wanglab/gogpt-training-data huggingface dataset:
Protein: Phenylalanine--tRNA ligase (EC 6.1.1.20) (Q8I5A1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- phenylalanine--tRNA ligase
- phenylalanine--tRNA ligase
Sequence:
MFFSFFVCFIFVIIEFIESYKKNPQISDIYFRKLNKNYHIKDDIINYNRFKYVYKIKNHPLNEIKEEVLNFLKKKTSFYLVYNKCPLYYKNLCFKEILIRDTNETTSIKNNFYFSHDYLYIPQATSLFPYIYDLLKNNNKQNIQKCNDTIYVRNNPYSENTPNNNIDVNNNIEKKQDNYINKEIVENNNVHIINNSNILNKQRDNFCIISNIFRKDNIDKLHFPFFNQMDIYFKITNELVHKKKQLVYFLCELLSNIFGPNYKWRIRKDSFDFTTHSLQAEVFHNNKWIEILGSGILKSKIIFNKKKKYEINDYLAVGIGLDRIAMIKWDIDRIRDLYLYIYNTEKNIYSVEQHNEKDKCSQHISNDIFNKNINEYINHNDSYNHNNVKNYFLKNKKNENQNDKHQDENILLSSPKLEGQKLRHNLLTHIKQKMHIQQKQKIINMPHEEVLYFSNLYNIKDEQRDLSFYSNEQWNNDDFIKNIMELKNIKNLHFLKTVYLFDIFLNEQSKKTSYAYKFIYTPTTNIKEQHVFKNHVKELHEQIITQITKMYNIIIR
Protein: Leukemia inhibitory factor (LIF) (Differentiation-stimulating factor) (D factor) (Melanoma-derived LPL inhibitor) (MLPLI) (Emfilermin) (P15018)
Organism: Homo sapiens (Human)
Function: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-6 receptor subunit beta
- Leukemia inhibitory factor receptor
- Oncostatin-M
- Ciliary neurotrophic factor
- Ciliary neurotrophic factor receptor subunit alpha
- Oncostatin-M-specific receptor subunit beta
- Interleukin-11
- Interleukin-6
- Signal transducer and activator of transcription 3
- Cardiotrophin-1
Sequence:
MKVLAAGVVPLLLVLHWKHGAGSPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLCGPNVTDFPPFHANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGHVDVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAF
Protein: Bis(5'-adenosyl)-triphosphatase ENPP4 (EC 3.6.1.29) (AP3A hydrolase) (AP3Aase) (Ectonucleotide pyrophosphatase/phosphodiesterase family member 4) (E-NPP 4) (NPP-4) (Q9Y6X5)
Organism: Homo sapiens (Human)
Function: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22995898}; Single-pass type I membrane protein {ECO:0000269|PubMed:22995898}.
Interaction partners:
- Bis
Sequence:
MKLLVILLFSGLITGFRSDSSSSLPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSDSNDKDPFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISSYFMNYNSSVSFEERLNNITMWLNNSNPPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDSCIDHSYYTLIDLSPVAAILPKINRTEVYNKLKNCSPHMNVYLKEDIPNRFYYQHNDRIQPIILVADEGWTIVLNESSQKLGDHGYDNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILGLKPHPNNGTFGHTKCLLVDQWCINLPEAIAIVIGSLLVLTMLTCLIIIMQNRLSVPRPFSRLQLQEDDDDPLIG
Protein: Proprotein convertase subtilisin/kexin type 6 (E9Q4D0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPPRAPPAPGPRPPPRAADVARGAGAAGRHGLPPLALRPWRWLLLLALPAACSALPPPRPVYTNHWAVQVLGGPGAADRVAAAHGYLNLGQIGNLDDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKRQARSDSLYFNDPIWSNMWYMHCTDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGPGRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEECASTLATTYSSGAFYERKIVTTDLRQRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHLKASDWKVNGAGHKVSHLYGFGLVDAEALVLEARKWTAVPSQHVCVATADKRPRSIPIVQVLRTTALTNACADHSDQRVVYLEHVVVRISISHPRRGDLQIHLISPSGTKSQLLAKRLLDFSNEGFTNWEFMTVHCWGEKAEGEWTLEVQDIPSQVRNPEKQGKLKEWSLILYGTAEHPYRTFSSHQSRSRMLELSVPEQEPPKAAGQPPQAETPEDEEEYTGVCHPECGDKGCDGPNADQCLNCVHFSLGNSKTNRKCVSECPLGYFGDAAARRCRRCHKGCETCTGRSPAQCLSCRRGFYHHQETNTCVTLCPAGLYADESQRLCLRCHPSCQKCVDEPEKCTVCKEGFSLARGSCIPDCEPGTYFDSELVKCGECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFYPEEMPGLPHKVCRRCEENCLSCEGSSRNCSRCKAGFTQLGTSCITNHTCSNADETFCEMVKSNRLCERKLFIQFCCRTCLLAG
Protein: DNA polymerase beta (EC 2.7.7.7) (5'-deoxyribose-phosphate lyase) (5'-dRP lyase) (EC 4.2.99.-) (AP lyase) (EC 4.2.99.18) (P06766)
Organism: Rattus norvegicus (Rat)
Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}.
Interaction partners:
- DNA repair protein XRCC1
- Bifunctional polynucleotide phosphatase/kinase
- Flap endonuclease 1
- DNA repair nuclease/redox regulator APEX1
- Nei endonuclease VIII-like 1
- Poly
- Poly [ADP-ribose] polymerase 1
- DNA ligase 1
- Ubiquitin carboxyl-terminal hydrolase 47
- Endonuclease 8-like 2 lyase Neil2)
Sequence:
MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYREPKDRSE
Protein: Elongation factor Tu, mitochondrial (EC 3.6.5.3) (P85834)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy. Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P49411}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL21m
- Elongation factor Ts, mitochondrial
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL33m
- Mitochondrial ribosomal protein L20
Sequence:
MAAATLLRATPRFSGLCASPTPFLQGRLRPLKAPASPFLCRGLAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDVPAMTEEDKNIKWS
Protein: Splicing factor proline/glutamine rich (Polypyrimidine tract binding protein associated) (Q6NUU2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MGMRGGMGMGMGMGMGMGMGMGMGMGNPNFRNQNQHHFQNRGPQMGGGFRQNQGNQGNQVSTQQKPQEPAQNKPVVQTPPAQGPGQAQQAANKGPTPQQTPTVAPPKIQSAPPKIQSPPPKIQSPPPAQNNAKTPEIASPQNQQRKNLPKPAMGNGQKPPAPLKQEQTPAPTPPPAQQQQQQQQQQKQTPANEQSSQPQELKATLSLLRKPGEKTYTQRCRLFIGNLPNDITEPEFRKLFAKYGEPSEIFINQGKGFGFIRLESRALAEVAKAELDDTPMKGRPLRVRFATHSAALSVRNLSPFVSNELLEEAFSQFGLVERAIVIVDDRGRSTGKGIVEFSSKPAARKAMDRISDGVFLLTSSPRPIVVELLEQYDDEDGLPEKLAQKNPSYQKEREQPPRFARPGTFEYEYSQRWKSLDEMEKQQRQQVEKNICEAREKLETEMDDAYHEHQANMLRQDLLRRQEELRRMEELHSQEMQKRKEMQLRQEEERRRREEEMMRQREIEEQLRRKREESYRMNNFMDNRDREMRMNTSGGMGLSDMSFGSPNQKFSLTGMSFDGHQGLSGSTQGGLASNEMRNDRFQQGGSGGQRGIGAGNSGFGRVREEFDGPAKKPRF
Protein: Predicted iron-dependent peroxidase (Q8NPY9)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- Uncharacterized BCR
- Uncharacterized protein, homolog of Cu resistance protein CopC
- Uncharacterized iron-regulated membrane protein
Sequence:
MVSRRGFLGGAGLIAGASALAGCSAGENEPDGASISLKGQVVEFDGRHQAGIATPHQANLNLVAFTLRAGVDRAGVTRLMRVWTEDARALCAGETPLGSLEPEMVTSPANLTITCGFGASLFDVTQQVDLRPEWLKPIPEFERDQLRPEWGEADLVLQICSDDPVTLSHATRHMIRSGVDYAATRWVQQGFMNAHGVNETDETPRNLFGQKDGTVNPRTDDEIQQTAWISEGPDWAIDGSCMVVRRIAMNLDEWEILDRPSREVSVGRTLDTGAPLSGGDEFSEADYSARDSYGLPLIDPASHMARSRAPESNPEQVILRRVFNYDLPPDPTSEELSNAGLVFICFQKNPDLQFTPIQQRLDEQDRLNQWITHIGSAVFFIPPGTDPNDSSRDDFWGAGLLL
Protein: Protein-arginine deiminase type-2 (EC 3.5.3.15) (Zgc:66317) (Q6PFK7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVSRRSLTIDTEKATKTTYVLGTTLTVNLIRCAPPQSKSFSIRCTPNVHYKITPPITDKNALPYPLGPNTILLITMDTVSETAFDSKLSVRYYGEKTETLGDAILHLTAVEISLDVDADRDGVVEKNNPNKASWKWGPNGHGAILLVNCDSESINNKKPDNENSDIGKVSDLKDMSKMVLRTNGPSQLPEGYKLSMHISQSTSESVRVFRPRTNTKTENLWKYQLLKLFLKDFLMVVGTDTLTQEVPYLGGSSELEFHVEGLRFPDKDFDGLVTINLSLLEPCGKGFPETPIFTDKVVFRVSPWIMTPNTLKPVEVYVCSTEDNYSFLKSIRNLVEKSGYKLKICHEYMNRGDRWMQDFPYDALLGPDFGYVTRNALNEEVSSLDSFGNLEVSPPVTVNGKNYPLGRIIIGVAFPTARKGRNMTKVVQDFLWAQKVQEPIALYSDWLFVGHVDEFMSFVPAPDRKKFRLLLASPDAGYKVFKSLQNSGLGKAEMFPGKEEAISVNDLLSDKKLQAENRYVQNCIDWNRDVLKKELGLDDEDIIDLPILFKVMEEKNEDSVPRAVAYYPDMVNMIVLGDQLGVPKPFGPQVKGVCALEKEMCSLLEPLGLKCTFIDDFAPYHKLLGEVHCGSNVLREPFTVRWWNLEL
Protein: Retinal guanylyl cyclase 2 (RETGC-2) (EC 4.6.1.2) (Guanylate cyclase 2F, retinal) (Guanylate cyclase F) (GC-F) (Rod outer segment membrane guanylate cyclase 2) (ROS-GC2) (P51842)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors. Plays an essential role in phototransduction, by mediating cGMP replenishment. May also participate in the trafficking of membrane-asociated proteins to the photoreceptor outer segment membrane (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:7831337}; Single-pass type I membrane protein. Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:O02740}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Guanylyl cyclase-activating protein 1
- Guanylyl cyclase-activating protein 2
- Retinal guanylyl cyclase 1
- Guanylate cyclase 2D
- Inosine triphosphate pyrophosphatase
- Phosphodiesterase
- Phosphodiesterase
- Phosphodiesterase
- cGMP-dependent 3',5'-cyclic phosphodiesterase
- cGMP-specific 3',5'-cyclic phosphodiesterase
Sequence:
MFLGPWPFSRLLSWFAISSRLSGQHGLTSSKFLRYLCLLALLPLIWWGQALPYKIGVIGPWTCDPFFSKALPEVAAALAIERISRDMSFDRSYSFEYVILNEDCQTSKALTSFISHQQMASGFVGPANPGYCEAASLLGNSWDKGIFSWACVNHELDNKHSYPTFSRTLPSPIRVLVTVMKYFQWAHAGVISSDEDIWVHTANQVSSALRSHGLPVGVVLTSGQDSRSIQKALQQIRQADRIRIIIMCMHSALIGGETQTHFLELAHDLKMTDGTYVFVPYDVLLYSLPYKHSPYQVLRNNQKLREAYDAVLTITVESHEKTFYEAFTEAAAGGEIPEKLDSHQVSPLFGTIYNSIYFIAQAMSNALKENGQASAASLTRHSRNMQFYGFNQLIRTDSNGNGISEYVILDTNGKEWELRGTYTVDMETELLRFRGTPIHFPGGRPTSADAKCWFAQGKICQGGIDPALAMMVCFALLLALLSINGFAYFIRRRINKIQLIKGPNRILLTLEDVTFINPHFGSKRGSRASVSFQIISEVQSGRSPRLSFSSGSLTPATYENSNIAIYQGDWVWLKKFPPGDFGDIKSIKSSASDVFEMMKDLRHENVNPLLGFFYDSGMFAIVSEFCSRRSLEDILTQDDVKLDWMFKSSLLLDLIKGMKYLHHREFIHGRLKSRNCVVDGRFVLKVTDYGFNNILEMLRLSEEEPSEEELLWTAPELLRAPGGIRLGSFAGDVYSFAIIMQEVMVRGAPFCMMDLSAKEVIDRLKMPPPVYRPVVSPEFAPPECLQLMKQCWAEAAEQRPTFDEIFNQFKTFNKGKKTNIIDSMLRMLEQYSSNLEDLIRERTEELEIEKQKTEKLLTQMLPPSVAESLKKGCTVEPEGFDLVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPKRNGSRHAAEIANMSLDILSSVGTFKMRHMPEVPVRIRIGLHTGPVVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVSLSTVTILRTLSEGYEVELRGRTELKGKGTEETFWLVGKKGFTKPLPVPPPVGKDGQVGHGLQPAEIAAFQRRKAERQLVRNKP
Protein: Nuclear hormone receptor family member nhr-80 (Q8ITW8)
Organism: Caenorhabditis elegans
Function: Transcription factor. Binds to regulatory elements and regulates transcription of target genes, including acyltransferase dgat-2. As part of a lysosome-to-nucleus retrograde lipid signaling pathway, acts as a direct nuclear receptor of oleoylethanolamide (OEA) and, acting in concert with nuclear hormone receptor nhr-49, activates the transcription of genes promoting longevity and mitochondrial beta-oxidation. Required to modulate expression of delta-9 fatty acid desaturases, thereby regulating lipid metabolism; in some contexts, acting in concert with nhr-49. Involved in modulation of lipid metabolism in response to the citrate-induced mitochondrial unfolded protein response (mtUPR), acting downstream of transcription factor dve-1 and ubiquitin-like protein 5. Plays a role in modulating mitochondrial morphology and function. Involved in positively modulating life-span in a germline-dependent manner, acting in concert with nuclear hormone receptor daf-12. Plays a role in transgenerational lipid accumulation in response to a high-fat diet.
Subcellular location: Nucleus {ECO:0000255|RuleBase:RU004334, ECO:0000269|PubMed:21423649, ECO:0000269|PubMed:35021096}.
Interaction partners:
- Delta
- Lipase lipl-4
- Nuclear hormone receptor family member nhr-49
- Delta
- Delta
- WW domain-containing protein
- Mediator of RNA polymerase II transcription subunit 15
- Fatty acid-binding protein homolog 8
- Sterol regulatory element binding protein sbp-1
- Forkhead box protein O
Sequence:
MTAEGRYLEIRKKTVKSKFRFPASSSSTRCLICSAQATGFHFEAQSCSACAAFFRRTVALTKSFKCITGRDDCNVHYSMHQICRSCRHKKCLSNGMKPGGVQPKKPNIETGRAFFTKSGLKRNKKFANVSPQTADEQKLVVEGVKVPKIEVQEPNSLEDLEQDNEFVIKTPTPRKISSSTSFSASTTTNYSTPGPSPMAPCSAGPDVLTLFIREEMKLGERRRLLFSERAVGTLLGQNKHCPYKKEDIKPLVFHDFRLTIKTHIMLVYEWLQTWPELQELDDFDRMSLLRKAVLIHFLLDPSFLSYQIGEPDKLIMQNGGFISTADHHGVGWEDETDISGENKRKYYVPIMKQITDEIMPAMEAMKITFEEFVALKALACFQGGFENVSEAKRHLITQQVNRIMTSLHTHYLENSEEKIAERFGTIVLMLSNIFTAGNDFVQNHREIDIFHIWDLDKLVLQLLNLDKIMETEARETAEKRAMRNGINVVNNNNDVLLGQAKLEK
Protein: Caprin-1 (Cytoplasmic activation- and proliferation-associated protein 1) (GPI-anchored protein p137) (GPI-p137) (p137GPI) (RNA granule protein 105) (Q5M9G3)
Organism: Rattus norvegicus (Rat)
Function: May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types. Binds directly and selectively to MYC and CCND2 RNAs. In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q14444}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14444}. Cell projection, dendrite {ECO:0000269|PubMed:15858068, ECO:0000269|PubMed:20516077}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14444}. Note=Mediates formation and localizes to cytoplasmic ribonucleoprotein membraneless compartments. Associated with RNA granules. At the leading edge of migrating fibroblasts, colocalizes with DDX3X. {ECO:0000250|UniProtKB:Q14444}.
Interaction partners:
- Ras GTPase-activating protein-binding protein 1
- NTF2 domain-containing protein
- Ras GTPase-activating protein-binding protein 2
- Fragile X messenger ribonucleoprotein 1
- Cytotoxic granule associated RNA binding protein TIA1
- Ubiquitin carboxyl-terminal hydrolase 10
- Fxr2 protein
- RNA-binding protein FXR1
- Transitional endoplasmic reticulum ATPase
Sequence:
MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDDVRTDLKQGLSGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKALKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPIVEDQVAEAEPEPTEEYTEQSEVESTEYVNRQFMAETQFSSGEKEQVDEWAVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQSDPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPQVHSESRLAQSNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHAAEQRPQKEPIDQIQATISLNTEQTTASSSLPAASQPQVFQAGASKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQSQYQASYNQSFSSQPHQVEQTELQQDQLQTVVGTYHGSQDQPHQVPGNHQQPPQQSTGFPRSSQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRSSFSNTPNSGYTQSQFNAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN
Protein: Cone-rod homeobox (Q9WTQ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Photoreceptor-specific nuclear receptor
- Rhodopsin
- Neural retina-specific leucine zipper protein
- Recoverin
- Rod outer segment membrane protein 1
- Aryl-hydrocarbon-interacting protein-like 1
- Short-wave-sensitive opsin 1
- Medium-wave-sensitive opsin 1
- Neurogenic differentiation factor 1
- Retinal guanylyl cyclase 1
Sequence:
MMTYMNPGPHYSVNALALSGPSVDLMHQAVPYSSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGVQAKARPAKRKAGTSPRPSTDVCTDPLGISDSYSPSLPGPSGSPTTAVATVSIWSPASESPLPEAQRAGLVASGSSLTSAPYAMTYAPASAFCSSPSAYASPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYSTYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
Protein: DNA cross-link repair 1A protein (Beta-lactamase MBLAC2) (EC 3.5.2.6) (SNM1 homolog A) (Q9JIC3)
Organism: Mus musculus (Mouse)
Function: May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons.
Subcellular location: Nucleus {ECO:0000250}. Note=In some cells it may be found in typically 1 or 2 discrete nuclear aggregates of unknown function which also contain TP53BP1. Also found in multiple discrete nuclear foci which increase in number following treatment with ionizing radiation or interstrand cross-linking agents. These foci overlap with those formed by the MRN complex (composed of MRE11, RAD50 and NBN) and BRCA1 (By similarity). {ECO:0000250}.
Interaction partners:
- Fanconi anemia group D2 protein homolog
- Fanconi anemia group M protein homolog
- Structure-specific endonuclease subunit MUS81
- Fanconi anemia group I protein homolog
- Fanconi-associated nuclease 1
- Structure-specific endonuclease subunit SLX1
- Structure-specific endonuclease subunit SLX4
- DNA excision repair protein ERCC-1
- Fanconi anemia group A protein homolog
- Fanconi anemia core complex-associated protein 24
Sequence:
MLEDTWEEEIWEYKSKRKPKPVHPNNCSENISESVEKSTDGKHQSKGNEKRTSENPGKTKDHKVCLAETDSQISAGSSQSSSCRDESQQSQNKETTPKKQHRTRRGKQVTPKVRPVYDGYCPSCQMPFSSLLGQTPQWHVFECLDSPPISDTECPEGLLCTSTIPSHYKKYTHILLAQSRDSKEPLGSPSDALAGLFAAAAPGSPCNLEERRSMTLKTENLRKVSDHSLLMMQYLETSQPSAEINRKNVSSPCSQTSPVPQCAEFVKRDQLVGGGSPLAEVALNSQSKSGSMGLPLPENDTDSCEISYSPLHSDEETYDIDQELDDSQQELFFTQSSKDSSLEEDGSAIFENLHGPSPKEAEGIRPTAKSLVAQARCSAPSEGSTLSDSFLLLSYTSNRLSQEDLPHTDAAFHLLSPALAVGGAASNYQTSKAKLDEPEKFLSLASSHQQQKIETSAVGNQTSLPLLTRARSKPLEKEGGKCLPLHPTQSQTRGSPRKGLGAPGANCACRNAQKRSSMPLDKPLGTSPSSPKCSPSQPSKKVMKQMDIGVFFGLPPKRQETSLRESASEGPNVSPVVSPNQKRPRLCKRKAQSSLSDLEFDAKNLNESQHSVGLSGEKRQHRRKRHKTSNSPREGPCQRRSGHLMNNPELGPVSLSKAFVRRTRGRTQRGNMNISESSGAGEVRRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTRPVYCSEITGNLLKKKLRVQEQYIRQLPMDTECVVDSVKVVLLDANHCPGATMILFQLPNGAVILHTGDFRADPSMERSRLAGRKVHTLFLDTTYCSPEYTFPSQQEVIQFAINTAFEAVTLNPRALVVCGTYCIGKEKVFLAIADVLGSKVGMSQEKYKTLQCLNIPEVSSLITTDMCDSLVHLLPMMQINFKGLQSHLKKCGGKYDQILAFRPTGWTHSNNITSTADIIPQTRGNISIYGIPYSEHSSYLEMKRFVQWLKPQKIIPTVNVGSFRSRNTMEKYFKEWRLEAGY
Protein: Collagen alpha-1(II) chain (Alpha-1 type II collagen) (P02460)
Organism: Gallus gallus (Chicken)
Function: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Aggrecan core protein
- Link domain-containing protein.
- Integrin beta-1
- Transcription factor SOX-9
- Runt-related transcription factor
- ZnMc domain-containing protein.
- Indian hedgehog protein
- Transcription factor LSox5-II
- SRY-box 6
Sequence:
LQGLPGKDGETGAAGPLDPGPVGERGEQGAPGPSGFQGLPGPPGPPGESGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGATGPAGPNGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGARGLTGPIGPPGPAGPNGEKGESGPPGPSGAAGARGAPGERGEPGAPGPAGFAGPPGADGQPGAKGEQGEPGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGPNGNPGPPGPPGSAGKDGPKGVRGDAGPPGRAGDPGLQGPAGPPGEKGEPGEDGPAGPDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGSAGDRGPPGPVGPPGLTGPAGEPGREGNPGADGPPGRDGAAGVKGDRGETGPVGAPGAPGAPGAPGPVGPTGKQGDRGETGAQGPMGPSGPAGARGMPGPQGPRGDKGETGEAGERGLKGHRGFTGLQGLPGPPGPSGDQGAAGPAGPSGPRGPPGPVGPSGKDGSNGMPGPIGPPGPRGRSGEPGPAGPPGNPGPPGPPGPPGTGIDMSAFAGLGQTEKGPDPIRYMRADEAAGGLRQHDVEVDATLKSLNNQIESIRSPEGSKKNPARTCRDIKLCHPEWKSGDYWIDPNQGCTLDAIKVFCNMETGETCVYPTPSSIPRKNWWTSKTKDKKHVWFAETINGGFHFSYGDENLSPNTASIQMTFLRLLSTEGSQNVTYHCKNSIAYMDEETGNLKKAILIQGSNDVEIRAEGNSRFTYSVLEDGCTKHTGKWGKTVIEYRSQKTSRLPIVDIAPMDIGGADQEFGVDIGPVCFL
Protein: Contig An13c0040, genomic contig (EC 5.1.2.2) (A2R1E3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MGSTGQFPRIKEIRTFIIDGVGSGGDYHNVKGGHWLIDSNISTPMTRWAQYRGSRTSWGINVLGSFCVEIEATDGTKGFATGFGGPPACWLVHQHFERFLLGADPRDTNDLFEKMYRGSMFYGRKGLPVAVISVIDLAIWDLLGKIRNEPVYKLIGGATRSRLDFYCTGPQPASAKAMGFSGAKVALPHGPDEGTEGLLKNVDYLRKQRESVGPNFPLRVDCYMSLNVPYTIELVKRCEAEGINIDWWEECLTPDDFDGHALLKRAHPTVKFTTGEHEYSRYGFRKLVEGRNLDILQPDVMWVGGMTELLKVSALASAYDLPVVPHASGPYSYHFVVSQPNTPFQEYLANSADGHTVEPVFGNLFLNEPIPTKGYLDVSILDKPGFGLELNPAASLIPAASILTPAPQKALVAPTENQQEST
Protein: Slr1940 protein (P74500)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Slr0929 protein
Sequence:
MPQFPMGFCIVRRINLRFASILALAIPLNLVASSLTAAPLTNGECLLLAQASQRRNVGSIGAPGARGVDGQDGANTDDLTVFSDGSPMTLNLAGRDGAPGTPGAEGSPANCPALDTSQRQDVQMANGSDGGDGGDGGNGGNGGSITIYTRNLDSLNQIFVGAAGGKGGAPGMGGGGGQACQCSQPYWTVESCSGRPGDSGYRCSTEEFRCFNGLNGRDGRSGIAGQDGLTGRLTVLNLDRPLEPDRPGTTVSLDVLKNQGFNLSKNIWETRPGAAQLLAPGSVIADEYLILLDRIERSFLVVWNAPQPFERFANTNVSLTLTEDNQIAPELPSNLWLEGTTQQRNNVTEFVVYNAMWEGDATSLGRLTLSGSGNNLKLSLVDEANQSNLMATKFRLRYRVTNEDPRFRPPSTYTLRYEGEIEDSLVTVNGNQFTIDIGQLPIPPKDLESGTGVEIELVAERTFSGNTAEQKLIIRDLIRGRN
Protein: Packaging efficiency factor P6 (P27379)
Organism: Enterobacteria phage PRD1 (Bacteriophage PRD1)
Function: Together with the packaging ATPase P9, forms the external part of the portal vertex that is embeded in the capsid and which plays critical roles in genome packaging and genome ejection. Both proteins multimerize as a single ring-shaped heterdodecamer arranged around a central channel.
Subcellular location: Virion {ECO:0000305}. Note=Localizes at the unique vertex of the capsid, which extends to the internal membrane via two small integral membrane proteins, P20 and P22. Packaging efficiency factor P6 attaches to the virion via these proteins and is, in turn, necessary for the attachment of DNA packaging protein P9 to the capsid. {ECO:0000269|PubMed:12743288}.
Interaction partners:
Sequence:
MDTEEIKEEMQEAAEAAIENAVETAELETAAIKAEGAAAAAEQSAEQAAVMAATLAASVEANAAQQIAEHSEQVQTQEEKISWLENQVMAMASNLQMMQEAVTALTVSQSLTPEPSPVPAVEVEAMPEAVTVEILPESAGDQQEAEPVPSVGDQQETAPRKRFRAI