wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc/iron regulated transporter-related protein 1, DZIP1 protein (Q7K9B7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSQEQTQDVDHHALLVAKIVSMVVLVVITVLCGSLPYVLNRCFHWTKASPEETRSSLVVRCLLFFGGGVLICTTFLHMLPEVIEVVEALQECGSLVKTPFALAEMLLCTGFFLMYALDELMTSLVRHHQGKLSRKESVASLAFERGRSIRHSVLLNPQAKEEVEVKDTEPQPHKDHHGHSHMPVPADDGSSARGLGIILALSLHELFEGMAIGLEGTVSTVWFMFGAVSAHKLVLAFCVGMELLVARTRSSLAILYLVTFSIVTPIGIGVGLGISQQVAAGQPSLPSGVLQGIACGTLLYVVFFEILIESHAGWRALVAAVAGFALMFGLQILSDEAEGDDSLTCS
Protein: Coiled-coil protein (Q8VYC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- YTH domain-containing family protein
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL42z/eL42y
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein eS28z/eS28y
Sequence:
MPKKMGLNSKAEVAKSRKNAAEAEQKDRQTREKEEQYWREAEGPKSKAVKKREEEAEKKAETAAKKLEAKRLAEQEEKELEKALKKPDKKANRVTVPVPKVTEAELIRRREEDQVALAKKAEDSKKKQTRMAGEDEYEKMVLVTNTNRDDSLIEAHTVDEALARITVSDNLPVDRHPEKRLKASFKAYEEVELPRLKSEKPGLTHTQYKDLIWKMWKKSPDNPLNQAAAAAANE
Protein: Transcriptional regulator FleQ (G3XCV0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression. In addition to flagella genes, regulates also expression of biofilm-related genes. Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present.
Interaction partners:
- Antiactivator FleN
- RNA polymerase sigma-54 factor
- Sensor protein kinase FleS
- Flagellar biosynthesis protein FlhF
- B-type flagellin
- RNA polymerase sigma factor FliA
- diguanylate cyclase
- Flagellar secretion chaperone FliSB
- Transcription factor AmrZ
- PelD
Sequence:
MWRETKLLLIDDNLDRSRDLAVILNFLGEDQLTCNSEDWREVAAGLSNSREALCVLLGSVESKGGAVELLKQLASWDEYLPILLIGEPAPADWPEELRRRVLASLEMPPSYNKLLDSLHRAQVYREMYDQARERGRSREPNLFRSLVGTSRAIQQVRQMMQQVADTDASVLILGESGTGKEVVARNLHYHSKRREGPFVPVNCGAIPAELLESELFGHEKGAFTGAITSRAGRFELANGGTLFLDEIGDMPLPMQVKLLRVLQERTFERVGSNKTQNVDVRIIAATHKNLEKMIEDGTFREDLYYRLNVFPIEMAPLRERVEDIALLLNELISRMEHEKRGSIRFNSAAIMSLCRHDWPGNVRELANLVERLAIMHPYGVIGVGELPKKFRHVDDEDEQLASSLREELEERAAINAGLPGMDAPAMLPAEGLDLKDYLANLEQGLIQQALDDAGGVVARAAERLRIRRTTLVEKMRKYGMSRRDDDLSDD
Protein: 12 kDa heat shock protein (Glucose and lipid-regulated protein) (P22943)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism.
Interaction partners:
- Catalase T
- Meiotic sister chromatid recombination protein 1
- Heat shock protein 26
- Protein DDR2
- Heat shock protein 104
- Heat shock protein SSA3
- Protein GRE1
- Heat shock protein 42
- Zinc finger protein MSN2
- Restriction of telomere capping protein 3
Sequence:
MSDAGRKGFGEKASEALKPDSQKSYAEQGKEYITDKADKVAGKVQPEDNKGVFQGVHDSAEKGKDNAEGQGESLADQARDYMGAAKSKLNDAVEYVSGRVHGEEDPTKK
Protein: Beta-sarcoglycan (Beta-SG) (43 kDa dystrophin-associated glycoprotein) (43DAG) (A3b) (Q16585)
Organism: Homo sapiens (Human)
Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Subcellular location: Cell membrane, sarcolemma {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Alpha-sarcoglycan
- Delta-sarcoglycan
- Epsilon-sarcoglycan
- Dystrophin
- Dystroglycan 1
- Gamma-sarcoglycan
- Caveolin-3
- Sarcospan
- Beta-1-syntrophin
- Utrophin
Sequence:
MAAAAAAAAEQQSSNGPVKKSMREKAVERRSVNKEHNSNFKAGYIPIDEDRLHKTGLRGRKGNLAICVIILLFILAVINLIITLVIWAVIRIGPNGCDSMEFHESGLLRFKQVSDMGVIHPLYKSTVGGRRNENLVITGNNQPIVFQQGTTKLSVENNKTSITSDIGMQFFDPRTQNILFSTDYETHEFHLPSGVKSLNVQKASTERITSNATSDLNIKVDGRAIVRGNEGVFIMGKTIEFHMGGNMELKAENSIILNGSVMVSTTRLPSSSSGDQLGSGDWVRYKLCMCADGTLFKVQVTSQNMGCQISDNPCGNTH
Protein: Vacuolar protein sorting-associated protein 27 (Golgi retention defective protein 11) (P40343)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. Controls exit from the prevacuolar compartment (PVC) in both the forward direction to the vacuole and the return to the Golgi. Allows VPS10 to return to the (trans-Golgi network) TGN from the PVC. Might also function as an alternate adapter in the COPIb clathrin-like coat.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:12006563, ECO:0000269|PubMed:12900393, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15169871, ECO:0000269|PubMed:17101773, ECO:0000269|PubMed:17101785}; Peripheral membrane protein {ECO:0000269|PubMed:12006563, ECO:0000269|PubMed:12900393, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15169871, ECO:0000269|PubMed:17101773, ECO:0000269|PubMed:17101785}; Cytoplasmic side {ECO:0000269|PubMed:12006563, ECO:0000269|PubMed:12900393, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15169871, ECO:0000269|PubMed:17101773, ECO:0000269|PubMed:17101785}.
Interaction partners:
- Class E vacuolar protein-sorting machinery protein HSE1
- Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
- Polyubiquitin
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein sorting-associated protein 28
- Vacuolar protein sorting-associated protein 5
- Vacuolar-sorting protein SNF7
- Vacuolar protein-sorting-associated protein 25
- Sorting nexin-3
- Vacuolar protein sorting-associated protein 20
Sequence:
MSVSTPSELDALIEQATSESIPNGDLDLPIALEISDVLRSRRVNPKDSMRCIKKRILNTADNPNTQLSSWKLTNICVKNGGTPFIKEICSREFMDTMEHVILREDSNEELSELVKTILYELYVAFKNDSQLNYVAKVYDKLISRGIKFPEKLTLSNSPTAMFDSKTPADWIDSDACMICSKKFSLLNRKHHCRSCGGVFCQEHSSNSIPLPDLGIYEPVRVCDSCFEDYDLKRHDDSKKSKKHRHKRKKDRDYSTPEDEEELIRKAIELSLKESRNSASSEPIVPVVESKNEVKRQEIEEEEDPDLKAAIQESLREAEEAKLRSERQKASRQMQPQQPSPQPQPIHSVDLSDEEKDSIYMFASLVEKMKSRPLNEILEDSKLQNLAQRVFASKARLNYALNDKAQKYNTLIEMNGKISEIMNIYDRLLEQQLQSINLSQQYTLPQVPSDPYNYLTENVQNPAESYQTPPLQQLSSHQYKPQQDVSRQQSVKANSSPTTNIDHLKTIDVTPHAQQKPQSHVELAPSDPPYPKEEAEDEGTQAVQDEESSTQESRERPYPVETENGETSINKRPQGITRYDFPTVPARKFVQPESTVPLPASSSEIPIKEERPPSPQEELLIEL
Protein: Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain) (Q61730)
Organism: Mus musculus (Mouse)
Function: Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Secreted forms (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD. May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (By similarity).
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Interleukin-33
- Interleukin-1 beta
- Interleukin-1 receptor type 1
- Interleukin-1 receptor-like 1
- Receptor-type tyrosine-protein phosphatase delta
- Interleukin-1 alpha
- Interleukin-1 receptor type 2
- TNF receptor-associated factor 6
- Interleukin-1 receptor-associated kinase 1
- Interleukin-1 receptor-associated kinase 4
Sequence:
MGLLWYLMSLSFYGILQSHASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSAMRFPVHKMYIEHGIHKITCPNVDGYFPSSVKPSVTWYKGCTEIVDFHNVLPEGMNLSFFIPLVSNNGNYTCVVTYPENGRLFHLTRTVTVKVVGSPKDALPPQIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEVWWTIDGKKPDDVTVDITINESVSYSSTEDETRTQILSIKKVTPEDLRRNYVCHARNTKGEAEQAAKVKQKVIPPRYTVELACGFGATVFLVVVLIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNVEEEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKDMKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRWSSNDKQGLSYSSLKNV
Protein: Low-density receptor-like protein (Q8H0X5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein PTST homolog 2, chloroplastic
Sequence:
MASCIATAPLSLSGVSQSHYVKANGLSTTTKLSSICKTSDLTIHKKSNRTRKFSVSAGYRDGSRSGSSGDFIAGFLLGGAVFGAVAYIFAPQIRRSVLNEEDEYGFEKPKQPTYYDEGLEKTRETLNEKIGQLNSAIDNVSSRLRGREKNTSSLNVPVETDPEVEATT
Protein: Putative permease IIC component (Putative PTS system EIIC component) (P39365)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Putative phosphotransferase enzyme IIB component SgcB
- Putative phosphotransferase IIA component SgcA
- PTS system galactitol-specific EIIB component
- PTS system galactitol-specific EIIA component
- Galactitol 1-phosphate 5-dehydrogenase
- Putative sgc region protein SgcQ
- Putative aminopeptidase SgcX
- Phosphocarrier protein HPr
- Protein SgcE
- PTS system glucitol/sorbitol-specific EIIC component
Sequence:
MFDYILSLGGTVFVPIIMIVIGLIFRIPWLQAIKAGVTVGIGFVGMGLVIVMAIDSLSPPIKVMIERFGLALHVFDVGAGPASGVGYATAIGAMIIPVIFLLNVAMLVTRLTKTMNVDIYNYWHYAITGTVVQLMTGSLIYGVLGAICHAALSLKMADWTAKRVQNIVGLEGISIPQGYGSSSVPLFVLLDAIYEKIPFMKGRNIDAQEIQKRYGMVGDPVIIGVVLGLIFGLAAGEGFKGCASLMITVAAIMVLFPRMIRLIVEGLLPISDGARKFFQKYFKGREVYIGLDTAVTLGHPTTIAVGLLLIPIMLILASILPGNKVLPLADLPVAPFFICMATVIHRGDLVRTLISGVIVMITVLLIATQFAPYFTEMALKGGFSFAGESAQISALSVGNMFGWSISELMSLGIIGVVVAVGIVASVVLFLRKRELSE
Protein: Collagen alpha-1(XXVIII) chain (Q2UY09)
Organism: Homo sapiens (Human)
Function: May act as a cell-binding protein.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}.
Interaction partners:
Sequence:
MWNRYFVFYLLLLSAFTSQTVSGQRKKGPKSNLLARKSDVQGSICFIDIVFIVDSSESSKIALFDKQKDFVDSLSDKIFQLTPGRSLEYDIKLAALQFSSSVQIDPPFSSWKDLQTFKQKVKSMNLIGQGTFSYYAISNATRLLKREGRKDGVKVVLLMTDGIDHPKNPDVQSISEDARISGISFITIALSTVVNEAKLRLISGDSSSEPTLLLSDPTLVDKIQDRLDILFEKKCERKICECEKGDPGDPGPPGTHGNPGIKGERGPKGNPGNAQKGEAGERGPGGIPGYKGDKGERGECGKPGIKGDKGSPGPYGPKGPRGIQGITGPPGDPGPKGFQGNKGEPGPPGPYGSPGAPGIGQQGIKGERGQEGRPGAPGPIGVGEPGQPGPRGPEGVPGERGLPGEGFPGPKGEKGSEGPTGPQGLQGLSIKGEKGDIGPVGPQGPMGIPGIGSQGEQGIQGPIGPPGPQGPAGQGLPGSKGEVGQMGPTGPRGPVGIGVQGPKGEPGSIGLPGQPGVPGEDGAAGKKGEAGLPGARGPEGPPGKGQPGPKGDEGKKGSKGNQGQRGLPGPEGPKGEPGIMGPFGMPGTSIPGPPGPKGDRGGPGIPGFKGEPGLSIRGPKGVQGPRGPVGAPGLKGDGYPGVPGPRGLPGPPGPMGLRGVGDTGAKGEPGVRGPPGPSGPRGVGTQGPKGDTGQKGLPGPPGPPGYGSQGIKGEQGPQGFPGPKGTMGHGLPGQKGEHGERGDVGKKGDKGEIGEPGSPGKQGLQGPKGDLGLTKEEIIKLITEICGCGPKCKETPLELVFVIDSSESVGPENFQIIKNFVKTMADRVALDLATARIGIINYSHKVEKVANLKQFSSKDDFKLAVDNMQYLGEGTYTATALQAANDMFEDARPGVKKVALVITDGQTDSRDKEKLTEVVKNASDTNVEIFVIGVVKKNDPNFEIFHKEMNLIATDPEHVYQFDDFFTLQDTLKQKLFQKICEDFDSYLVQIFGSSSPQPGFGMSGEELSESTPEPQKEISESLSVTRDQDEDDKAPEPTWADDLPATTSSEATTTPRPLLSTPVDGAEDPRCLEALKPGNCGEYVVRWYYDKQVNSCARFWFSGCNGSGNRFNSEKECQETCIQG
Protein: Zinc finger CCCH domain-containing protein 33 (AtC3H33) (Zinc finger CCCH domain-containing protein ZFN1) (Q8GXX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At2g20710
- F19P19.27 protein
- T1B9.12 protein
- Protein GLUTAMINE DUMPER 3
Sequence:
MDFNAGVPMSSLSPLMNQDAMWQMNLSSDETMETGSYPERPGEPDCSYYIRTGLCRFGSTCRFNHPRDRELVIATARMRGEYPERIGQPECEYYLKTGTCKFGVTCKFHHPRNKAGIAGRVSLNMLGYPLRSNEVDCAYFLRTGHCKFGGTCKFNHPQPQPTNMMVPTSGQQSYPWSRASFIASPRWQDPSSYASLIMPQGVVPVQGWNPYSGQLGSVSPSGTGNDQNYRNLQQNETIESGSQSQGSFSGYNPGSSVPLGGYYALPRENVFPERPGQPECQFYMKTGDCKFGTVCKFHHPRDRQAPPPDCLLSSIGLPLRPGEPLCVFYTRYGICKFGPSCKFDHPMRVFTYDNTASETDEVVETSTGKSRRLSVSETRQAATTSSGKDTTIDNTQQ
Protein: tRNA (uracil-5-)-methyltransferase homolog B (EC 2.1.1.35) (TRM2 homolog B) (rRNA (uracil-5-)-methyltransferase TRMT2B) (EC 2.1.1.-) (Q96GJ1)
Organism: Homo sapiens (Human)
Function: Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine in tRNAs and 12S rRNA. Catalyzes the methylation of uridine at position 54 (m5U54) in all tRNAs. Specifically methylates the uridine in position 429 of 12S rRNA (m5U429). Does not affect RNA stability or mitochondrial translation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:31948311}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix {ECO:0000269|PubMed:27184847}.
Interaction partners:
- Ribosome biogenesis protein BOP1
- tRNA
- 12S rRNA N
- tRNA
Sequence:
MAGLKRRVPLHSLRYFISMVGLFSKPGLLPWYARNPPGWSQLFLGTVCKGDFTRVIATKCQKGQKSQKKPSHLGPLDGSWQERLADVVTPLWRLSYEEQLKVKFAAQKKILQRLESYIQMLNGVSVTTAVPKSERLSCLLHPIIPSPVINGYRNKSTFSVNRGPDGNPKTVGFYLGTWRDGNVVCVQSNHLKNIPEKHSQVAQYYEVFLRQSPLEPCLVFHEGGYWRELTVRTNSQGHTMAIITFHPQKLSQEELHVQKEIVKEFFIRGPGAACGLTSLYFQESTMTRCSHQQSPYQLLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKEDGQSIVAVVNPARAGLHYKVIQAIRNFRAIHTLVFVSCKLHGESTRNVIELCCPPDPAKKLLGEPFVLQQAVPVDLFPHTPHCELVLLFTR
Protein: 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory complex subunit p37B) (26S proteasome regulatory subunit rpn11) (Yippee-interacting protein 5) (Q9V3H2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear (By similarity).
Interaction partners:
- Regulatory particle triple-A ATPase 4
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 6B
- Ubiquitin carboxyl-terminal hydrolase
- Proteasome subunit alpha type-5
- Proteasomal ubiquitin receptor ADRM1 homolog
- GH11341p
- 26S proteasome regulatory subunit 4
Sequence:
MDRLLRLGGAMPQAAPPTDAPVVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVQVIDVFAMPQTGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINPNMLVLGQEPRQTTSNLGHLQKPSVQALIHGLNRHYYSISINYRKNELEQKMLLNLHKKSWKDGLTLSDYNEHCSINEDTVAEMLDLAKNYNKSLEDEEKMTPEQLAIKNVGKQDPKRHLEEKVDKVMQNNIVQCLGAMLDTIVFK
Protein: Inner kinetochore subunit NKP1 (Constitutive centromere-associated network protein NKP1) (Non-essential kinetochore protein 1) (Q12493)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:12408861}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12408861, ECO:0000269|PubMed:29046335}. Note=Associated with kinetochores.
Interaction partners:
- Inner kinetochore subunit OKP1
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit NKP2
- Inner kinetochore subunit IML3
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit AME1
- Inner kinetochore subunit MCM16
- Inner kinetochore subunit MCM21
- Inner kinetochore subunit CTF3
- Inner kinetochore subunit CTF19
Sequence:
MTDTYNSISNFIENELTALLSSDDYLMDDLAGELPNEVCRLLKAQVIEKRKDAMSRGKQDLLSKEIYDNESELRASQSQQIMELVGDIPKYSLGSELRNRVEGEPQSTSIERLIEDVLKLPQMEVADEEEVEVENDLKVLSEYSNLRKDLILKCQALQIGESKLSDILSQTNSINSLTTSIKEASEDDDISEYFATYNGKLVVALEEMKLLLEEAVKTFGNSPEKREKIKKILSELKK
Protein: EG:100G10.4 protein (O76864)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPAKAVSRLWNFRARATSIQFVPVSQKTNIIMSPPRHILKLSLEEQRQFIDSFDLVISDCDGVVWLLVGWIPNTGAAVNALKAAGKQIKFVSNNSFRSEEDYMEKFRHIGAKNVQEDDIVHPVKTIVRYLKKHKPGERVYSLMSLEANETLRKHNIEFESLFKSFRVTFIFHIILFQQVKEHLTAASLVDHLAIEKPVGAVLFDIHLDLSYVELAKAIRHLQENDDCQLIAGGSDVIMPLAENLNVAGFFDFLEHVKRYTQREATFLGKPSPILGEMFGEMFEIRDCKRCIFIGDTLVQDVQFGKACGFQSLLVLSGCLTKEDMLNAPVEAQPDYYADSLADFTQLLENIQK
Protein: Warthog protein 4 (Protein M75) [Cleaved into: Warthog protein 4 N-product; Warthog protein 4 C-product] (Q94129)
Organism: Caenorhabditis elegans
Function: Intercellular signal essential for a variety of patterning events during development.
Subcellular location: [Warthog protein 4]: Secreted {ECO:0000250}. Cell surface {ECO:0000250}. Note=Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250}.; SUBCELLULAR LOCATION: [Warthog protein 4 N-product]: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: [Warthog protein 4 C-product]: Secreted, extracellular space {ECO:0000250}. Note=Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250}.
Interaction partners:
- MAM domain-containing protein
- WaRThog
- ShKT domain-containing protein
- Uncharacterized protein
- Warthog protein 3
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- EB domain-containing protein
- Ground-like domain-containing protein
Sequence:
MRFSLLALVLLSSSYKFTYGSECGDSTIPYSLEVLSSGQPILGCARPTCFGWHSNGHQLPTNAKFFRIDQQSDGFLRDDPLAIHTFDAADPRVYAQQQASCEQEFQSLSCNPEDQWVGGIAPVMNASTTKIVAYKCCTYAPLRASIDRGVATVSGGQIVVGGEIFADNKPYAFDYISNVEKKIDSEGEIFYEVNIKRFSCLDLQKVDRSVPEILNSENTIRHVNGHRFVVHQAPTVDVETPVETGQLVVPQGVQNGQEVIIEEIVAQEGFVQETNPQPPPPPGQQGGFVQPQGFQPQGGFQPQGFQPQGFQPQAFQPQVVQNPVPAAPAGYAPMGFAPSGLQLYYCFPGDAMVNVYNGGFKRMDELAVGDWVQALDKNGSQVTFIPVQYWLHRDPKQVADFVEFTLDNGETFSLTEKHLVFVTQCSVPYSEDENINANPVPAERVNIGDCFYIAHRKKSQMYQRVKVLDINIVQKTGIYSPMTSRGHLLVDRIHASCHSETDNYSLQNTFFTNVLRWKSQIRNYFWTVEDSTNEDNIGYGLNGVMAVLDIVIPSKLM
Protein: Homeobox protein otx5-B (Orthodenticle homolog 5-B) (XOtx5b) (Q9PT61)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor involved in anterior and eye development. Promotes the differentiation of both rod and cone photoreceptors cells in the retina. Together with other retinal homeobox proteins, acts as an effector of a cellular clock which, depending on cell cycle progression, establishes the generation of distinct retinal neuronal cell types. Acts synergistically with nrl to activate the rhodopsin promoter. Promotes the formation of anterior regions and represses the formation of posterior structures during development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:16903786}.
Interaction partners:
Sequence:
MMSYIKQPHYAVNGLTLAGTGMDLLHSAVGYPTNPRKQRRERTTFTRAQLDILESLFAKTRYPDIFMREEVALKINLPESRVQVWFKNRRAKCRQQQQQSTGQAKPRPAKKKTSPARETNSEASTNGQYSPPPPGTAVTPSSSASATVSIWSPASISPIPDPLSAVTNPCMQRSTGYPMTYSQAPAYTQSYGGSSSYFTGLDCGSYLSPMHPQLSAPGATLSPIATPTMGSHLSQSPASLSAQGYGAASLGFTSVDCLDYKDQTASWKLNFNATDCLDYKDQSSWKFQVL
Protein: RNA-binding Fox protein 1, isoform F (A8JNQ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYYPHMVQAGVAPFPGAPAGYAAAPNPGAAVVAAAAAAQQQQQQQQQQQQQQQQAQQQQQQQVAGGPPSAADSLSMAVAAAAAKQSADPVTQMKSGSEAAGSGNSNNNNTAGAGTGAPGAAGGLTTEYSSGGCGGGGASTANSVVVATSVSDVVNASLYMQQKSTVLIANEAAESQQSSAMQNAGGGGNTGGGGGGGGGGTPSSPLSNSPSSATASQAGGCGLTLNGSATEGSMSGDTSPVASGEPLLQTPPAHQQQQQQQQPLLCSSPTSMQSSGTSVTGSSIASGTLAATSSSGVGLLPTTGLDSIANGGAPTGCAVVPASTSQVIAHLNAAAAAASGIVSPSANVATSLSSALVPAQSVAAVAAASLDAKSQPKRLHVSNIPFRFRDPDLRAMFGQFGTILDVEIIFNERGSKGFGFVTFANSNDAERARERLHGTVVEGRKIEVNNATARVQTKKVTAVPNVCVQWPEAAVAAAMRGVAIQRGHVGVVGATPYHHPHHPHHHPALLAASAAAAQQQQQRQLAAAAVATAAVAQQQQQQQQAVVQQQQQQVAAAAQQQHQQQQQQQQQAVQQQQAVQQQQQHQQQQQQQQQQQHAAVAAAAAAASHPHMHAAHAHAHAHALGPQLAQLQAVAVPTAASNAAALQQSLAAAIQNPSGNPNAAAAAAAYAARLSAATGATQSPQTAAAAAAAASMAASANAANNAAALHGFAPVYYDPFLAAAASADPNLRFQCRNLTPKPEEIRQSIEHFCKTLCKLNNFY
Protein: T-complex protein 1 subunit alpha (CCT-alpha) (B2ZDY6)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEGPLSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYISENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFSNMVVDAVLAVKYTDVRGQPRYPVNSINILKAHGRSQTESMLVSGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVDAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEETFEAVMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLINGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPETKDDKHGGYEDAVHSGALDD
Protein: Uncharacterized protein (Q9CV93)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
ARCQGNNQIILLEPEPVDNVTCANRHLPIKVWDQEPCHFHYECECFCSGWGHSHYLTFDGTSYTFLDNCTSVLMREIHPRHGNLSILAHSYYCGATTNVTSCPRALSVYYNSMEIILTISTTESGKDESLIIWDQMWIRSGFSKNGVTVSLSGATTMSVNISTIGTIITFDGNIFQIWLPYRYFSSNTEGQCGTCTNSQIDDCRRPDGTIASDCQDMAKEWLVPGNSSSSCLAQPSPLPSTTPQTPVSSTLTSTPCPSAPLCELMLSQVFAECHRLIPPDAFFRSCVSDHCNANITDMLCQSLEAYAALCRAQGVCTNWRNATGGLCDLSCPPTKEYRPCGPLHPASCNSRTQDSTTGMLAEGCFCPENQLLFNSRMDICVSECPCVGPDGLPKFPGEHWISNCQACVCEPGSVSVQCEPVKCESQDKPPQCTEAGFVTVTWPSADNPCCPETLCVCNSTTCPKSLPTCEPGYELVQTHENSSCCPSYSCRPRLCTYNDTIYGVGTTFPGGPCHTCTCLSDGDQEPKVECKETNCTTSCPQGFKYTLVPEQCCGECLQNACLTPEGHAVQPNETWVNSPVDNCTAYHCMAENGVYVLTPIPTSCPDVSNCTGTLRKTGCCYSCEKEDSSTCQVHVNATVLRYKGCETEVNITFCEGSCSGISKYSMEAQAMERQCTCCQESKVHDVAVTMQCPDGTVIQHTYTHIDECNCAPACSSLPGTSMIAS
Protein: Isopentenyl-diphosphate Delta-isomerase 1 (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerase 1) (IPP isomerase 1) (IPPI1) (O35586)
Organism: Mesocricetus auratus (Golden hamster)
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Subcellular location: Peroxisome {ECO:0000269|PubMed:9228075}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Terpene cyclase/mutase family member
- Squalene synthase
- RUN and SH3 domain-containing protein 1 isoform X2
- Farnesyl pyrophosphate synthase
- Hydroxymethylglutaryl-CoA synthase
- Squalene monooxygenase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Lanosterol 14-alpha demethylase
- Alkyl transferase
Sequence:
MPEINTSHLDEQQVQLLAEMCILIDENDNKIGADTKKNCHLNENIDKGLLHRAFSVFLFNTENKLLLQQRSDAKITFPGCFTNSCCSHPLSNPGELEENDAIGVKRAAQRRLKAELGIPLEEVDPNEMHYLTRIYYKAQSDGIWGEHEIDYILFLKKNVTLNPDPNEIKSYCYVSKEELKELVKKAASGEVKLTPWFKIIVDTFLFKWWDNLNHLSQFVDHEKIHRM