wanglab/gogpt-training-data huggingface dataset:
Protein: Actin-related protein 2/3 complex subunit 3 (Arp2/3 complex 21 kDa subunit) (p21-ARC) (O96624)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 1
- Actin-related protein 2/3 complex subunit 5
- Wiscott-Aldrich syndrome protein
- WASP-related protein
- SPIN90/Ldb17 leucine-rich domain-containing protein
- Putative actin-22
Sequence:
MVYHSQFNDESAGFRLVGNVPILPLKTTHKGPAPKGDANSVDIIDEALDLFKANILFRNFEVQGNGDRVLIYLTLYITKCLLKIAPMNKADAEKALFLIAQEQFSIPGESAFPLGGLVTVPNTRDAADTLRQYFTQLRLELGVRLCQRVYAVDPSKANKWWICFSKRKFLNKAL
Protein: Pentatricopeptide repeat-containing protein At2g18940, chloroplastic (O64624)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- RNA-binding
- AT3G20230 protein
- Small ribosomal subunit protein cS23y
- RNA polymerase sigma factor sigB
- Large ribosomal subunit protein uL3c
- Large ribosomal subunit protein bL28c
Sequence:
MDGALFPHKPPYPIQSKRPPPSQSSNQSIKFSSATLHLPPPSPPSFPLDSLLHHLVHLSSPPPRHSNSAAARFPSLEVSTDSSSSKPILGIEIENERNGSLKLLCKKEVVLVNSIVEQPLTGLSRFFDSVKSELLRTDLVSLVKGLDDSGHWERAVFLFEWLVLSSNSGALKLDHQVIEIFVRILGRESQYSVAAKLLDKIPLQEYLLDVRAYTTILHAYSRTGKYEKAIDLFERMKEMGPSPTLVTYNVILDVFGKMGRSWRKILGVLDEMRSKGLKFDEFTCSTVLSACAREGLLREAKEFFAELKSCGYEPGTVTYNALLQVFGKAGVYTEALSVLKEMEENSCPADSVTYNELVAAYVRAGFSKEAAGVIEMMTKKGVMPNAITYTTVIDAYGKAGKEDEALKLFYSMKEAGCVPNTCTYNAVLSLLGKKSRSNEMIKMLCDMKSNGCSPNRATWNTMLALCGNKGMDKFVNRVFREMKSCGFEPDRDTFNTLISAYGRCGSEVDASKMYGEMTRAGFNACVTTYNALLNALARKGDWRSGENVISDMKSKGFKPTETSYSLMLQCYAKGGNYLGIERIENRIKEGQIFPSWMLLRTLLLANFKCRALAGSERAFTLFKKHGYKPDMVIFNSMLSIFTRNNMYDQAEGILESIREDGLSPDLVTYNSLMDMYVRRGECWKAEEILKTLEKSQLKPDLVSYNTVIKGFCRRGLMQEAVRMLSEMTERGIRPCIFTYNTFVSGYTAMGMFAEIEDVIECMAKNDCRPNELTFKMVVDGYCRAGKYSEAMDFVSKIKTFDPCFDDQSIQRLALRVRENLES
Protein: Zinc finger protein rsv2 (Required for stationary phase viability protein 2) (Q9Y815)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Transcription factor atf21
- Transcription factor atf31
- Zinc finger protein rsv1
- Protein lsd90
- Hydrogen peroxide stress regulator 1
Sequence:
MDTTNNTYARSISSNGNDNFPTPDWQFNGSQLQQNRKSKMNGRSVTNVFPNAFSDAEFEQISMPELNLKRFNPTTLEENNSDLSDMSSWDYMMNVPIRVYNDADTMDPFSLDTIPDSSMDMPFDPLASDYGNAANFPSVPSSLGSNHQFITTPPVNGSNEPTSAQTNHIITANSSPSGNAGSNASASMSVPPPLTPSASTINDQPFSNSFDLPSQVIADGTGAISDINGNPFPMNSPPLDMEPLPSISMDASDSVSEQLVKDASLPSGPFSTDYLENGSDLKRSLGHNQKSDRVSKDVSPQHQANPSTLNNPLKTQNFDSSKNLYTDNKDSSLVSPTGLQSRMEQNPEVRAHPMKDSATSTALRRSHALGAAADSLLPQENSAQIYDGKDVSMVNDNMHSDVRQDSFNKESIKQRIPSLSPPITRSYNAKHRPSLVLGTSVNPHSLSPSQPPVVVPSNTTISSSPPLTSPVKTSANIPNLLPTSELDSSNAPHSQSAATHDLNDVKSYYNTRSSHSVVPNPTNQKVSITGAAADGPNGSAPVDTTPTNSSTTATGAQRKRRKFKFGKQIGPVRCTLQNRVTGEICNTVFSRTYDLIRHQDTIHAKTRPVFRCEICGDQRHFSRHDALVRHLRVKHGR
Protein: Aquaporin PIP1-1 (Plasma membrane intrinsic protein 1-1) (ZmPIP1-1) (ZmPIP1;1) (ZmPIP1a) (Q41870)
Organism: Zea mays (Maize)
Function: Water channel required to facilitate the transport of water across cell membrane. Active as heteromers with PIP1-2, but not as homomers.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Aquaporin SIP1-1
- Aquaporin SIP2-1
Sequence:
MEGKEEDVRLGANKFSERHAIGTAAQGTDDKDYKEPPPAPLFEPGELKSWSFYRPGIAEFVATFLFLYISILTVMGVSKSTSKCATVGIQGIAWSFGGMILALVYCTAGISGHINPAVTFGLFLARKLSLTRAVFYIIMQCLGAICGRGVVKGFQQGLYMGNGGRRNVVAPGYTKGDGLGAEIVGTFILVYTVFSATDAKRRARDSHVPILAPLPIGFAVFLVHLATMGITGTGINPARSLGAAVIYNQHHAWADHWIFWVGPFIGAALAAIYHQVIIRAIPFKSRS
Protein: MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3) (F7BJB9)
Organism: Mus musculus (Mouse)
Function: Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response. Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function. Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity. Binds RNA in vitro. Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17332504}. Nucleus matrix {ECO:0000250|UniProtKB:Q14149}. Nucleus, PML body {ECO:0000269|PubMed:17332504}. Chromosome {ECO:0000269|PubMed:27528681}. Note=Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent. {ECO:0000250|UniProtKB:Q14149}.
Interaction partners:
- Histone H3.3
- Histone H3.1
- Histone H3.2
- E3 ubiquitin-protein ligase TRIM33
- Interferon-induced helicase C domain-containing protein 1
- SUMO-activating enzyme subunit 1
Sequence:
MAAQPPTGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYLEVIKAEHVVVPIVTFNKHRQMINLTESKASLAAILEHSLFSTEQKLLAELNAIMGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDETAGRKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTRTVRITFGFNCRNKDHYGIMMYHKNRLIKAYEKVGCQLKANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYWNEMKVKKNAEYPVNLPVEDIQKRPDQTWVQCDACLKWRKLPDGIDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTSKERFRIRQPEILPRILPQINPELLYQTSVSSQSFSPVKESVPRPHLSEVTSPFAARIINLNLASPASEPENSSMKRKLGVHSSILNAKTRRLSNPPVENSSYKNDDDEDVIILEENSTPKPAVDLEVKSDIEVKSEQSHTEQSGIHVDLVSSPKPCVQASSTSTSTSRSDPGITVSTQTDAPGLTVKKEESMEEDMGVRNGTATLSCVGTEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST
Protein: Retinal dehydrogenase 2 (RALDH 2) (RalDH2) (EC 1.2.1.36) (Aldehyde dehydrogenase family 1 member A2) (ALDH1A2) (Retinaldehyde-specific dehydrogenase type 2) (RALDH(II)) (Q63639)
Organism: Rattus norvegicus (Rat)
Function: Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Retinol dehydrogenase 10
- Cytochrome P450, family 26, subfamily C, polypeptide 1
- Retinol dehydrogenase 5
- All-trans-retinol dehydrogenase [NAD
- Dehydrogenase/reductase
- Alcohol dehydrogenase class-3
- Dehydrogenase/reductase SDR family member 9
- Retinol dehydrogenase 16
Sequence:
MTSSEIAMPGEVKADPAALMASLQLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVCNPATGEQVCEVQEADKVDIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRATLATMESLNGGKPFLQAFYIDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFTWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVKRSVERAKRRIVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALMVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
Protein: Small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (A0A8I6AA88)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU365053}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365053}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000256|RuleBase:RU365053}.
Interaction partners:
Sequence:
MAYRGQGQKVQKNLIFRYLQNRSRIQVWLYEQVNMRIEGCIIGFDEYMNLVLDDAEEIHSKTKSRKQLGRIMLKGDNITLLQSVSN
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (A0A8I6A5T3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKSCGVSLATAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEEYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQLENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQACKPHHPNTEPVLGLSQTPISQQSLPLHMIPPSQVDDLSSPAKRKRTSSPTKNTSDNWSGGNAVPHPPVQQQTHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRQTGVAQVRPTGIPNGPTADSSLPTNSASGQQPQLPLTRMPSVSQPGVQPACPRQALANGPFSAGHVPCSTSRTLGSTDTILIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGQSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTLPETNRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDIVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSVSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRRGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMVKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCAWKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
Protein: Core histone macro-H2A.1 (Histone macroH2A1) (mH2A1) (H2A.y) (H2A/y) (Q02874)
Organism: Rattus norvegicus (Rat)
Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (By similarity). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O75367}. Chromosome {ECO:0000250|UniProtKB:O75367}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin. Recruited to DNA damage sites in an APLF-dependent manner. {ECO:0000250|UniProtKB:O75367}.
Interaction partners:
- Cytokine-like nuclear factor N-PAC
- Histone deacetylase 2
- Poly [ADP-ribose] polymerase 1
- Histone deacetylase 1
- Histone deacetylase 1
- Histone deacetylase 8
- Deubiquitinase MYSM1
- Histone deacetylase
- Histone deacetylase
- Protein deacetylase HDAC6
Sequence:
MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVAKKTGGKKGARKSKKQGEVSKAASADSTTEGAPTDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNADFYIGGEVGSTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDRKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
Protein: CBY1-interacting BAR domain-containing protein 1 (Q8BP22)
Organism: Mus musculus (Mouse)
Function: Acts as a positive regulator of ciliary hedgehog signaling. Probable regulator of ciliogenesis involved in limb morphogenesis. In cooperation with CBY1 it is involved in the recruitment and fusion of endosomal vesicles at distal appendages during early stages of ciliogenesis (By similarity). Plays an important role in the mitochondrial function and is essential for maintaining mitochondrial morphology and inner membrane ultrastructure (By similarity). In vitro, can generate membrane curvature through preferential interaction with negatively charged phospholipids such as phosphatidylinositol 4,5-bisphosphate and cardiolipin and hence orchestrate cristae shape (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A1XBS5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:A1XBS5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27528616}. Cell projection, cilium {ECO:0000269|PubMed:29459677}. Nucleus {ECO:0000250|UniProtKB:A1XBS5}. Mitochondrion inner membrane {ECO:0000305|PubMed:30404948}; Peripheral membrane protein {ECO:0000250|UniProtKB:A1XBS5}; Matrix side {ECO:0000250|UniProtKB:A1XBS5}. Note=Weak punctate vesicular distribution throughout the cytoplasm. Localizes at the distal end of mother centrioles. Extensive colocalization with CBY1 at mother centrioles (PubMed:27528616). Localizes at the transition zone, a region between the basal body and the ciliary axoneme (PubMed:29459677). {ECO:0000250|UniProtKB:A1XBS5, ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:29459677}.
Interaction partners:
- Protein chibby homolog 1
Sequence:
MLRRNLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAEVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRATIDATRTSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDLEVFRNSLYLSDYPSRLDIVRANSKSPLQRSLSTKCTSGTGQISTCRTRKDQQVEDEDDEELDVTEDEN
Protein: Transmembrane channel-like protein (A0A0G2KB87)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}.
Interaction partners:
- LHFPL tetraspan subfamily member 5 protein
- Calcium and integrin-binding family member 2
- Transmembrane inner ear
- Protocadherin-15
- USH1 protein network component sans
- Calcium and integrin binding family member 3
- Myosin VIIA
- Cadherin-23
- USH1 protein network component harmonin.
- Unconventional myosin-XV
Sequence:
MIATVKCKPWKMEKKIEVLKEAKKFVSENEGALGKGKGKKWFAFKMMMAKKWAKFLRDFENFKAACVPWENKIKAIESQFGSSVASYFLFLRWMYGVNMVLFILTFSLIMLPEYLWGLPYGSLPRKTVPRAEEASAANFGVLYDFNGLAQYSVLFYGYYDNKRTIGWLNFRLPLSYFLVGIMCIGYSFLVVLKAMTKNIGDDGGGDDNTFNFSWKVFCSWDYLIGNPETADNKFNSITMNFKEAIIEERAAQVEENIHLIRFLRFLANFFVFLTLGASGYLIFWAVKRSQEFAQQDPDTLGWWEKNEMNMVMSLLGMFCPTLFDLFAELEDYHPLIALKWLLGRIFALLLGNLYVFILALMDEINNKIEEEKLVKANITLWEANMIKAYNESLSGNTTGPPFFVHPADVPRGPCWETMVGQEFVRLTVSDVLTTYVTILIGDFLRACFVRFCNYCWCWDLEYGYPSYTEFDISGNVLALIFNQGMIWMGSFFAPSLPGINILRLHTSMYFQCWAVMCCNVPEARVFKASRSNNFYLGMLLLILFLSTMPVLYMIVSLPPSFDCGPFSGKNRMFEVIGETLEHDFPSWMAKILRQLSNPGLVIAVILVMVLTIYYLNATAKGQKAANLDLKKKMKQQALENKMRNKKMAAARAAAAAGGQ
Protein: Protein 4.1 (P4.1) (4.1R) (Band 4.1) (EPB4.1) (Erythrocyte membrane protein band 4.1) (P11171)
Organism: Homo sapiens (Human)
Function: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12427749}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12427749, ECO:0000269|PubMed:23870127}. Nucleus {ECO:0000269|PubMed:12427749}.
Interaction partners:
- Glycophorin-C
- Ankyrin-1
- Ankyrin-2
- Ankyrin-3
- Alpha-adducin
- Gamma-adducin
- Beta-adducin
- Dematin
- Spectrin beta chain, erythrocytic
- Ezrin
Sequence:
MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECSKIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNGDQTQKLAEKTEDLIRMRKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEIADE
Protein: Neuralized-like protein 4 (Q96JN8)
Organism: Homo sapiens (Human)
Function: Promotes CCP110 ubiquitination and proteasome-dependent degradation. By counteracting accumulation of CP110, maintains normal centriolar homeostasis and preventing formation of ectopic microtubular organizing centers.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22261722, ECO:0000269|PubMed:22441691}. Note=Localizes to procentriole and daughter centriole in growing and quiescent cells (PubMed:22441691). May loose association with centrosomes during mitosis (PubMed:22261722). {ECO:0000269|PubMed:22261722, ECO:0000269|PubMed:22441691}.
Interaction partners:
- E3 ubiquitin-protein ligase HERC2
- Mitogen-activated protein kinase 6
- Centriolar coiled-coil protein of 110 kDa
- Ubiquitin-protein ligase E3A
- Centrosomal protein of 97 kDa
- Centrosomal protein of 290 kDa
Sequence:
MAAGSGGSGGSGGGPGPGPGGGGGPSGSGSGPGSNGGLGSGGELHPRTGRLVSLSACGRTARRQQPGQEFNHGLVLSREPLRDGRVFTVRIDRKVNSWSGSIEIGVTALDPSVLDFPSSATGLKGGSWVVSGCSVLRDGRSVLEEYGQDLDQLGEGDRVGVERTVAGELRLWVNGRDCGVAATGLPPRVWAVVDLYGKCTQITVLPPEPGFSPPTPIPTPPLEPLAPTEDSALAEQGTSADEAFMVSPAQARPETFPNSLESHNDFANMELSEVVSNTILSAYNGGLLNVNLSSPPAGEGLGSSGAATSPILTSNDALLFHEKCGTLIKLSNNNKTAERRRPLDEFNNGVVMTNRPLRDNEMFEIRIDKLVDKWSGSIEIGVTTHNPNSLEYPATMTNLQSGTIMMSGCGILTNGKGTRREYCEFSLDELQEGDHIGLTRKSNSALHFFINGIDQGVATPLTPPVVYGVVDLYGMAVKVTIVHNNNHSDRLRRNNAILRALSPEGALRRAAPAAQAEPERLLFHPNCGQKAAITHEGRTALRPHATDDFNHGVVLSSRALRDGEVFQVRIDKMVDKWAGSIEIGVTTHNPAYLQLPSTMTNLRSGTWMMTGNGVMHNGTTILDEYGHNLDRLKAGDTVGVVRREDGTLHFFVNGMTQGPAAWNVPPGVYAVVDLYGQAAQATIVDDVEVAPVPEPLPEGNNQVSPSSPSSGAGGSDLRFHQLHGSNAVITNGGRTALRHNCRSEFNDAIVISNRALRDGELFEIVIQKMVDRWSGSIEAGVTAIRPEDLEFPNTMTDIDYDTWMLSGTAIMQDGNTMRNNYGCDLDALGTGARIGMMRTAKGDLHYFINGQDQGAACSGLPPGKEVYAVVDLYGQCVQVSITNATGPMDNSLATSNTATEKSFPLHSPVAGVAHRFHSTCGKNVTLEEDGTRAVRAAGYAHGLVFSTKELRAEEVFEVKVEELDEKWAGSLRLGLTTLAPGEMGPGAGGGGPGLPPSLPELRTKTTWMVSSCEVRRDGQLQRMNYGRNLERLGVGSRVGVRRGADDTMHILVDGEDMGPAATGIAKNVWAVLDLYGPVRGVSIVSSTRLEESEGTQPPSPSSDTGSEGEEDDEGEEHGLGGQNEVGIIPTTLEFLENHGKNILLSNGNRTATRVASYNQGIVVINQPLVPQLLVQVRIDFLNRQWTSSLVLGVITCAPERLNFPASACALKRAAWLLRGRGVFHNGLKICEKFGPNLDTCPEGTILGLRLDSSGGLHLHVNGVDQGVAVPDVPQPCHALVDLYGQCEQVTIVNPEPGAASGKSAGTQGDMEKADMVDGIKESVCWGPPPAASPLKSCEYHALCSRFQELLLLPEDYFMPPPKRSLCYCESCRKLRGDEAHRRRGEPPREYALPFGWCRFNLRVNPRLEAGTLTKKWHMAYHGSNVAAVRRVLDRGELGAGTASILSCRPLKGEPGVGFEEPGENCAPPREEQPPPVLLSPSLQYAGAETLASKVQFRDPKSQRTHQAQVAFQVCVRPGSYTPGPPSAALGEPPDPHFSPAELEWVTKEKGATLLCALLVRVE
Protein: Evasin P1180 (A0A023G6B6)
Organism: Amblyomma triste (Neotropical tick)
Function: Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3, CCL4, CCL8 and CCL18.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MARNWSFRVIFVSAMWCALLKFATLEEPKDGYDYTEGCPFVVLGNGTHAKPAGCSHLCNGAPETLDDNMECYNVTEEVAKRMTPDIPYTCWLGWCSKGECKRDNRTEVCYRGSERE
Protein: Actin-associated protein FAM107A (Down-regulated in renal cell carcinoma 1) (Protein TU3A) (O95990)
Organism: Homo sapiens (Human)
Function: Stress-inducible actin-binding protein that plays a role in synaptic and cognitive functions by modulating actin filamentous (F-actin) dynamics. Mediates polymerization of globular actin to F-actin. Also binds to, stabilizes and bundles F-actin. Involved in synaptic function by regulating neurite outgrowth in an actin-dependent manner and for the acquisition of hippocampus-dependent cognitive function, such as learning and long-term memory (By similarity). Plays a role in the actin and microtubule cytoskeleton organization; negatively regulates focal adhesion (FA) assembly promoting malignant glial cell migration in an actin-, microtubule- and MAP1A-dependent manner. Also involved in neuroblastoma G1/S phase cell cycle progression and cell proliferation inhibition by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a COMMD1- and actin-dependent manner. May play a role in tumor development.
Subcellular location: Nucleus {ECO:0000269|PubMed:10564580, ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}. Cell junction, focal adhesion {ECO:0000269|PubMed:20543869}. Cell projection, ruffle membrane {ECO:0000269|PubMed:20543869}. Synapse {ECO:0000250|UniProtKB:Q78TU8}. Note=Colocalizes with F-actin and COMMD1 in the nucleus (PubMed:28604741). Colocalizes with MAP1A along actin stress fibers and membrane ruffles (PubMed:20543869). {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}.
Interaction partners:
Sequence:
MYSEIQRERADIGGLMARPEYREWNPELIKPKKLLNPVKASRSHQELHRELLMNHRRGLGVDSKPELQRVLEHRRRNQLIKKKKEELEAKRLQCPFEQELLRRQQRLNQLEKPPEKEEDHAPEFIKVRENLRRIATLTSEEREL
Protein: Cation channel sperm-associated protein 1 (CatSper1) (hCatSper) (Q8NEC5)
Organism: Homo sapiens (Human)
Function: Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:16625279}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q91ZR5}. Note=Specifically located in the principal piece of the sperm tail. {ECO:0000269|PubMed:16625279}.
Interaction partners:
- Cation channel sperm-associated auxiliary subunit beta
- Cation channel sperm-associated auxiliary subunit gamma
- Cation channel sperm-associated auxiliary subunit delta
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated protein 3
- Cation channel sperm-associated protein 2
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated auxiliary subunit zeta
- Cation channel sperm-associated auxiliary subunit epsilon
- Heat shock-related 70 kDa protein 2
Sequence:
MDQNSVPEKAQNEADTNNADRFFRSHSSPPHHRPGHSRALHHYELHHHGVPHQRGESHHPPEFQDFHDQALSSHVHQSHHHSEARNHGRAHGPTGFGLAPSQGAVPSHRSYGEDYHDELQRDGRRHHDGSQYGGFHQQSDSHYHRGSHHGRPQYLGENLSHYSSGVPHHGEASHHGGSYLPHGPNPYSESFHHSEASHLSGLQHDESQHHQVPHRGWPHHHQVHHHGRSRHHEAHQHGKSPHHGETISPHSSVGSYQRGISDYHSEYHQGDHHPSEYHHGDHPHHTQHHYHQTHRHRDYHQHQDHHGAYHSSYLHGDYVQSTSQLSIPHTSRSLIHDAPGPAASRTGVFPYHVAHPRGSAHSMTRSSSTIRSRVTQMSKKVHTQDISTKHSEDWGKEEGQFQKRKTGRLQRTRKKGHSTNLFQWLWEKLTFLIQGFREMIRNLTQSLAFETFIFFVVCLNTVMLVAQTFAEVEIRGEWYFMALDSIFFCIYVVEALLKIIALGLSYFFDFWNNLDFFIMAMAVLDFLLMQTHSFAIYHQSLFRILKVFKSLRALRAIRVLRRLSFLTSVQEVTGTLGQSLPSIAAILILMFTCLFLFSAVLRALFRKSDPKRFQNIFTTIFTLFTLLTLDDWSLIYMDSRAQGAWYIIPILVIYIIIQYFIFLNLVITVLVDSFQTALFKGLEKAKQERAARIQEKLLEDSLTELRAAEPKEVASEGTMLKRLIEKKFGTMTEKQQELLFHYLQLVASVEQEQQKFRSQAAVIDEIVDTTFEAGEEDFRN