wanglab/gogpt-training-data huggingface dataset:
Protein: Porphobilinogen deaminase (PBG-D) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase) (P08397)
Organism: Homo sapiens (Human)
Function: As part of the heme biosynthetic pathway, catalyzes the sequential polymerization of four molecules of porphobilinogen to form hydroxymethylbilane, also known as preuroporphyrinogen. Catalysis begins with the assembly of the dipyrromethane cofactor by the apoenzyme from two molecules of porphobilinogen or from preuroporphyrinogen. The covalently linked cofactor acts as a primer, around which the tetrapyrrole product is assembled. In the last step of catalysis, the product, preuroporphyrinogen, is released, leaving the cofactor bound to the holodeaminase intact.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22907}.
Interaction partners:
- Uroporphyrinogen-III synthase
- Delta-aminolevulinic acid dehydratase
- Uroporphyrinogen decarboxylase
- Ferrochelatase, mitochondrial
- Protoporphyrinogen oxidase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- 5-aminolevulinate synthase, non-specific, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- T-cell surface glycoprotein CD3 gamma chain
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDAH
Protein: Spi-1 proto-oncogene b (Transcription factor PU.1b isoform 2) (F1R668)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MLHPYRMEGYIIPPQQTEEMFETEIYRPPMEYQYIIDDSQNDHSWDYNTHHIHPVDFENLPESHFTELQSVQSLHAASVHRFPDVESSHFMDPGLGSHHIPLTNPQMTYLPRTSVCYPHNVQPSPLQRSSDEEDPSSRSPPLEVSDEECMRDHISSTTGGEHGNKKKIRLYQFLLDLLRNGDMKDSIWWVDREKGTFQFSSKHKEVLANRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKIKKKLTYQFSGEVLGKSHTDRKHYM
Protein: Signal recognition particle receptor subunit alpha homolog (DP-alpha) (Docking protein alpha) (SR-alpha) (GTP-binding protein) (Q9U5L1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the SRP (signal recognition particle) receptor (By similarity). Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SRP subunit Srp54 (By similarity). SRP receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER (By similarity). May have a role in axonogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32916}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32916}; Cytoplasmic side {ECO:0000250|UniProtKB:P32916}. Note=Thought to be anchored in the membrane through an interaction with SrpRbeta, which contains a bona fide transmembrane domain. {ECO:0000250|UniProtKB:P32916}.
Interaction partners:
- Signal recognition particle receptor subunit beta
- Signal recognition particle 54 kDa protein
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP68
- DSec61alpha
- Signal recognition particle 19 kDa protein
- FI01658p
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein bL33m
Sequence:
MLDFVVIFTKGGVVLWHSNASGNSFASCINSLIRGVILEERNTEAKYYEEDHLAVQFKLDNELDLVYAAIFQKVIKLNYLDGFLADMQAAFKEKYGDIRLGDDYDFDREYRRVLSAAEEASAKQVKAPKTMRSYNESQKSKKTVASMIQDDKKPVEKRVNIQEAPPPSKSQPSSPPTGSPMDKIIMEKRRKLREKLTPTKKTSPSDSKSSKPEKAGKKPRVWDLGGNSKDAALLDRSRDSPDDVQYQNINSELVGTMQGVIRDLDVESEDEADNEDASSEGEAEEQVQSKKGKRGGLLSYFKGIVGAKTMSLADLQPALEKMRDHLISKNVASEIAAKLCDSVAASLDGKQMGTFDSIASQVKEALTESLVRILSPKRRIDIIRDALESKRNGRPYTIIFCGVNGVGKSTNLAKICFWLIENDFNVLIAACDTFRAGAVEQLRTHTRHLNALHPAAKHDGRNMVQLYEKGYGKDAAGIAMEAIKFAHDTRVDVVLVDTAGRMQDNEPLMRSLSKLIKVNNPDLVLFVGEALVGNEAVDQLVKFNQSLADYSSNENPHIIDGIVLTKFDTIDDKVGAAISMTYITGQPIVFVGTGQTYADLKAINVNAVVNSLMK
Protein: ABC transporter B family member 4 (ABC transporter ABCB.4) (AtABCB4) (Multidrug resistance protein 4) (P-glycoprotein 4) (O80725)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin influx transporter that mediates the transport of auxin in roots. Contributes to the basipetal transport in hypocotyls and root tips by establishing an auxin uptake sink in the root cap. Confers sensitivity to 1-N-naphthylphthalamic acid (NPA). Regulates the root elongation, the initiation of lateral roots and the development of root hairs. Can transport IAA, indole-3-propionic acid, NPA syringic acid, vanillic acid and some auxin metabolites, but not 2,4-D and 1-naphthaleneacetic acid.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16243904}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:16243904}. Note=Non-polar distribution in apical cells. Apical (bottom) localization in mature root cells. Basal (top) localization in the root elongation zone.
Interaction partners:
- Auxin efflux carrier component 3
- Auxin efflux carrier component 2
- Peptidyl-prolyl cis-trans isomerase FKBP42
- Auxin transporter protein 1
- Auxin efflux carrier component 4
- Auxin efflux carrier component 7
- Auxin efflux carrier component 8
- Auxin efflux carrier component 5
- Auxin efflux carrier component 6
- Auxin efflux carrier component 1
Sequence:
MASESGLNGDPNILEEVSETKRDKEEEEEVKKTEKKDEEHEKTKTVPFYKLFAFADSFDFLLMILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDIDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETIERRPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIRLQEEKKSDENAAEEQKMSSIESFKQSSLRKSSLGRSLSKGGSSRGNSSRHSFNMFGFPAGIDGNVVQDQEEDDTTQPKTEPKKVSIFRIAALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEPENSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASIFAIMDRESKIDPSVESGRVLDNVKGDIELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKDGVYASLVQLHLTAAS
Protein: Uncharacterized protein, isoform M (L0MLJ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDSTLNIEEKEIATKNETQIDYADEIKTTPQDNDNLNEKLLVSYIDSGFDKPVTSRDNKDDDDLKIEESESEDCNSEKKNTTDLEVNPAALIDKPSLDISSSDMERTVEIEDSESNNPIIIDASIKTDPLISVENLSTVSENNFELDLIDGSTNGENSSNAENESPVQDTSNILIKGEDDKAIENCKSQDTTKSSSEKNVNDPTSIASDLSAENTKADLVSLNEPNVNDQTSSASDLTAENTKADHDSLNKPKDFNNQILNIISDIDINIKAQEKITQLKEQELKLIQKQNDLANEIHKQQILAKQLSAQNQLKQNECQSGELDLHSQYQNERGGPTSTLYQEKNIASKESANVSKTVDLRKIFTPATDAAEILPKNRKLYASSAFYSPTLHPTVEDQVELARRISHSLSDISNQTSKGQSMYVNRKKRSDKWVHEGGSQENSETKSTMEVAKLEKIPLKLIMNPNGKVRDYNSLKDLINVEAGLLSPDNCAELITALQLHQGRDFQQYQQRPVLSPNILPAYSDAGKHRVQLNIHQNQLIEKYSKPGLQVVQSPWKAALQTGSASSAFLEDTKSFSPPALTPIPSSQAGSKDWTDANEPMPHGSSRRNTNAVASSPRSVIVPSNPQRDLAYTPCVAQGWGGRSVELPKGLYVPKEISLSSYAAPSQQCEIHSKHFERPYEDTFPRTFPRNNYSANNNFPGNDGIGEFPLSKPTGLTTGTLHQQPYSPTSYKKTVPGLEKVENFARYEQPDRKRLTSGSPQYLNALQNSQVRNASPIPFGTSLNEQTSWPPRSVLLQGGSPSPLPNHVQTFNKCAKGWGSIPVKQQSYSSQYNLPGNLPYSDF
Protein: Uncharacterized protein (A0A0H3MHH0)
Organism: Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)
Interaction partners:
Sequence:
MYFTRDPVIETVITSREGYKLSIRNSKHLSQDPFVVEAIEVVRLGGTSFFRNCDHSKPFLLPASDYEVMEIRDAKINLKAVGLDRGVKIVGSREALLKMPKVAPIVSVSEDNTIVSEEEVVADSTVAAPASTPVAPMSKKERRKEFKNEKWKDKKKQGRRRNSKEIADAVGSSQEMIDTVAEECLQESSSEEGDFSERRFSLIPPPTRLISDGPEEPEEESQPVTSVDLNESLNALVSESCNVIESILADEDTVVFTKEKDQTAEESQEQPSLSLEETPVHDSISSEE
Protein: Bifunctional IPC transferase and DIPP synthase [Includes: 1L-myo-inositol-1-phosphate cytidylyltransferase (IPCT) (EC 2.7.7.74); CDP-L-myo-inositol myo-inositolphosphotransferase (DIPP synthase) (EC 2.7.8.34) (Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase)] (O67379)
Organism: Aquifex aeolicus (strain VF5)
Function: Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Myo-inositol-1-phosphate synthase GAPDH-like domain-containing protein
- Fructose-1,6-bisphosphatase/inositol-1-monophosphatase
- Glycerol-3-phosphate cytidyltransferase
- Flagellar hook-associated protein 1
- Putative thiamine-phosphate synthase 2
- Apolipoprotein N-acyltransferase
Sequence:
MVETAVILAGGEGNRLKPLTEEVPKALLKVAGRELLYRTIKQLQDVGVKNFVIVVNKKFEGKVKAFLKEHNFEAEVIPNEHPEKENGYSLYLAKGRIKGEFAVVMSDHIYEKAFLEKAVEGKGLIVDRLGLYINKNEATKVKCEEGRIKYIGKNLEKYDGFDTGFFVLDESIFEVAEEALKEQKKLTMSELAKRAQIPCTEVSGYFWMDVDTPEDVEKAKKYLVKTAIKGVGDGFISRNLNRKVSTRISPYLVDKFTPNQLTVLTFLLGMFSALVAYFSPALGGILLQINSMLDGLDGEVARAQMRTTKFGAWLDSVLDRYVDFAFLSALAMHLKPSWDFMPWVFAALFGSVMVSYSTERYKGAYCEDAYAVIKELRYLLGKRDERIFMIMIFTILGWIKALFVVLAIITNLRVILTIYLVWKKKGNV
Protein: SUN domain-containing protein 1 (AtSUN1) (Q9FF75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Required for the maintenance and/or formation of polarized nuclear shape in root hairs. Modulates the anchoring and mobility of WIP proteins and RANGAP1 in the nuclear envelope (NE). In association with SUN2, may be involved in telomere attachment to nuclear envelope in the prophase of meiosis. As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:19807882, ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21294795}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21294795}; Single-pass type II membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:22270916}. Note=Dynamic localization during mitosis and meosis, tightly coupled with nuclear envelope (NE) dynamics. Localized with the nuclear envelope during meiotic prophase I. NE re-formation during metaphase is temporally and spatially coordinated with plant-specific microtubule structures such as phragmoplasts. During anaphase, after NE breakdown (NEBD), predominantly localized with the endoplasmic reticulum, in the outside of the segregated chromosomes and not in between segregated chromosomes. {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:25412930}.
Interaction partners:
- Protein CROWDED NUCLEI 1
- Zinc finger protein WIP3
- SUN domain-containing protein 4
- SUN domain-containing protein 3
- WPP domain-interacting tail-anchored protein 1
- SUN domain-containing protein 5
- TIR domain-containing protein
- Protein CROWDED NUCLEI 2
- Protein SINE1
- Protein KAKU4
Sequence:
MSASTVSITANTAAATRRTPILAGEKKSNFDYPQSESLANGGVGEAGGTSRDLSRGEATLDRSQGQDLGPVTRRSVSAATGTNTTATQRRTRKVATPKSEKARWKTVVRIFAKQLGALLIIVGLIQLTRKMILKASSPSSPISSYETEMAFSGLESRIAEVDGLVKATTNSMQVQVELLDKKMEREAKVLRQEIERKASAFQSELKKIESRTESLEKSVDEVNAKPWVTKDELERIYEELKKGNVDDSAFSEISIDELRAYARDIMEKEIEKHAADGLGRVDYALASGGAFVMEHSDPYLVGKGSSWFATTMRRAHTNAVKMLSPSFGEPGQCFPLKGSEGYVQIRLRGPIIPEAFTLEHVAKSVAYDRSSAPKDCRVSGSLQGPESSAETENMQLLTEFTYDLDRSNAQTFNILESSSSGLIDTVRLDFTSNHGSDSHTCIYRFRVHGRAPDPVPVVGTNLDQDSSPESE
Protein: Chitinase-like protein Idgf2 (Imaginal disk growth factor protein 2) (Q9V3D4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cooperates with insulin-like peptides to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex.
Subcellular location: Secreted {ECO:0000269|PubMed:9847235}. Note=Secreted in hemolymph. It is probably transported to target tissues via hemolymph.
Interaction partners:
Sequence:
MKAWIWFTFVACLFAASTEAASNLVCYYDSSSYTREGLGKLLNPDLEIALQFCSHLVYGYAGLRGENLQAYSMNENLDIYKHQFSEVTSLKRKYPHLKVLLSVGGDHDIDPDHPNKYIDLLEGEKVRQIGFIRSAYDLVKTYGFDGLDLAYQFPKNKPRKVHGDLGLAWKSIKKLFTGDFIVDPHAALHKEQFTALVRDVKDSLRADGFLLSLTVLPNVNSTWYFDIPALNGLVDFVNLATFDFLTPARNPEEADYSAPIYHPDGSKDRLAHLNADFQVEYWLSQGFPSNKINLGVATYGNAWKLTKDSGLEGVPVVPETSGPAPEGFQSQKPGLLSYAEICGKLSNPQNQFLKGNESPLRRVSDPTKRFGGIAYRPVDGQITEGIWVSYDDPDSASNKAAYARVKNLGGVALFDLSYDDFRGQCSGDKYPILRAIKYRL
Protein: Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase) ((1->3)-beta-glucanase) (CaLam) (Endo-beta-1,3-glucanase) (Laminarinase) (C1IE32)
Organism: Cryptopygus antarcticus (Antarctic springtail)
Function: Hydrolyzes laminarin majorily to glucose (G1), laminaribiose (L2), laminaritriose (L3), laminaritetraose (L4) and laminaripentaose (L5). Hydrolyzes laminarioligosaccharides L3, L4, L5 and laminarihexaose (L6) to G1, L2 and L3. Hardly hydrolyzes L2. Does not hydrolyze lichenan, pustulan, carboxymethyl cellulose, locust bean gum or soluble starch.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MNAFTFPLLLAFCAFAHGAWVLDWEDEFNGGNLADRWNFELGCNGWGNNELQCYTDNRGANARQEDGKLVISAVREWWGDGVNPDKEFTSARMTTKANWLHGKFEMRARLPKGKHLWPAFWMMPQNSEYGGWPRSGEIDITEYRGQRPQQILGTLHFGAAPDNKGDVGTGERDFPIDFSADFHTFGLDWSPDSMQWLLDDQVYHTESLQRNFWDGVYNQNGSPFDKNFFIILNLAVGGNFFGGEPFDPSESDGWAKNTFEVEYVKKWTWN
Protein: Uncharacterized protein C26F1.11 (Q10497)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MIIITAKENVPTNQKLDTCKNQSTVHQKVNKSLGNSNKVLRSNAVQSDKANREPRRITKSVKKKENNTISAVKKVITTESRIEGESKNGNSRKNTRKFENIKKTP
Protein: Ring finger protein 38 (A0A8I5ZJ72)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVPRGRKRLDSASVGTRVPRARTIGDGGPGELAAGRASSHNRRRRPGPERWEQPRRAEPPLAGTGGDGRWLPREGGTGRGRLGAGGQRTADVSRQPGALCSRGSGEPARPCLDETQSEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPNQHHFSGERCNTPARNRRSPPVRRQRGRRERLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGIPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLLHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLQVGSFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRSRYRSQQPVPPPTYHPSLLPYVLSMLPVPPTVGPTFSFELDVEDGEVENYEALLNLAERLGEAKPRGLTKADIEQLPSYRFNPSNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKGNRTCPICRADASEVHRDSE
Protein: C-C chemokine receptor type 4 (C-C CKR-4) (CC-CKR-4) (CCR-4) (CCR4) (K5-5) (CD antigen CD194) (P51679)
Organism: Homo sapiens (Human)
Function: High affinity receptor for the C-C type chemokines CCL17/TARC, CCL22/MDC and CKLF isoform 1/CKLF1. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Can function as a chemoattractant homing receptor on circulating memory lymphocytes and as a coreceptor for some primary HIV-2 isolates. In the CNS, could mediate hippocampal-neuron survival.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-C motif chemokine 22
- C-C motif chemokine 17
- C-C motif chemokine 5
- C-C motif chemokine 2
- Guanine nucleotide-binding protein G
- C-C motif chemokine 27
- Stromal cell-derived factor 1
- C-C motif chemokine 3
- Beta-adrenergic receptor kinase 1
- G protein-coupled receptor kinase 3
Sequence:
MNPTDIADTTLDESIYSNYYLYESIPKPCTKEGIKAFGELFLPPLYSLVFVFGLLGNSVVVLVLFKYKRLRSMTDVYLLNLAISDLLFVFSLPFWGYYAADQWVFGLGLCKMISWMYLVGFYSGIFFVMLMSIDRYLAIVHAVFSLRARTLTYGVITSLATWSVAVFASLPGFLFSTCYTERNHTYCKTKYSLNSTTWKVLSSLEINILGLVIPLGIMLFCYSMIIRTLQHCKNEKKNKAVKMIFAVVVLFLGFWTPYNIVLFLETLVELEVLQDCTFERYLDYAIQATETLAFVHCCLNPIIYFFLGEKFRKYILQLFKTCRGLFVLCQYCGLLQIYSADTPSSSYTQSTMDHDLHDAL
Protein: Adenylosuccinate lyase (A0A8I6AM95)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAASGDPACAESYRSPLAARYASHEMCFLFSDRYKFQTWRQLWLWLAEAEQTLGLPITDEQIQEMRSNLSNIDFQMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKACSADHGWETLLPLDSRSLHGSSELEACPR
Protein: Myosin heavy chain 95F (95F MHC) (Protein jaguar) (Q01989)
Organism: Drosophila melanogaster (Fruit fly)
Function: Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Together CLIP-190 and jar may coordinate the interaction between the actin and microtubule cytoskeleton. May link endocytic vesicles to microtubules and may be involved in transport in the early embryo and in the dynamic process of dorsal closure. It is believed that its function changes during the life cycle.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9472041}. Note=Microtubule-associated.
Interaction partners:
- Calmodulin-related protein 97A
- GH21964p
- Calmodulin
- Protein disabled
- Yuri gagarin, isoform B
- GH05942p
- AT09290p
- PFTAIRE-interacting factor 1A, isoform H
- Eukaryotic translation initiation factor 3 subunit M
- Dynamin
Sequence:
MLEDTQLVWVRDAAEGYIQGRITEIGAKEFEVTPTDRKYPKRTCHFDDIHSSCDGPQDHDDNCELMLLNEATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGESGAGKTESTKYLLKYLCYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQYFANAKTEQLIPGSQKSKNHQQKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSGLLGVDQTELRTALVSRVMQSKGGGFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHKSWANHYRLGLPRSSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPSGSSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFRPGKFVEFDRIMRSDPENMLAIVAKVKKWLIRSRWVKSALGALCVIKLRNRIIYRNKCVLIAQRIARGFLARKQHRPRYQGIGKINKIRTNTLKTIEIASGLKMGREEIISGVNDIYRQIDDAIKKIKMNPRITQREMDSMYTVVMANMNKLTVDLNTKLKEQQQAEEQERLRKIQEALEAERAAKEAEEQRQREEIENKRLKAEMETRRKAAEAQRLRQEEEDRRAALALQEQLEKEAKDDAKYRQQLEQERRDHELALRLANESNGQVEDSPPVIRNGVNDASPMGPNKLIRSENVRAQQQALGKQKYDLSKWKYSELRDAINTSCDIELLEACRQEFHRRLKVYHAWKAKNRKRTTMDENERAPRSVMEAAFKQPPLVQPIQEIVTAQHRYFRIPFMRANAPDNTKRGLWYAHFDGQWIARQMELHADKPPILLVAGTDDMQMCELSLEETGLTRKRGAEILEHEFNREWERNGGKAYKNLGAAKPNGPAAAMQKQQ
Protein: Large ribosomal subunit protein eL19x (60S ribosomal protein L19-1) (Protein EMBRYO DEFECTIVE 2386) (Q9SRX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL3z
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL30y
- Large ribosomal subunit protein uL1y
- Small ribosomal subunit protein eS6y
- Large ribosomal subunit protein uL6z/uL6y
Sequence:
MVSLKLQKRLAASVMKCGKGKVWLDPNESSDISMANSRQNIRKLVKDGFIIRKPTKIHSRSRARKMKIAKMKGRHSGYGKRKGTREARLPTKVLWMRRMRVLRRLLKKYRETKKIDKHMYHDMYMRVKGNVFKNKRVLMESIHKSKAEKAREKTLSDQFEAKRAKNKASRERKHARREERLAKGPGGDVAPVAAPAPAATPAPTAAVPKKKSKK
Protein: Apical sushi protein (Q8I1W9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIIYHILIFLLHYNIIIKAKENKNDNFLNGIYKLQNIWRNTTLGELDLKKANIENAEGIIEKFNDSNKTDFNQHPHFRSKLSFLEHKNHKDMGIVTNHQNKDHKKNEYTSEEIIDMKPQLASQEMWRKGENFYMHGATNTNEQNDDEDLFESFHKNHNSNIKINSPCFDLQDKEMCSNNKECFYDDAYKACFQNCALVNEKKCSLYSECKHTPNGCQNEGYLNIQVFGSNLGGDVRACELFESEGSCYLMEKLFKKLSEEKKETSFNCVWISYKHELRSYDDENEPKENNDNIVALENKNKYMYMNNVESIHNNHHLENPYHEDIKHNKHKSFNYHVLSSSVPRQIAKNEKFLSLLQLNLKGKKKEKNKKKKKDDEDDDDIDEEDDDLDIEGKNNEFNADEEENSKDLKNNNIDDNEEDGTTDEDDLFNNKKKKKNNNNNNSNNNNNKNKNKQNTNKKNNKIINEFDDDIDEVSEENLLNDEEKKQNKIKNKNINETNNISENNEIEISSKDLTEQYEDKYNYDKKNNMGTNNNFNNTNTFANNKNNLHNKYINHASHTQNEKDILKHNFYGKDNNGTYEIIKVETHICANLNEKPNPSTLLEGALIAENEAQLQKIKKKYKVTDNEICVRPTNSSYVSLIPDKKYYLLGEKIEFKCQEGYKIIGTTNIGVCTGRNIISPNITCESLTNFDDVEKDNIQKMNNIINSASKYTFYNIIIIVFIIINLFFCA
Protein: Heme oxygenase 2 (F4IUM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
MASLLRPTPLLSTPRKLTHSHLHTSISFPFQISTQRKPQKHLLNLCRSTPTPSQQKASQRKRTRYRKQYPGENIGITEEMRFVAMRLRNVNGKKLDLSEDKTDTEKEEEEEEEDDDDDDEVKEETWKPSKEGFLKYLVDSKLVFDTIERIVDESENVSYAYFRRTGLERCESIEKDLQWLREQDLVIPEPSNVGVSYAKYLEEQAGESAPLFLSHFYSIYFSHIAGGQVLVRQESSIYREFCWFLVYFSHIAGGQVICKTASLIELEIDIDIVDSGELGLSGVLRLWWVSEKLLEGKELEFNRWEGDAQDLLKGVREKLNVLGEHWSRDEKNKCLKETAKAFKYMGQIVRLIIL
Protein: NACHT, LRR and PYD domains-containing protein 5 (Mater protein homolog) (Q647I9)
Organism: Bos taurus (Bovine)
Function: As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for the formation of F-actin cytoplasmic lattices (CPL) in oocytes, which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity). Required for the localization of cortical granules to the cortex of oocytes, via association with the cortical actin scaffold (By similarity). Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Involved in regulating post-fertilization Ca(2+) release and endoplasmic reticulum (ER) storage via regulation of ER cellular localization (By similarity). May be involved in the localization of mitochondria to the cytoplasm and perinuclear region in oocytes and early stage embryos, independent of its role in CPL formation (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:P59047}. Mitochondrion {ECO:0000250|UniProtKB:Q9R1M5}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9R1M5}. Cytoplasm {ECO:0000250|UniProtKB:Q9R1M5}. Golgi apparatus {ECO:0000250|UniProtKB:P59047}.
Interaction partners:
- Oocyte-expressed protein homolog
- Transducin-like enhancer protein 6
- Zona pellucida sperm-binding protein 4
- Peptidyl arginine deiminase 6
- Growth/differentiation factor 9
- Zona pellucida sperm-binding protein 2
- Zygote arrest 1
- Bone morphogenetic protein 15
- Neurofilament light polypeptide
Sequence:
MREAKIAPLSNYGLQWCFEQLGKEEFQTFKALLKEHASESAACSFPLVQVDRADAESLASLLHEHCRASLAWKTSTDIFEKMSLSALSEMARDEMKKYLLAEISEDSAPTKTDQGPSMKEVPGPREDPQDSRDYRIHVMTTFSTRLDTPQRFEEFASECPDAHALSGAFNPDPSGGFRPLTVVLHGPPGVGKSSLARRLLLFWAQGDLYKGLFSYVFLLRARDLQGSRETSFAELISKEWPDAPVPVEKVLSQPERLLIVVDGLEELELTFRDQDSSLLADWAERQPAPVLAHSLLKKVLLPECALLLTVQDAGLQRLQALLRSPRYLWVGGLSVENRMQLLLGGGKHCRRKTCAWHAGADHQEVLDKCQVPVVCALVREALELQGEPGKGLPVPGHTLTGLYATFVFQRLAPKDAGWRALSGEERGALKGLCRLAADGVWNAKFVFDGDDLGVHGLQGPELSALQQASILLPDGHCGRGHAFSHLSLQEFFAALFYVLRGVEGDGEGYPLFPQSTKSLTELRHIDLNVQLVQMKRFLFGLVSKEVMRALETLLGCPVRPVAKQQLLHWICLVGQHPAAAASPDLLEAFYCLFEAQDDEFVRLALNGFQEVWLQLNRPMDLTVSSFCLRRCQHLRKVRLDVRGTPKDEFAEAWSGAPQGLKIKTLDEHWEDLCSVLSTHPNLRQLDLSGSVLSKEAMKTLCVKLRQPACKIQNLIFKGARVTPGLRHLWMTLIINRNITRLDLTGCRLREEDVQTACEALRHPQCALESLRLDRCGLTPASCREISQVLATSGSLKSLSLTGNKVADQGVKSLCDALKVTPCTLQKLILGSCGLTAATCQDLASALIENQGLTHLSLSGDELGSKGMSLLCRAVKLSSCGLQKLALNACSLDVAGCGFLAFALMGNRHLTHLSLSMNPLEDPGMNLLCEVMMEPSCPLRDLDLVNCRLTASCCKSLSNVITRSPRLRSLDLAANALGDEGIAALCEGLKQKNTLTRLGLEACGLTSEGCKALSAALTCSRHLASLNLMRNDLGPRGMTTLCSAFMHPTSNLQTIGLWKEQYPARVRRLLEQVQRLKPHVVISDAWYTEEEEDGPCWRI