSPGDCCQDDRFMSGEQNHPLGALSHRDLRDSLMKMPLSNGQMGQPLRPQANYSQTHHPPQASVARHPSREQLIDYLMLKVAHQPPYTHPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFHNAVELIIVREVSS
Protein: 5,10-methenyltetrahydromethanopterin hydrogenase (EC 1.12.98.2) (H(2)-dependent methylene-H(4)MPT dehydrogenase) (H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase) (N(5),N(10)-methenyltetrahydromethanopterin hydrogenase) (P32440)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
Interaction partners:
- F420-dependent methylenetetrahydromethanopterin dehydrogenase
- formylmethanofuran dehydrogenase subunit B
- Probable [NiFe]-hydrogenase-type-3 Eha complex membrane subunit A
- Coenzyme F420 hydrogenase subunit alpha
- F420-non-reducing hydrogenase subunit A
- Methenyltetrahydromethanopterin cyclohydrolase
- Bifunctional enzyme Fae/Hps
- Hmd co-occurring protein HcgA
- Serine hydroxymethyltransferase
- 5,10-methylenetetrahydromethanopterin reductase
Sequence:
MKLAILGAGCYRTHAASGITNFSRACEVAEMVGKPEIAMTHSTITMGAELKELAGVDEVVVADPVFDNQFTVIDDFAYEDVIEAHKEDPEKIMPQIREKVNEVAKELPKPPEGAIHFTHPEDLGFEITTDDREAVADADFIMTWFPKGDMQPDIINKFIDDIKPGAIVTHACTIPTTKFYKIFEQKHGDLVTKPETLNVTSYHPGAVPEMKGQVYIAEGYASEDAIETLFELGQKARGNAYRLPAELLGPVCDMCSALTAITYAGILSYRDSVTQVLGAPASFAQMMAKESLEQITALMEKVGIDKMEENLDPGALLGTADSMNFGASAEILPTVFEILEKRKK
Protein: DNA terminal protein (Protein P8) (P09009)
Organism: Enterobacteria phage PRD1 (Bacteriophage PRD1)
Function: Acts as a primer for viral genomic replication. DNA terminal protein is covalently linked to the 5'-ends of both strands of the genome through a phosphodiester bond between the beta-hydroxyl group of a tyrosine residue and the 5'-phosphate of the terminal deoxyadenylate. This protein is essential for DNA replication and is involved in the priming of DNA elongation (By similarity).
Subcellular location: Virion. Host nucleus {ECO:0000269|PubMed:23091024}.
Interaction partners:
Sequence:
MAKKKPVEKNGLVYKEFQKQVSNLKKAGLIPKTLDVRKVKPTKHYKGLVSKYKDVATGGAKLAAIPNPAVIETLEARGESIIKKGGKAYLKARQQINQRGQIVNPFTVRVTKRGEVVRRYRKTTPEGKPVYITQRELPIKFENMEQWLTELKAAGFQLQPGEQIYFTFNGNYSRRTYTSFDEAFNKFMTYDIIIDAVAGKLKVEDEADLVKSVGFQRISGPEAKAYNRNRIVLPEMQFSQAAKKKYKRRQKRGYGSKGV
Protein: Centromere protein S (CENP-S) (Apoptosis-inducing TAF9-like domain-containing protein 1) (FANCM-associated histone fold protein 1) (FANCM-interacting histone fold protein 1) (Fanconi anemia-associated polypeptide of 16 kDa) (Q8N2Z9)
Organism: Homo sapiens (Human)
Function: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own.
Subcellular location: Nucleus {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:24522885}. Chromosome, centromere {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:24522885}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19620631}. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX (PubMed:19620631, PubMed:24522885). During S phase, rapidly recruited to DNA interstrand cross-links that block replication (PubMed:20347428). Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes (PubMed:24522885). {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:24522885}.
Interaction partners:
- Fanconi anemia group E protein
- Centromere protein T
- Fanconi anemia group F protein
- Centromere protein C
- Centromere protein X
- Fanconi anemia core complex-associated protein 24
- Fanconi anemia group B protein
- Fanconi anemia group M protein
- Fanconi anemia group C protein
- E3 ubiquitin-protein ligase FANCL
Sequence:
MEEEAETEEQQRFSYQQRLKAAVHYTVGCLCEEVALDKEMQFSKQTIAAISELTFRQCENFAKDLEMFARHAKRTTINTEDVKLLARRSNSLLKYITDKSEEIAQINLERKAQKKKKSEDGSKNSRQPAEAGVVESEN
Protein: Interferon regulatory factor 3 (M0R3C2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTV