wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar transporter chaperone complex subunit 1 (Negative regulator of cdc42) (SPX-dependent polyphosphate polymerase VTC subunit 1) (Vacuolar membrane polyphosphate polymerase accessory subunit 1) (PolyP polymerase) (Q9UR17)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. Vtc1 contributes only 3 transmembrane domains to the complex. The VTC complex also plays a role in vacuolar membrane fusion (By similarity). Involved in the control of cell polarity.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:10628977, ECO:0000269|PubMed:11042180}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vacuolar transporter chaperone complex subunit 2
- Vacuolar transporter chaperone complex subunit 4
- Probable electron transfer flavoprotein subunit beta
- Cell division control protein 42 homolog
- T-complex protein 1 subunit gamma
- Probable T-complex protein 1 subunit eta
- Probable T-complex protein 1 subunit beta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit alpha
Sequence:
MSTQPLLQTTPGKRIALPVRVEPKVFFANERTFLSWLSFAVVLGGLSVGLLNFGDRIGKISAGLFTIVAIGTMGYALGIYHWRASAIRRRGSGPYDDRLGPTILCFVLLAAIITNFVLRMLF
Protein: HTH crp-type domain-containing protein (O57938)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MTRERVELTNRQIELLRKLYREGKTIEVHTVEKTQDELAQELGITRQALSNHLKILKELGYIRTGRGFIDLTDKALELLGEKRGDVFIFVKIEPTKRKQVYDTIRKLRVKKIYRVTGDIDLIIEADKSKLDEILEEIAALDGVKETITHVVLGVL
Protein: Serine/threonine-protein kinase Nek9 (EC 2.7.11.1) (Nercc1 kinase) (Never in mitosis A-related kinase 9) (NimA-related protein kinase 9) (NimA-related kinase 8) (Nek8) (Q8TD19)
Organism: Homo sapiens (Human)
Function: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14660563}. Nucleus {ECO:0000269|PubMed:14660563}.
Interaction partners:
- Serine/threonine-protein kinase Nek7
- Ankyrin repeat and SAM domain-containing protein 6
- Serine/threonine-protein kinase Nek6
- Nephrocystin-3
- Inversin
- Protein bicaudal D homolog 2
- Serine/threonine-protein kinase PLK1
- Dynein light chain 1, cytoplasmic
- Echinoderm microtubule-associated protein-like 4
- Ankyrin repeat and SAM domain-containing protein 3
Sequence:
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVFQSSSPGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAMGNSNGASSSCPGWLRKELENAEFIPMPDSPSPLSAAFSESEKDTLPYEELQGLKVASEAPLEHKPQVEASSPRLNPAVTCAGKGTPLTPPACACSSLQVEVERLQGLVLKCLAEQQKLQQENLQIFTQLQKLNKKLEGGQQVGMHSKGTQTAKEEMEMDPKPDLDSDSWCLLGTDSCRPSL
Protein: AUGMIN subunit 5 (Q9FMB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in microtubules reorganization during spindle and phragmoplast development.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22505726}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:22505726}. Note=Preferentially localizes to microtubules minus ends. {ECO:0000269|PubMed:22505726}.
Interaction partners:
- AUGMIN subunit 2
- AUGMIN subunit 3
- AUGMIN subunit 4
- AUGMIN subunit 7
- AUGMIN subunit 6
- Coiled-coil domain-containing protein SCD2
- AUGMIN subunit 1
- AUGMIN subunit 8
- Anaphase-promoting complex subunit 5
Sequence:
MQSLSSSAPTPEAILEWLQKEMGYRQLGPYNGSSKSHVPSIDAIRKICRGNMIPIWNFLINRVKSEKTVERIRRNITVHGGSSNASIGSSVNPGKEESKSKGRRKDKTVTGESSSYAEDREAALQERELAAKEVERLRNIVRRQRKDLKARMLEVSREEAERKRMLDERANYRHKQALLEAYDQQCDEATRIFAEYHKRLQVYVNQANDAQRSVNSSNEVLSSLSANSEREAVYSTVKGTKSADDVILMETTRERNIRIVCDLLASRMIERIRNSFPAYEGNGICSLPELETAKLGFEYDGEITDEMKTVIVNSLRGPPLLLQAIAAYTLRIKTLISREMEKIDVRADAEMLRYKFENNRVTDNSSSDVSSPLSYQFNGNGKIGTDTHFQGSNNQLLERQKAHVQQFLATEDALNKAAEARDLCHKFINRLHGSADTATHSFVGGTTQSGSNLRQFELDVWGKEREAAGLRASLNTLLSEIQRLNKLCAERKEAEDSLKKKWKKIEEFDARRSELETIYTTLLKANMDAVAFWNQQPLAAREYASATVIPASEVVVDISNSAKDFIEKEVSAFFQSPDNSLYMLPATPQGLLESMGANGSTGPEAVAYAEKNAALLTARAGARDPSAIPSICRISAALQYPAGLEGSDASLASVLESLEFCLRVRGSEACVLEDLAKAIDLVHIRQDLVESGHSLLDHAFRAQQKYERTTNYCLDLASEQENTISDQWLPELRTAVQNAQASSEHCKYVRGLLDEWWEQPASTVVDWVTVDGQSVAAWQNHVKQLLAFYDKESLRT
Protein: Nucleolar protein 16 (HBV pre-S2 trans-regulated protein 3) (Q9Y3C1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
Interaction partners:
- 60S ribosome subunit biogenesis protein NIP7 homolog
- mRNA turnover protein 4 homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex subunit 2
- U3 small nucleolar ribonucleoprotein protein IMP4
- Ribosome biogenesis protein WDR12
Sequence:
MPKAKGKTRRQKFGYSVNRKRLNRNARRKAAPRIECSHIRHAWDHAKSVRQNLAEMGLAVDPNRAVPLRKRKVKAMEVDIEERPKELVRKPYVLNDLEAEASLPEKKGNTLSRDLIDYVRYMVENHGEDYKAMARDEKNYYQDTPKQIRSKINVYKRFYPAEWQDFLDSLQKRKMEVE
Protein: Putative U-box domain-containing protein 46 (EC 2.3.2.27) (Plant U-box protein 46) (RING-type E3 ubiquitin transferase PUB46) (Q3E9F7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as an E3 ubiquitin ligase.
Interaction partners:
- Putative U-box domain-containing protein 42
- Ferrochelatase-2, chloroplastic
Sequence:
MADSTETNADTLRRELQKVLTEILNDGGGNDRDETEAFSGVVKAIDEAVRILTCLRKVESKIPESDISPVEVPKEFICTLSNTIMIEPVIIASGQTYEKRYITEWLKHERTCPKTKQVLSHRLWIPNHLISDLITQWCLVNKYDHQKPSDELVAELFTSDIEALLQRVSSSSSVADQIEAAKELRHQTKKFPNVRVFFVAGIHDSITRLLSPLSTLDEAVDSSLELQENIVTALFNLSILESNKTVIAENCLVIPLLTKSLKQGTDETRRNAAATLSSLSAIDSNKIIIGNSEAVKALIDLIEEGDLLATKEATSTVFNLCIVLENKGKVVSAGLIHAATKKIKAGSNVDELLSLLALISTHNRAVEEMDKLGFIYDLFSILRKPSSLLTGENAVVIVFNMYDRNRDRSRLKVVGEEENQHGTFTKLAKQGSVRAARKAQGILQWIKRFVTGKEPQRA
Protein: Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D (Soluble scavenger protein with 5 SRCR domains) (SSc5D) (A1L4H1)
Organism: Homo sapiens (Human)
Function: Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced cytokine release. Does not possess intrinsic bactericidal activity. May play a role in the innate defense and homeostasis of certain epithelial surfaces (By similarity).
Subcellular location: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MRVLACLLAALVGIQAVERLRLADGPHGCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRQLGCGGALAAPGGAFFGEGAGPVWLSELACRGNEGQLGLCHHRGWKAHICSHEEDAGVVCAGQRVANSRDDSTSPLDGAPWPGLLLELSPSTEEPLVTHAPRPAGNPQNASRKKSPRPKQAKSTRAPLLTTGAPRQERLRLVSGPHRCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRELGCGGALAAPGGARFGPGAGPVWMDDVGCGGGEQALRDCPRSPWGRSNCDHSEDAGLVCTGPAPRLRLADGPHGCAGRLEVWHGGRWGSVCDDAWDLRDAAVACRELGCGGALAAPGGAFFGEGSGPIILDDLRCRGNETALRFCPARPWGQHDCHHREDAGAVCDGMPLGYVPPTAPTDSNNSTPREAASRPPSTMTSQAPGTAGVSPPPASPTVLWEPGPEAGSPQLRLVAGPSKCSGRLEVWHDQRWGTVCDDSWDMRDSAVVCRELGCGGPQQPDPAAGRFGWGAGPIWLDDVGCVGTEASLSDCPAAPWGKHNCAHNEDVGVTCTGPPGLDSISDPFSWSWIPGLGRDRDAWLPGELATKPSASVTASVLEKTTTKAPGKMPKSTKKWVTKNAKRPTTQPPVMPTTKHSRAQSPPDLTSQTTAALTTEASRRPTSEFTRRPTTEAPQRWTSHTTATLTPQAPRERTTKTMAMLTTQGPQEMTSESTIKSIPQASLEPSAEIPEGSPESPKDPAPSPSVSTTGESGLFRVRLADGPNRCAGRLEVWHAGRWGTVCDDNWDLRDATVACWELGCGKVRPRVGKTHYGPGTGPIWLDDMGCKGSEASLSDCPSGAWGKHNCDHEEDVGLTCTGYTDYDDYPPWTWDPTSREDLAKGTTTAGVPGHTLPWRTTRRPGSSSPAIRRLPDTGSKDGYKLPWTWDTPSGRGLAEGTPTAGKLGPTLGAGTTRSPGSPPTLRVHGDTGSPRKPWPERRPPRPAATRTAPPTPSPGPSASPGPPGPALTSDSSRELTPHSALTSEATSDAPDTSPPTPDPASRTNPDLILTSPDFALSTPDSSVVPALTPEPSPTPLPTLPKELTSDPSTPSEVTSLSPTSEQVPESDTTPDLDTTPYSSTVSEYSRSPDPSPSPHPTTTPDPTMAPDPITTLNPTVTPHFPTTPHPTTTPHPTTITHSTMIPDPTTTPQPFTTITHSTMIPDPTTTPQPFTTMQPTTTPHSTTPHPTTTPHPTTITHSTMIPDPTTTPQPFTTMQPTTMPHPTTTPHPTTTPHPTTTPHPTTTPHPTMTPDPTTTPYPTTTPDPTTTPHPTTPDPSSTPVITTVSLPTSLGTELSSPTLAPTVKPSLHPQLTFTAPAPHTSTSQIPTLEPSPALESSPSRSSTATSMDPLSTEDFKPPRSQSPNLTPPPTHTPHSASDLTVSPDPLLSPTAHPLDHPPLDPLTLGPTPGQSPGPHGPCVAPTPPVRVMACEPPALVELVAAVRDVGGQLQRLTQVVEQERQERQALLLGLTQLVEAARGLGQLGEAVKRLAEMAWTTSMPAPTTTTPEEEERPLRGDV
Protein: Gibberellin 3-beta-dioxygenase 4 (EC 1.14.11.15) (GA 3-oxidase 4) (AtGA3ox4) (Gibberellin 3 beta-hydroxylase 4) (Q9C971)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts the inactive gibberellin (GA) precursors GA9 and GA20 in the bioactives gibberellins GA4 and GA1. Involved in the production of bioactive GA for reproductive development.
Interaction partners:
- Gibberellin 20 oxidase 3
- Gibberellin 20 oxidase 1
- Gibberellin 20 oxidase 4
- Gibberellin 20 oxidase 2
- Gibberellin 2-beta-dioxygenase 6
- Gibberellin 2-beta-dioxygenase 4
- Gibberellin 2-beta-dioxygenase 3
- Gibberellin 2-beta-dioxygenase 2
- Gibberellin 2-beta-dioxygenase 1
- Gibberellin 2-beta-dioxygenase 7
Sequence:
MPSLAEEICIGNLGSLQTLPESFTWKLTAADSLLRPSSAVSFDAVEESIPVIDLSNPDVTTLIGDASKTWGAFQIANHGISQKLLDDIESLSKTLFDMPSERKLEAASSDKGVSGYGEPRISPFFEKKMWSEGFTIADDSYRNHFNTLWPHDHTKYCGIIQEYVDEMEKLASRLLYCILGSLGVTVEDIEWAHKLEKSGSKVGRGAIRLNHYPVCPEPERAMGLAAHTDSTILTILHQSNTGGLQVFREESGWVTVEPAPGVLVVNIGDLFHILSNGKIPSVVHRAKVNHTRSRISIAYLWGGPAGDVQIAPISKLTGPAEPSLYRSITWKEYLQIKYEVFDKAMDAIRVVNPTN
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q49IK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EHEAKLQRLREELSRPVIEAHHHQSHHQKQAQHRQHHQSHHRKKHRRQQQHHRRRGQSTTQYVNHSPPGFNQSQQAQQQSVLEMDLLKAETSKDEEPLRHRVARAVTAKKERIWDYGVIPYEIDGNFSGIHKALFKLAMRHWENSTCIKFVERDPEIHPNYIVFTVRSCGCCSFVGKRGNGPQAISIGRNCDKFGIVVHELGHVVGFWHEHTRPDREKHVVIEHNNIMKGQDYNFNMLSPDEVDSLGMAYDYDSIMHYARNTFSKGTYLDTILPIEMKGRKRPEIGQRLRLSQGDIAQANLLYKCPKCGRTFQESSGIFASPSHYTAGALSNETEHCEWRITATYGERVELKLENMNIFKSNNCETDYLEIRDGYFEKSPLIGRFCGKVDKEVIRTESSRMLLTYVNTHRIEGFRGFKAEFD
Protein: Two-component response regulator ARR12 (P62598)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Could directly activate some type-A response regulators in response to cytokinins. Involved in the root-meristem size determination through the regulation of cell differentiation. Involved in activating SHY2 during meristem growth and controls PIN expression via activation of SHY2.
Subcellular location: Nucleus.
Interaction partners:
- Histidine-containing phosphotransfer protein 5
- Histidine-containing phosphotransfer protein 3
- Pseudo histidine-containing phosphotransfer protein 6
- Histidine-containing phosphotransfer protein 4
- Histidine kinase 3
- Histidine kinase 4
- Histidine kinase 2
- Ethylene-responsive transcription factor CRF6
- Ethylene-responsive transcription factor CRF2
- Auxin-responsive protein IAA3
Sequence:
MTVEQNLEALDQFPVGMRVLAVDDDQTCLKILESLLRHCQYHVTTTNQAQKALELLRENKNKFDLVISDVDMPDMDGFKLLELVGLEMDLPVIMLSAHSDPKYVMKGVTHGACDYLLKPVRIEELKNIWQHVVRSRFDKNRGSNNNGDKRDGSGNEGVGNSDQNNGKGNRKRKDQYNEDEDEDRDDNDDSCAQKKQRVVWTVELHKKFVAAVNQLGYEKAMPKKILDLMNVEKLTRENVASHLQKFRLYLKRISGVANQQAIMANSELHFMQMNGLDGFHHRPIPVGSGQYHGGAPAMRSFPPNGILGRLNTPSGIGVRSLSSPPAGMFLQNQTDIGKFHHVSSLPLNHSDGGNILQGLPMPLEFDQLQTNNNKSRNMNSNKSIAGTSMAFPSFSTQQNSLISAPNNNVVVLEGHPQATPPGFPGHQINKRLEHWSNAVSSSTHPPPPAHNSNSINHQFDVSPLPHSRPDPLEWNNVSSSYSIPFCDSANTLSSPALDTTNPRAFCRNTDFDSNTNVQPGVFYGPSTDAMALLSSSNPKEGFVVGQQKLQSGGFMVADAGSLDDIVNSTMKQEQSQGDLSGGDLGYGGFSSLRTCI
Protein: Tektin-1 (Q9DAJ2)
Organism: Mus musculus (Mouse)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q32KZ9}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}.
Interaction partners:
- Piercer of microtubule wall 1 protein
- Protein Flattop
- Tektin-4
- EF-hand domain-containing protein 1
- Cilia- and flagella-associated protein 52
- Cilia- and flagella-associated protein 45
- EF-hand domain-containing family member C2
- Tektin-2
- Outer dynein arm-docking complex subunit 4
- Tektin-3
Sequence:
MAKLLQSPPRFLPEEWYIANKSQYHRAEAQRSQSERLVAESQRLVEEIEKTTRKSQSDVNKKLEQRLEEVRFWKKELDDKLEQLVNQTDDLLTYKTRLERSLESYKEPLHITEKCLEYREKRVGIDLVHDVVEQELQKEADIIHGVMNLLIRTLEESTEQIRLNRSAKYNLEKDLRDKFTAITIDDVCFSLNNNSPNINFSEKVVRIEPNSVSLEDWLDFSNANVEKADKQLNNSTALKTLVDQILSQTANDLRRQCEVVDEAFINGLKETKDARNKLADHLAKVMEEIASQEKNIMALENAITQQEGPAKVAHTRLETRTHRPNVELCRDIAQYRLIKEIQEINHNVARLKETLAQAQTQLKALYRRQLALQEEIQVKENTIYIDQVLCMEMRKSIPPRDGDDHGAWEGGIRAEAIC
Protein: RNA-binding protein 4 (Q9VFT3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO13361p1
- LD31543p
- rhomboid protease
Sequence:
MDAGNCASSACLGDCKGDGKTAIKEEGYEHLRKIFIGGLSTQTTVETLRGFFSQFGIVADAVVLRDPVSNHSRGFGFVTYVDPKSVEIVQRARPHTIDNKIVETKHALPRQDFKRGGGVGSVVGSFGCEAGFMNSKRIFLGGLKEYHDENIVREYFSQFGPVASVKLLMDRETGRQRAFGFLEFVDPSSAEKALAPRKHWILQTLVEVKRSTQKADRRFRFPIFSSVRAGYIPPQPATADSYNYNNPNYNPYLAQSVLPPSAFTNGWAHYVIPMAPKPTPGQNMAASLPSQQLAEHSLNGHGPDMWSSYPKTGIYSAQEWTSSKVAEWGPKAGHKHAQTSTNDRAKIDLKELQAATFNNKLDFGARGDADRMSGAGLGLGLTGGAAVGVGAIKKWPTQDYKVFKPAKSPTNGVIPKIGKEATTPPYGI
Protein: Glypican-3 (Q8IYG2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004471}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004471}; Extracellular side {ECO:0000256|ARBA:ARBA00004471}.
Interaction partners:
Sequence:
MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRFAYYPEDLFIDKKVLKVAHVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSMPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMIKVKNQLRFLAELAYDLDVDDAPGNSQQATPKDNEISTFHNLGNVHSPLKLLTSMAISVVCFFFLVH
Protein: Uncharacterized protein (Q38BU1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFSRSFVGRMGNGTYGGWPWPVKLPLKRGWHHELDRHQSIAEESRRYILFGDALLVSIVLYSVYRLYYLALCSDAYRTHLSHLSGAPPAIIANSFDFANLENNRTVPRAVLDEYREAVVDGKVKRAPIESIIFKY
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Q9VWP1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- 116 kDa U5 small nuclear ribonucleoprotein component
- RE11167p
- Pre-mRNA-processing-splicing factor 8
- Probable ATP-dependent RNA helicase DDX23
- U4/U6 small nuclear ribonucleoprotein Prp31
- Ubiquitin carboxyl-terminal hydrolase
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Ubiquitin carboxyl-terminal hydrolase 16/45
- Precursor RNA processing 3, isoform A
- SD09427p
Sequence:
MAQTQAPAAKRMKLEKTPANPVEEDETPSVFNPKYRVCPYLDTINRNLLDFDFEKLCSISLTRINVYACLVCGKYFQGRGTNTHAYTHSVGEAHHVFLNLHTLRFYCLPDNYEIIDSSLDDIKYVLNPTFTRQEISKLDQLQPKHSRTVDGVLYLPGVVGLNNIKANDYCNVVLHALSHVGPLRDYFLQKQSYAHVVRPPGDSVFTLVQRFGELMRKMWNPRNFKSHVSPHEMLQAVVLWSSKRFQITEQGDPIDFLSWFLNTLHRALKGNKHPNSSILYKIFLGEMKIYTRKMPPVELDDAAKAQLLATEEYKDQVEDKNFIYLTCDLPPPPLFTDEFRENIIPQVNLYQLLSKFNGTAEKEYKTYKANFMKRFEITRLPQFIILYIKRFTKNTFFLEKNPTIVNFPIKHVDFGDILGMRQRDKDVKDTKYNLVANIVHDGDPKKGTYRAHILHKANGQWYEMQDLHVTEILPQMITLTESYIQIYERCPNSS
Protein: Phosphatase 1 nuclear targeting subunit, isoform D (Phosphatase 1 nuclear targeting subunit, isoform E) (Q7KU01)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649}.
Interaction partners:
- LD21442p
- Splicing factor 3A subunit 2
- Cell division cycle 5, isoform A
- Splicing factor 3A subunit 1
- Transferrin
- Splicing factor 3A subunit 3
- Splicing factor 3B subunit 1
- Serine/threonine-protein phosphatase alpha-2 isoform
- Serine/threonine-protein phosphatase alpha-3 isoform
- LD24714p
Sequence:
MPRIVPLQLLRCLRVLLDNNGGILSAVEVKRISGLMAKYSKKLVSKCVYVQILKSTKTELLGDFMAVGGWSLVYTWLNDAIRAMNWPLVQEILELLLLSPVDVNRLKINSAPILVKGLCKDGGNEGVRILAKRLVEQWLKIVTENTSMTIQGAAPHIAATTASQVPASVSGAGSASVPDSASSSDSTDSAGAPVTYTITSAANSSNSNSITIKWKPLLDNPDGGDETDSGTQSKDNEVEHLEKGSSATHLLADASLGKKSGLDDSSSAAEVKSGEDVDNKKHKSSKSDKSKRSEKEREKDRKKESSSHRSSSSSHKSSSSSSSSSSKSSSSKSSSSSSSSHRSSSDKYRDKDKARSSSGSSSSSKDRERSSGSSSSSSNKHKSSKSSSSSSSSSSSSSGSSSSKDRKSSSSTSSSSSSSRQDKDKDNKLMPPPAVAASNAAGTSPTASAKESDAQKPRSIPIMSRKASISIEIRRDTEKTATVKTYQSKFRSHGLTEEAPPPPSRKGLKKPTSSAVAASPALMAVPSSLKRPSPPPRDLSTDKKAKIDINNVAGHVERPGAAKLIAPKKIQTLVETNLFSDALAASIEPKKVVKRKRTSATSPTDKDAPLAPLKFYQDTLDESKSEEKSDDSSKENDDARSSSPGKDTDADDDDIPLKRVKEDIEQKVQKAKAAAGGEGGEAGNTSDNAEDLPEEPKKPGPGCGPDGPPGVLTLHRRKGPKKKLTWQSEEKLTQIRYFEVDRSERVNVMKQTFLEMKNMERFSERDALTIARRGFDDTMEPQMEWRPLLEVDNVPDHPNGNLSKQRQVQMDREATTLRALYFSPDMIPDSPAEAELEPHFAHDIPVIPMDDLTGNPDAVNDYSALAWPEPKKYAPSSGVGANISGSDMGFNDNMLTGLGAGPNLMQNPFDPFMGGMPAPTGMPPGPNMMPNQVPNGTPQIWQNQMGPVGGPPGVPPMMNGPGGPGMDMSNMNMNNMPPQNFMGNQFGSPVSPFGSGPPPGFNQYPPMMMNGPGPGPVMGPNGPVMGPNGPMMNGPPNGPMMNGPPNGMGPGLMMGGPRNNNNNNNRNKNNGGGIWRSGGNNFQENSGGNWRSAGSGPNRGGGGGNGNTGVCKQFMRGHCNMGKNCKYVHPQKKRL
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (D4A978)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Protein kinase C gamma type
- Inositol polyphosphate-5-phosphatase A
- Protein kinase C beta type
- Inositol polyphosphate multikinase
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
Sequence:
MLCGGWRRSRRSPEEPRVSAQVAAPLAFLPSPASSDSSTKRPGLRALKKMGLTEDEDVQAMLRGSKLLKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAASQHIFFVQHIEAVREGHQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLAKLRARLDAMSQRERAHTWIHSYLHRADSDQDSKMSFKEIKSLLRMVNVDMNDMYAYRLFKECDHSNNERLEGAEIEAFLRRLLKRPELEEIFRRYSGEDRVLSASELLEFLEDQGEDGATLACAQKLIQTYELNETAKQHELMTLDGFMMYLLSPEGAALNVAHTCVFQDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFTQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRDHAFTLSPYPVILSLENHCGLEQQIVMARHLRNILGDMLVTQALDSQNPEELPSPEQLKCRVLVKGKKLPAARNEDGRILSDREDEDEDEEEAEEALETAEQRKRAKQISPELSALVVYCCATRLRTLEPSPGPPQPCKIGSLSERKARKFTREAGRNQTIPLFNPVDYSTVALNFQTPGYEMDLNTGRFLINGQCGYVLKPAYLRQLNTTFDPECPGPPRTTLTVQVLTAQQLPKLNVEKPNSIVDPLVRVEIYGVPEDCAHKETDYVLNNGFNPCWEQTLQFQLRAPELVLVRFVVEDYDTTSPNDFVGQFTLPLNSLKQGYRHIHLLSKDGASLSPATLFVHIRIENS
Protein: Prospero homeobox 3 (Prospero-like protein Prox1b) (D2DHG1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Lymphatic vessel endothelial hyaluronic receptor 1b
Sequence:
MDSPSDRFHQQPSQMCPFELYRSLPDSNPSGHRFPPGSLSSHPLFSPLMHPNSMSQKWGSFRQRQGLFPGLLVDDDVSEEDVFGKREFGATSSSQRGSGERGQAPEPSDWGQDFARVKRLRMDSAARSEDESIREGKRGRKSRSSFRMDEKKGMEQGNRRESREGRKRQRQELKLQLEETRGKLLELQRKVWRVYGGQADDEKDQENGGINLDEVADMFSDSDDPLVGNGFSPQRCSSKKNNETNGNGNAGIFPETSVDLDLELNGSQVWLGCSLIRGEWESAEGGQKFAQALKQELANVVAQVIDRVVRLYAESDPEAVSSAQEPSMTMDLNSDRRPRPQAVEQVEALPLVTKSPQDKRAPVAQSGHKDLLLPQANPSLAPLAQPPLPALLPPRGKEHFLPSYPPDNPVHLPLLHYTMQNLFARSLSSLPLHKDCLSESFMDFRSHNSAFPPLPLLGQLDPSPSDRAREVGMRAGGAGMVDGADAALYLAAGSSQEGLSPCHLKKAKLMFFYTRYPSSSTLKTYFPDVKFNRCVTSQLIKWFSNFREFFYIQMERFARQAAREVLTSARERALRLGRDTELYRILNMHYNKSNDYQVPERFVEISEVALREFFTAIQSGRDADPCWKKSIYKIICKLDSPVPDSFRLPGCPTDTYRMG
Protein: Cofilin-1B (P0DJ27)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods (By similarity).
Subcellular location: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-interacting protein 1
Sequence:
MSSGIALAPNCVSTFNDLKLGRKYGGIIYRISDDSKEIIVDSTLPAGCSFDEFTKCLPENECRYVVLDYQYKEEGAQKSKICFVAWCPDTANIKKKMMATSSKDSLRKACVGIQVEIQGTDASEVKDSCFYEKCTKI
Protein: Natural killer cells antigen CD94 (KP43) (Killer cell lectin-like receptor subfamily D member 1) (NK cell receptor) (CD antigen CD94) (Q13241)
Organism: Homo sapiens (Human)
Function: Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20952657, ECO:0000269|PubMed:9485206}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- HLA class I histocompatibility antigen, alpha chain E
- TYRO protein tyrosine kinase-binding protein
- NKG2-A/NKG2-B type II integral membrane protein
- NKG2-C type II integral membrane protein
- HLA class I histocompatibility antigen, C alpha chain
- HLA class I histocompatibility antigen, alpha chain G
- NKG2-E type II integral membrane protein
- Killer cell immunoglobulin-like receptor 2DL3
- Killer cell immunoglobulin-like receptor 2DL1
- Killer cell immunoglobulin-like receptor 3DL1
Sequence:
MAVFKTTLWRLISGTLGIICLSLMSTLGILLKNSFTKLSIEPAFTPGPNIELQKDSDCCSCQEKWVGYRCNCYFISSEQKTWNESRHLCASQKSSLLQLQNTDELDFMSSSQQFYWIGLSYSEEHTAWLWENGSALSQYLFPSFETFNTKNCIAYNPNGNALDESCEDKNRYICKQQLI
Protein: Protein ELF4-LIKE 1 (O80877)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the central CCA1/LHY-TOC1 feedback loop in the circadian clock that promotes clock accuracy and is required for sustained rhythms in the absence of daily light/dark cycles.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MEASRNRSLVGNNRSPEMNENDGEDVAASAAVEDVEVWDTLSNGFKRAQLYLDQNRDLIQRVNENHMSRIPDNVSRNVGLINEINGNISQVMEIYSDLSLNFAKKFDQRRRTTKDGDTTTTTTGS