wanglab/gogpt-training-data huggingface dataset:
Protein: Transferrin receptor 2 (Transferrin receptor protein 2) (Q5MPX2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MMDSVTGLITGAAGGGAQANEGVEEGGGVRRRAPPIEMKLVPLEGSDVTLNSDITALMLQQHVNRRKAAVYLTLTGLLIFTTAFLLGYVAFRGMCHLCRSEPDNIPLSDALGDDRQPEEVVLYMAELREMLKKYLKEERIENTLRRVSRESHPPGSSEGNAIAREILQNLQNLGMDHTWTDSHYATLQFPSRTHRNTLWLVDSEGAELEEIRLDSEGYCAYSATGTATGGLVYVNYGRREDFDQLRVMGVSLNGSIAMVRVGGGVSFAEKVWLAQEAGHVGVLIYPDPADVPQDPRRLGLHSNAVISEHVHLGSGDPFTPGFPSFNHTQFPSTQSSGLPIIPAQPISANVAAKLLSQLSGAVCPRGWQGRLPYVQCVLGPGFSGVGVRQLKMAVYNSMKPVLLNNIFASIEGKVEPDHYIIIGAQRDAWGPGAVKSGVGTALLMELARTFSNMVENGFSPRRSLLFVSWDGGEFGNVGATEWLEGYLTMLHLKAVAYFSLDQAILGDDVLSVYSSPLLSHLIEGAIKQVEHPKHTGQSILSLVQRQGGWRNIVKPLYLNSGAYSFTAFGGVPAMQLHFTEDXRSYPFVNTQLDSVGRLQELLQGRLGSVGRAVGELVGLMVLKLAHDHILPLDVSCYSSSAQQLSSTLSQHAAQLQSRGLSPQWVFSARGDYSRAAKNLLEAIKNSDTQDEKLARLYNTRIXRVEYYFLSQYVSVVETPFRHVFLGRGDHTMSSLADHLNQLRLEPHRFDEARFRKQLALFTWTLQGAANALSGDVWNIDNPL
Protein: Probable protein phosphatase 2C 59 (AtPP2C59) (EC 3.1.3.16) (HopW1-1-interacting protein 2) (Protein phosphatase 2C WIN2) (PP2C WIN2) (Q8RXV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein phosphatase that modulates defense response to pathogenic bacteria, conferring resistance and promoting salicylic acid (SA) accumulation.
Interaction partners:
- Protein phosphatase 2C 32
Sequence:
MGYLNSVLSSSSQVHSDDGPVSGGGLSQNGKFSYGYASSPGKRSSMEDFYETRIDGVEGEIVGLFGVFDGHGGARAAEYVKQNLFSNLIRHPKFISDTTAAIADAYNQTDSEFLKSENSQNRDAGSTASTAILVGDRLLVANVGDSRAVICRGGNAIAVSRDHKPDQSDERQRIEDAGGFVMWAGTWRVGGVLAVSRAFGDRLLKQYVVADPEIQEEKVDSSLEFLILASDGLWDVVSNEEAVGMIKAIEDPEEGAKRLMMEAYQRGSADNITCVVVRFFSDQAGGIGSSSTNIPIDHGIVPDRISGDSST
Protein: Ribosomal protein S3 (E9PPU1)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
Interaction partners:
Sequence:
MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA
Protein: Leukosialin (GPL115) (Galactoglycoprotein) (GALGP) (Leukocyte sialoglycoprotein) (Sialophorin) (CD antigen CD43) [Cleaved into: CD43 cytoplasmic tail (CD43-ct) (CD43ct)] (P16150)
Organism: Homo sapiens (Human)
Function: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (By similarity). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells. Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR. Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin. Acts as a T-cell counter-receptor for SIGLEC1 (By similarity).
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P13838}. Cell projection, uropodium {ECO:0000250|UniProtKB:P15702}. Note=Localizes to the uropodium and microvilli via its interaction with ERM proteins (EZR, RDX and MSN). {ECO:0000250|UniProtKB:P13838, ECO:0000250|UniProtKB:P15702}.; SUBCELLULAR LOCATION: [CD43 cytoplasmic tail]: Nucleus {ECO:0000269|PubMed:15003504}. Nucleus, PML body {ECO:0000250|UniProtKB:P15702}. Note=The sumoylated form localizes to the PML body. {ECO:0000250|UniProtKB:P15702}.
Interaction partners:
- Radixin
- Receptor-type tyrosine-protein phosphatase C
- Sialoadhesin
- E-selectin
- Intercellular adhesion molecule 1
- Ezrin
- P-selectin glycoprotein ligand 1
- Moesin
- Basigin
- T-cell surface glycoprotein CD5
Sequence:
MATLLLLLGVLVVSPDALGSTTAVQTPTSGEPLVSTSEPLSSKMYTTSITSDPKADSTGDQTSALPPSTSINEGSPLWTSIGASTGSPLPEPTTYQEVSIKMSSVPQETPHATSHPAVPITANSLGSHTVTGGTITTNSPETSSRTSGAPVTTAASSLETSRGTSGPPLTMATVSLETSKGTSGPPVTMATDSLETSTGTTGPPVTMTTGSLEPSSGASGPQVSSVKLSTMMSPTTSTNASTVPFRNPDENSRGMLPVAVLVALLAVIVLVALLLLWRRRQKRRTGALVLSRGGKRNGVVDAWAGPAQVPEEGAVTVTVGGSGGDKGSGFPDGEGSSRRPTLTTFFGRRKSRQGSLAMEELKSGSGPSLKGEEEPLVASEDGAVDAPAPDEPEGGDGAAP
Protein: Pyridoxine 5'-phosphate oxidase (PNP oxidase) (PNPOx) (EC 1.4.3.5) (Pyridoxal 5'-phosphate synthase) (P9WIJ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the oxidation of pyridoxine 5'-phosphate (PNP) into pyridoxal 5'-phosphate (PLP). Unlike many PNPOx enzymes, Rv2607 does not recognize pyridoxamine 5'-phosphate (PMP) as a substrate.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit PdxT
- Pyridoxal 5'-phosphate synthase subunit PdxS
- F420-dependent glucose-6-phosphate dehydrogenase
- Conserved protein
- 6,7-dimethyl-8-ribityllumazine synthase
Sequence:
MDDDAQMVAIDKDQLARMRGEYGPEKDGCGDLDFDWLDDGWLTLLRRWLNDAQRAGVSEPNAMVLATVADGKPVTRSVLCKILDESGVAFFTSYTSAKGEQLAVTPYASATFPWYQLGRQAHVQGPVSKVSTEEIFTYWSMRPRGAQLGAWASQQSRPVGSRAQLDNQLAEVTRRFADQDQIPVPPGWGGYRIAPEIVEFWQGRENRMHNRIRVANGRLERLQP
Protein: Gap junction beta-2 protein (Connexin-26) (Cx26) (Q00977)
Organism: Mus musculus (Mouse)
Function: Structural component of gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15692151, ECO:0000269|PubMed:19864490}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P29033}. Cell junction, gap junction {ECO:0000269|PubMed:15692151, ECO:0000269|PubMed:19864490}. Note=Colocalizes with GJB4 at gap junction plaques in the cochlea. {ECO:0000269|PubMed:15692151}.
Interaction partners:
- Gap junction beta-6 protein
- Gap junction beta-1 protein
- Gap junction alpha-5 protein
- Homeobox protein NANOG
- Gap junction beta-4 protein
- Gap junction alpha-1 protein
- Gap junction alpha-4 protein
- Gap junction delta-3 protein
- Gap junction alpha-3 protein
- Gap junction beta-3 protein
Sequence:
MDWGTLQSILGGVNKHSTSIGKIWLTVLFIFRIMILVVAAKEVWGDEQADFVCNTLQPGCKNVCYDHHFPISHIRLWALQLIMVSTPALLVAMHVAYRRHEKKRKFMKGEIKNEFKDIEEIKTQKVRIEGSLWWTYTTSIFFRVIFEAVFMYVFYIMYNGFFMQRLVKCNAWPCPNTVDCFISRPTEKTVFTVFMISVSGICILLNITELCYLFVRYCSGKSKRPV
Protein: Fms-related tyrosine kinase 3 ligand (Flt3 ligand) (Flt3L) (SL cytokine) (P49772)
Organism: Mus musculus (Mouse)
Function: Stimulates the proliferation of early hematopoietic cells by activating FLT3. Synergizes well with a number of other colony stimulating factors and interleukins.
Subcellular location: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted. Note=Biologically active.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted. Note=Inactive.
Interaction partners:
- Receptor-type tyrosine-protein kinase FLT3
- Ubiquitin-like protein FUBI
- Kit ligand
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS19
Sequence:
MTVLAPAWSPNSSLLLLLLLLSPCLRGTPDCYFSHSPISSNFKVKFRELTDHLLKDYPVTVAVNLQDEKHCKALWSLFLAQRWIEQLKTVAGSKMQTLLEDVNTEIHFVTSCTFQPLPECLRFVQTNISHLLKDTCTQLLALKPCIGKACQNFSRCLEVQCQPDSSTLLPPRSPIALEATELPEPRPRQLLLLLLLLLPLTLVLLAAAWGLRWQRARRRGELHPGVPLPSHP
Protein: Serum paraoxonase/arylesterase 1 (PON 1) (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Aromatic esterase 1) (A-esterase 1) (Serum aryldialkylphosphatase 1) (P27170)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Apolipoprotein A-I
- Clusterin
- Apolipoprotein C-I
- Cholesteryl ester transfer protein
- Apolipoprotein B
- Phosphatidylcholine-sterol acyltransferase
- Phospholipid transfer protein
- Apolipoprotein A-II
- Apolipoprotein M
- Hepatic triacylglycerol lipase
Sequence:
MAKLTALTLLGLGLALFDGQKSSFQTRFNVHREVTPVELPNCNLVKGIDNGSEDLEILPNGLAFISAGLKYPGIMSFDPDKPGKILLMDLNEKDPVVLELSITGSTFDLSSFNPHGISTFTDEDNIVYLMVVNHPDSKSTVELFKFQEKEKSLLHLKTIRHKLLPSVNDIVAVGPEHFYATNDHYFIDPYLKSWEMHLGLAWSFVTYYSPNDVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPVTGDLWVGCHPNGMRIFYYDPKNPPASEVLRIQDILSKEPKVTVAYAENGTVLQGSTVAAVYKGKMLVGTVFHKALYCELSQAN
Protein: Glutaredoxin-C6 (AtGrxC6) (Protein ROXY 21) (Q8L9S3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- AT5g23340/MKD15_20
- Probable LRR receptor-like serine/threonine-protein kinase At4g37250
- At1g66080
- Probable plastid-lipid-associated protein 10, chloroplastic
- At4g27652
- At4g27654
- GEM-like protein 6
Sequence:
MMQELGLQRFSNDVVRLDLTPPSQTSSTSLSIDEEESTEAKIRRLISEHPVIIFSRSSCCMCHVMKRLLATIGVIPTVIELDDHEVSSLPTALQDEYSGGVSVVGPPPAVFIGRECVGGLESLVALHLSGQLVPKLVQVGALWV
Protein: Type-1 fimbrial protein, A chain (Type-1A pilin) (P04128)
Organism: Escherichia coli (strain K12)
Function: Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
Subcellular location: Fimbrium.
Interaction partners:
- Chaperone protein FimC
- Fimbrin-like protein FimI
- Type 1 fimbrin D-mannose specific adhesin
- Probable fimbrial chaperone SfmC
- Uncharacterized fimbrial-like protein SfmH
- Protein FimF
- Uncharacterized fimbrial-like protein SfmF
- Probable autotransporter YfaL
- Type 1 fimbriae regulatory protein FimB
- Outer membrane usher protein FimD
Sequence:
MKIKTLAIVVLSALSLSSTAALAAATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQVRTASLAQEGATSSAVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSATNVGVQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANADATFKVQYQ
Protein: Zinc-coordinating transcription factor (Q5ANF0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- WD-repeat containing protein
- RNA-processing protein
- Transcriptional regulator HMO1
- Stb3p
- Transcriptional regulator IFH1
- Histone acetyltransferase
- Rab proteins geranylgeranyltransferase
Sequence:
MFNTKIFENTGSSGSTTAMNIPVQSEPSNTNSAQPQPIDITFNHRPSVFNNSRFRRDSVAHSQGMGGISWGSVTIGSWLKDEVMMASGGNNNHLNPHYHPTQSHNNQSSYPNYSQQQQQQQQQSQHQQNLINPRRGSFRTSNHPNLSPHLQTSYLPELEADYCKDYNCCGELLPTLHDLLRHYEEAHISASPPPDQNHFILNSRNRNNYNNAHNVMETVSTTDVFLNNNHNNHHAPTMHPSATTTNYNGNNSFGNQQAHQILQQHDQQQQQQQQQQQQQQQNQNQLHHNSDNYQHSSQSTSRQPGQQFGQGNSHFGPQQQSPSSGSQGGGTPMQTDEDDMYIDDPARHLYVMENEENKPFKCPVIGCDKTYKNQNGLKYHRQHGHQGQNLRENPDGTISIIDPDSNCPYLDNAALEKDKPYRCEVCGKRYKNLNGLKYHRGHTTH
Protein: FXYD domain-containing ion transport regulator 6 (Phosphohippolin) (Q9H0Q3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q91XV6}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit beta-1
- FXYD domain-containing ion transport regulator 5
- Sodium/potassium-transporting ATPase subunit alpha-2
Sequence:
MELVLVFLCSLLAPMVLASAAEKEKEMDPFHYDYQTLRIGGLVFAVVLFSVGILLILSRRCKCSFNQKPRAPGDEEAQVENLITANATEPQKAEN
Protein: Proteasome activator complex subunit 3 (Activator of multicatalytic protease subunit 3) (Proteasome activator 28 subunit gamma) (V9HWJ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY
Protein: Nucleoporin (Q38D32)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRCTASGLPPSFITAVRSGFDAFVHLQRHRFASYVELPDGQPREMKALWGEQTSAAATPETLCQWSDLFFLRLKAVSDEVPFDLTVGVVWELVSIVLGVLEGCGDDGLVVNGLYVDWYRSRFVHPEGVEQILNELSSSTPGKEGVLMEIVGPCMVAMQRCFLAGLFPISAQLLSTFMEYLRTFSLDIFSAEEESALADVIHLLLHPPASGVVHAAWADTANRLLVDCKRILGNANRKGGVAMQVAQQLKSLCLDLLLMVSGDAALVLHMCCLLNLDVVDYVAAVCVVCGPPMTLQQMHHLFRTAWDSWEGTVKGPWYVAVVEQLLGCRCVADVVGVMQFVRDAVRRNEHIQSVPATGRLKGQDGDSNFVSSPVSSIASLGEDVGDGSEDVSGVYGEDVSITDSGDDHLLGDAVELPMGGKSLRGFSLLFMAAHVADICAPPMGAPVDQISVTFTRNELIRDYVELFRWHPLLWRTAATYTVYSPFMNPAELYRTVIGQTSNAVRDRYTSLSLQTFIQTSWEDNSPFQVALRRLLHDKYPASATVSRWISAVDFYRHKAVDVLNRKLIREKMTCGDTASAVWLALESQQSKSVQVHFEEILRTPNALLSDEVQRVGQALSSSFISVDASQNLRMLNVLCACAALFEYRKACASAQRGGGSSASLPVGVVQHLLRAADRVLQCAASVRMHPEVILSVLDRAASIAINLPRSLRPRTLLPRLSSALELMFAAHSGNLASYNVKAAPIREKLMRLL
Protein: Pigment epithelium-derived factor (PEDF) (Cell proliferation-inducing gene 35 protein) (EPC-1) (Serpin F1) (P36955)
Organism: Homo sapiens (Human)
Function: Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.
Subcellular location: Secreted {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Enriched in stage I melanosomes.
Interaction partners:
- Plasminogen
- Low-density lipoprotein receptor-related protein 6
- Low-density lipoprotein receptor-related protein 5
- Alpha-2-macroglobulin
- Albumin
- Fibronectin
- Vitronectin
- Carboxypeptidase B2
- Tissue-type plasminogen activator
- Patatin-like phospholipase domain-containing protein 2
Sequence:
MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP
Protein: PHD and RING finger domain-containing protein 1 (Q9P1Y6)
Organism: Homo sapiens (Human)
Interaction partners:
- DNA
- PX domain-containing protein kinase-like protein
- B-cell scaffold protein with ankyrin repeats
Sequence:
MDDDSLDELVARSPGPDGHPQVGPADPAGDFEESSVGSSGDSGDDSDSEHGDGTDGEDEGASEEEDLEDRSGSEDSEDDGETLLEVAGTQGKLEAAGSFNSDDDAESCPICLNAFRDQAVGTPENCAHYFCLDCIVEWSKNANSCPVDRTLFKCICIRAQFGGKILRKIPVENTKASEEEEDPTFCEVCGRSDREDRLLLCDGCDAGYHMECLDPPLQEVPVDEWFCPECAAPGVVLAADAGPVSEEEVSLLLADVVPTTSRLRPRAGRTRAIARTRQSERVRATVNRNRISTARRVQHTPGRLGSSLLDEAIEAVATGLSTAVYQRPLTPRTPARRKRKTRRRKKVPGRKKTPSGPSAKSKSSATRSKKRQHRVKKRRGKKVKSEATTRSRIARTLGLRRPVHSSCIPSVLKPVEPSLGLLRADIGAASLSLFGDPYELDPFDSSEELSANPLSPLSAKRRALSRSALQSHQPVARPVSVGLSRRRLPAAVPEPDLEEEPVPDLLGSILSGQSLLMLGSSDVIIHRDGSLSAKRAAPVSFQRNSGSLSRGEEGFKGCLQPRALPSGSPAQGPSGNRPQSTGLSCQGRSRTPARTAGAPVRLDLPAAPGAVQARNLSNGSVPGFRQSHSPWFNGTNKHTLPLASAASKISSRDSKPPCRSVVPGPPLKPAPRRTDISELPRIPKIRRDDGGGRRDAAPAHGQSIEIPSACISRLTGREGTGQPGRGTRAESEASSRVPREPGVHTGSSRPPAPSSHGSLAPLGPSRGKGVGSTFESFRINIPGNMAHSSQLSSPGFCNTFRPVDDKEQRKENPSPLFSIKKTKQLRSEVYDPSDPTGSDSSAPGSSPERSGPGLLPSEITRTISINSPKAQTVQAVRCVTSYTVESIFGTEPEPPLGPSSAMSKLRGAVAAEGASDTEREEPTESQGLAARLRRPSPPEPWDEEDGASCSTFFGSEERTVTCVTVVEPEAPPSPDVLQAATHRVVELRPPSRSRSTSSSRSRKKAKRKRVSREHGRTRSGTRSESRDRSSRSASPSVGEERPRRQRSKAKSRRSSSDRSSSRERAKRKKAKDKSREHRRGPWGHSRRTSRSRSGSPGSSSYEHYESRKKKKRRSASRPRGRECSPTSSLERLCRHKHQRERSHERPDRKESVAWPRDRRKRRSRSPSSEHRAREHRRPRSREKWPQTRSHSPERKGAVREASPAPLAQGEPGREDLPTRLPALGEAHVSPEVATADKAPLQAPPVLEVAAECEPDDLDLDYGDSVEAGHVFDDFSSDAVFIQLDDMSSPPSPESTDSSPERDFPLKPALPPASLAVAAIQREVSLMHDEDPSQPPPLPEGTQEPHLLRPDAAEKAEAPSSPDVAPAGKEDSPSASGRVQEAARPEEVVSQTPLLRSRALVKRVTWNLQESESSAPAEDRAPRAPLHRPQKPREGAWDMEDVAPTGVRQVFSELPFPSHVLPEPGFPDTDPSQVYSPGLPPAPAQPSSIPPCALVSQPTVQFILQGSLPLVGCGAAQTLAPVPAALTPASEPASQATAASNSEEKTPAPRLAAEKTKKEEYMKKLHMQERAVEEVKLAIKPFYQKREVTKEEYKDILRKAVQKICHSKSGEINPVKVANLVKAYVDKYRHMRRHKKPEAGEEPPTQGAEG
Protein: Dynein beta chain, ciliary protein (Q9LIF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA-directed RNA polymerase I subunit 2
- DNA binding / DNA-directed RNA polymerase
- DNA-directed RNA polymerase subunit
- RNApolymerase 14 kDa subunit
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase family protein
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase subunit
- SIN-like family protein
Sequence:
MGQQLRRAVGKIKEVERSSPSRVSIDRRSLPTEELSAVKSSPSTAAVDGVSDKGRRTSEDNVLEERDPKYDTMLNQMVGRIKAKPGGKAEMGEASVVETSKRPLPKLRNTTPESTRYEENPVPQGTLNVAQVRHIMLLFQGKSQDHHGPMGVNEIAEKYRIDVSQVQKITQFLSLPQEITDKQKKQYE
Protein: Centromere protein H (CENP-H) (Interphase centromere complex protein 35) (Q9H3R5)
Organism: Homo sapiens (Human)
Function: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associates with active centromere-kinetochore complexes throughout the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA and CENPC during both interphase and metaphase.
Interaction partners:
- Centromere protein Q
- Centromere protein U
- Centromere protein K
- Centromere protein T
- Centromere protein C
- Centromere protein L
- Centromere protein I
- Centromere protein N
- Centromere protein P
- Centromere protein O
Sequence:
MEEQPQMQDADEPADSGGEGRAGGPPQVAGAQAACSEDRMTLLLRLRAQTKQQLLEYKSMVDASEEKTPEQIMQEKQIEAKIEDLENEIEEVKVAFEIKKLALDRMRLSTALKKNLEKISRQSSVLMDNMKHLLELNKLIMKSQQESWDLEEKLLDIRKKRLQLKQASESKLLEIQTEKNKQKIDLDSMENSERIKIIRQNLQMEIKITTVIQHVFQNLILGSKVNWAEDPALKEIVLQLEKNVDMM
Protein: Actin-binding protein WASF1 (Protein WAVE-1) (Wiskott-Aldrich syndrome protein family member 1) (WASP family protein member 1) (Q5BJU7)
Organism: Rattus norvegicus (Rat)
Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). Also involved in the regulation of mitochondrial dynamics (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92558}. Synapse {ECO:0000269|PubMed:17304222}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q92558}. Note=Dot-like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas. Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2. In neurons, colocalizes with activated NTRK2 after BDNF addition in endocytic sites through the association with TMEM108 (By similarity). {ECO:0000250|UniProtKB:Q8R5H6, ECO:0000250|UniProtKB:Q92558}.
Interaction partners:
- Abl-interactor 2
- Nck-associated protein 1
- Cytoplasmic FMR1-interacting protein
- Abl interactor 1
- Cytoplasmic FMR1-interacting protein
- NCK associated protein 1 like
- Protein BRICK1
- Wiskott-Aldrich syndrome protein family member
- BAR/IMD domain-containing adapter protein 2
- Actin-related protein 2/3 complex subunit 2
Sequence:
MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNVLTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDADLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLSRAEERVLVRPHEPPPPPPMHAAGDARPTPTCVSSAAGLIENRPQSPAAGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPAPALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVTVAALAHPPSGLHPTPSPAPGPHAPLMPPSPPSQVLPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE
Protein: Replication factor C subunit 4 (Replication factor C4) (O94449)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Replication factor C subunit 5
- Replication factor C subunit 3
- Replication factor C subunit 2
- Checkpoint protein rad17
- Replication factor C subunit 1
- Telomere length regulation protein elg1
- Proliferating cell nuclear antigen
- Chromosome transmission fidelity protein 18
- Sister chromatid cohesion protein dcc1
- DNA repair protein rad9
Sequence:
MSNAVSSSVFGEKNNSVAYELPWVEKYRPIVLDDIVGNEETIDRLKVIAKEGNMPHLVISGMPGIGKTTSILCLAHALLGPAYKEGVLELNASDERGIDVVRNRIKAFAQKKVILPPGRHKIIILDEADSMTAGAQQALRRTMEIYSNTTRFALACNQSNKIIEPIQSRCAILRYSRLTDQQVLQRLLNICKAEKVNYTDDGLAALIMTAEGDMRQAVNNLQSTVAGFGLVNGENVFRVADQPSPVAIHAMLTACQSGNIDVALEKLQGIWDLGFSAVDIVTNMFRVVKTMDSIPEFSRLEMLKEIGQTHMIILEGVQTLLQLSGLVCRLAKSQMKPESFII
Protein: Beta-conglycinin alpha subunit 1 (CG-alpha-1) (Beta-conglycinin alpha subunit) (allergen Gly m 5) (P0DO16)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.
Subcellular location: Vacuole, aleurone grain {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:15447650}. Protein storage vacuole. Note=Localizes in protein storage vacuoles in cotyledons of developing and mature beans (PubMed:15447650). Synthesized and assembled into trimers in the endoplasmic reticulum, and transported to the protein storage vacuoles by the dense vesicles (PubMed:15447650). {ECO:0000269|PubMed:15447650}.
Interaction partners:
- Glycinin G2
- Glycinin G1
- Glycinin G3
- Kunitz-type trypsin inhibitor KTI1
- Uncharacterized protein
- Kunitz trypsin inhibitor
- Cupin type-1 domain-containing protein
- Glycinin G5
- Maturing seed protein
- Seed maturation protein PM31
Sequence:
MMRARFPLLLLGLVFLASVSVSFGIAYWEKENPKHNKCLQSCNSERDSYRNQACHARCNLLKVEKEECEEGEIPRPRPRPQHPEREPQQPGEKEEDEDEQPRPIPFPRPQPRQEEEHEQREEQEWPRKEEKRGEKGSEEEDEDEDEEQDERQFPFPRPPHQKEERKQEEDEDEEQQRESEESEDSELRRHKNKNPFLFGSNRFETLFKNQYGRIRVLQRFNQRSPQLQNLRDYRILEFNSKPNTLLLPNHADADYLIVILNGTAILSLVNNDDRDSYRLQSGDALRVPSGTTYYVVNPDNNENLRLITLAIPVNKPGRFESFFLSSTEAQQSYLQGFSRNILEASYDTKFEEINKVLFSREEGQQQGEQRLQESVIVEISKEQIRALSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKFFEITPEKNPQLRDLDIFLSIVDMNEGALLLPHFNSKAIVILVINEGDANIELVGLKEQQQEQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSNLNFFAIGINAENNQRNFLAGSQDNVISQIPSQVQELAFPGSAQAVEKLLKNQRESYFVDAQPKKKEEGNKGRKGPLSSILRAFY