wanglab/gogpt-training-data huggingface dataset:
Protein: Astrotactin-2 (O75129)
Organism: Homo sapiens (Human)
Function: Mediates recycling of the neuronal cell adhesion molecule ASTN1 to the anterior pole of the cell membrane in migrating neurons. Promotes ASTN1 internalization and intracellular transport of endocytosed ASTN1 (By similarity). Selectively binds inositol-4,5-bisphosphate, inositol-3,4,5-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, suggesting it is recruited to membranes that contain lipids with a phosphoinositide headgroup (Ref.6).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q80Z10}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80Z10}. Perikaryon {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q80Z10}. Early endosome {ECO:0000250|UniProtKB:Q80Z10}. Late endosome {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q80Z10}. Note=Integral membrane protein not detected at the cell membrane. Detected in cytoplasmic vesicles in the cell cortex, close to the anterior pole of migrating neurons. Detected at the base of the leading process in migrating neurons. {ECO:0000250|UniProtKB:Q80Z10}.
Interaction partners:
- Mirror-image polydactyly gene 1 protein
- Tyrosine-protein kinase FRK
- Protein hinderin
- ADAMTS-like protein 3
- WD repeat-containing and planar cell polarity effector protein fritz homolog
- Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2
- Importin subunit alpha-6
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- F-box only protein 40
- Contactin-4
Sequence:
MAAAGARLSPGPGSGLRGRPRLCFHPGPPPLLPLLLLFLLLLPPPPLLAGATAAASREPDSPCRLKTVTVSTLPALRESDIGWSGARAGAGAGTGAGAAAAAASPGSPGSAGTAAESRLLLFVRNELPGRIAVQDDLDNTELPFFTLEMSGTAADISLVHWRQQWLENGTLYFHVSMSSSGQLAQATAPTLQEPSEIVEEQMHILHISVMGGLIALLLLLLVFTVALYAQRRWQKRRRIPQKSASTEATHEIHYIPSVLLGPQARESFRSSRLQTHNSVIGVPIRETPILDDYDCEEDEEPPRRANHVSREDEFGSQVTHTLDSLGHPGEEKVDFEKKAAAEATQETVESLMQKFKESFRANTPIEIGQLQPPLRSTSAGKRKRRSKSRGGISFGRAKGTSGSEADDETQLTFYTEQYRSRRRSKGLLKSPVNKTALTLIAVSSCILAMVCGSQMSCPLTVKVTLHVPEHFIADGSSFVVSEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPETGECSCHEGYAPDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKSFVVPPVELSINPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNGGCTRNFKCVSDRQVDSSGCVCPEELKPMKDGSGCYDHSKGIDCSDGFNGGCEQLCLQQTLPLPYDATSSTIFMFCGCVEEYKLAPDGKSCLMLSDVCEGPKCLKPDSKFNDTLFGEMLHGYNNRTQHVNQGQVFQMTFRENNFIKDFPQLADGLLVIPLPVEEQCRGVLSEPLPDLQLLTGDIRYDEAMGYPMVQQWRVRSNLYRVKLSTITLAAGFTNVLKILTKESSREELLSFIQHYGSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQKETTELGSKKELKSMPFITYLSGLLTAQMLSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDNGTKEAFKSALMSSYWCSGKGDVIDDWCRCDLSAFDANGLPNCSPLLQPVLRLSPTVEPSSTVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLSFADDLLSGLGTSCVAAGRSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHSELSTVTLRTACPLVDDNKAEEIADKIYNLYNGYTSGKEQQMAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGPRKAHLILRRLERVSSHCSSLLRSAYIQSRVETVPYLFCRSEEVRPAGMVWYSILKDTKITCEEKMVSMARNTYGESKGR
Protein: Probable asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase) (P78753)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Argininosuccinate synthase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Adenylosuccinate synthetase
- Aspartokinase
- Glutamate synthase
- Asparagine synthetase domain-containing protein C4F6.11c
- Multifunctional protein ura1
- CTP synthase
- Glutamine synthetase
Sequence:
MCGILAVHHVAEDIEAFKPKALHLSKQLRHRGPDWSGKAIRNQTILCHERLAIVGVESGAQPLVSDDGKLVLTVNGEIYNHLKLRENLKGNYKFKTYSDCEVILYLYREHGPACANMLDGMFSWVLYDQDKDKVVAARDPIGITTLYQGFSSDSPDTAYFASELKALHPVCDKIIAFPPGHYYDSETKQTVRYFKPSWWDENKIPSNPVDYKLLRETLEASVRKRLMAEVPYGVLLSGGLDSSLIASIAARETEKLANSTSQSEEARTITAWPKLHSFAIGLPGSPDLLAARKVADFLHTFHHEHTFTIDEGLDALRDVIYHLETYDVTTIRASTPMYLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFGNAPSREAFHSECVRRVKNLHLSDCLRANKSTMAWGLEARVPFLDKDFLEVALNIDPEEKMYINGRKEKYILRKAFDTTHDSSLQPYLPQDILWRQKEQFSDGVGYSWIDALKDTAELCISDDEFALPRREWGDDIPTTKEAFWYRKLFDEIFPRQCADTVMRWVPKAEWGCPEDPSGRYQAGHVAALK
Protein: Calcium-dependent secretion activator 2 (Calcium-dependent activator protein for secretion 2) (CAPS-2) (Q86UW7)
Organism: Homo sapiens (Human)
Function: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles (By similarity).
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Synapse. Cell projection, cilium {ECO:0000269|PubMed:38538594}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:38538594}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:38538594}. Note=Membrane-associated to vesicles. Strongly enriched in synaptic fra,ctions. Probably localizes to different vesicles compared to CADPS. Enriched on vesicular structures in the parallel fiber terminal of granule cells that are distinct from synaptic vesicles.
Interaction partners:
- Autism susceptibility gene 2 protein
- Pro-neuregulin-3, membrane-bound isoform
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Sequence:
MLDPSSSEEESDEGLEEESRDVLVAAGSSQRAPPAPTREGRRDAPGRAGGGGAARSVSPSPSVLSEGRDEPQRQLDDEQERRIRLQLYVFVVRCIAYPFNAKQPTDMARRQQKLNKQQLQLLKERFQAFLNGETQIVADEAFCNAVRSYYEVFLKSDRVARMVQSGGCSANDFREVFKKNIEKRVRSLPEIDGLSKETVLSSWIAKYDAIYRGEEDLCKQPNRMALSAVSELILSKEQLYEMFQQILGIKKLEHQLLYNACQLDNADEQAAQIRRELDGRLQLADKMAKERKFPKFIAKDMENMYIEELRSSVNLLMANLESLPVSKGGPEFKLQKLKRSQNSAFLDIGDENEIQLSKSDVVLSFTLEIVIMEVQGLKSVAPNRIVYCTMEVEGEKLQTDQAEASRPQWGTQGDFTTTHPRPVVKVKLFTESTGVLALEDKELGRVILYPTSNSSKSAELHRMVVPKNSQDSDLKIKLAVRMDKPAHMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEGYTVDYTDPHPGLQGGCMFFNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSYKPVPAIQTQKLNPKGGTLHADAQLSGKDADRFQKHGMDEFISANPCKLDHAFLFRILQRQTLDHRLNDSYSCLGWFSPGQVFVLDEYCARYGVRGCHRHLCYLAELMEHSENGAVIDPTLLHYSFAFCASHVHGNRPDGIGTVSVEEKERFEEIKERLSSLLENQISHFRYCFPFGRPEGALKATLSLLERVLMKDIATPIPAEEVKKVVRKCLEKAALINYTRLTEYAKIEETMNQASPARKLEEILHLAELCIEVLQQNEEHHAEGREAFAWWPDLLAEHAEKFWALFTVDMDTALEAQPQDSWDSFPLFQLLNNFLRNDTLLCNGKFHKHLQEIFVPLVVRYVDLMESSIAQSIHRGFEQETWQPVKNIANSLPNVALPKVPSLPLNLPQIPNISTASWMPSLYESTNGSATSEDLFWKLDALQMFVFDLHWPEQEFAHHLEQRLKLMASDMLEACVKRTRTAFELKLQKASKTTDLRIPASVCTMFNVLVDAKKQSTKLCALDGGQEQQYHSKIDDLIDNSVKEIISLLVSKFVSVLEGVLSKLSRYDEGTFFSSILSFTVKAAAKYVDVPKPGMDLADTYIMFVRQNQDILREKVNEEMYIEKLFDQWYSSSMKVICVWLTDRLDLQLHIYQLKTLIKIVKKTYRDFRLQGVLEGTLNSKTYDTVHRRLTVEEATASVSEGGGLQGITMKDSDEEEEG
Protein: At5g50330 (Protein kinase superfamily protein) (Q0WSU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable disease resistance protein At1g62630
- Probable disease resistance protein At1g12290
- Disease resistance RPP8-like protein 3
- Probable disease resistance protein At1g59620
- Putative disease resistance protein At3g14460
- Putative disease resistance RPP13-like protein 2
- Disease resistance protein At4g27190
- Putative disease resistance RPP13-like protein 1
Sequence:
MHGFDFKEIQEKISDSFRPWQRSFQFWVRATNIYTGYKVFQLRVSLVKDAKKQEEMWERQHEQAADKIYFMCSDLGGFFLKIAQLLAKPDMAPAAWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQVHRAIVKGNKMNVVVKVQHPGIERLMMTDIRNLQLFALYMQRTDIKFDLHSITKEMEKQIGYEFDFKREANAMERIRCFLYENNKKSPVLVPRVLRDMVTKRVLVMEYINGIPILSIGDEMAKRGINPHGKIAEAAKHNILNSLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKELPNKLRLGYANLVIAMADNNASRVSQSFWEMGLHTVAKCENEQQELLRLAQTLFDTKMPTGQTVLQPFSDDSSIKKIAVETFPEELFSVLRTVVLLRGLSVGMGVNYSCAEQWRAMAEEALLASGRVTRDGKERSRRRASLRRLRTGS
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q8I3I0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Pre-mRNA-processing protein 45, putative
- Pre-mRNA-splicing factor CEF1, putative
- U5 small nuclear ribonucleoprotein component, putative
- Pre-mRNA-processing-splicing factor 8, putative
- Intron-binding protein aquarius, putative
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor BUD31, putative
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor CWC15, putative
- Pre-mRNA-splicing factor CWF7, putative
Sequence:
MFTLCKGYSEDEDEEEVKDIIDNLKEQKKSFEEKINYYKLKGNIERSHITIYTNLGEFQVELYWYHSPKTCLNFYTLCTMGYYDNTIFHRVIPDYIIQGGDPTGTGKGGKSIYGEYFEDEINTELKHTGAGILSMSNNGPNTNGSQFFITLCPLPHLDGKHTIFARVSKNMTCIENIASVQTTATNKPIFDVKILRTSTAVNVD
Protein: Protein-lysine N-methyltransferase EFM2 (EC 2.1.1.-) (Elongation factor methyltransferase 2) (P38347)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-613' and methylates elongation factor 3A (YEF3).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein-lysine N-methyltransferase EFM4
- Protein-lysine N-methyltransferase EFM3
- Histidine protein methyltransferase 1
- Vacuolar protein sorting-associated protein 28
- Protein-lysine N-methyltransferase EFM1
- Ribosomal lysine N-methyltransferase 5
- 25S rRNA
- 25S rRNA
- Protein N-terminal and lysine N-methyltransferase EFM7
- 25S rRNA
Sequence:
MFDPLDLYTPDDIQVEALQFNLAEREPKDPCSPQRDEILTAVDEEESDDDDTIIDNLDLPSVKYAPPEVILCILILLKPDRQVNFNQETGKNKSVLEVCKSHGLEPDLLKRLLTWYTEEWPNKRLNSLEKICNKIPMLRFTVSKELLLGYYTSVLKKYNNSCGLNEEIIQELLKELSSRISENCGRTAQPSIVRYFELRNLSTSIPLHEPSLTADNLGWKTWGSSLILSQLVVDHLDYLHTTNVNMLANSDIKQIKVLELGAGTGLVGLSWALKWKELYGTENIEIFVTDLPEIVTNLKKNVSLNNLGDFVQAEILDWTNPHDFIDKFGHENEFDVILIADPIYSPQHPEWVVNMISKFLAASGTCHLEIPLRAKYAKEREVLKLLLKESDLKVVEERHSEGVDDWGAVKYLYRQIVRN
Protein: C4-dicarboxylate TRAP transporter small permease protein DctQ (Q9HU17)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in C4-dicarboxylates uptake.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:O07837}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- C4-dicarboxylate TRAP transporter large permease protein DctM
- C4-dicarboxylate-binding periplasmic protein DctP
- TRAP transporter small permease protein
- TRAP transporter large permease protein
- Probable C4-dicarboxylate-binding periplasmic protein
- Probable c4-dicarboxylate-binding protein
- Probable transcriptional regulator
- Bifunctional NAD
- Probable transporter
- FixH family protein
Sequence:
MHALARVWARLEEGLIAFLLAAMTLVTFVYVVLNNLYTLLYDLADLWEGGNETLLAIGDGVLTLAQEMTWSNALTKALFAWLIFLGIAYGVRTAGHLGVDVLVKLASRPVQRVLGVIACLACLGYAGLLCVASYDWVKTLFIAGIGAEDLDHFGIRQWHIGLIVPVGFALVFIRFAEILVRILRNRQTGLGLADEAADALKLTEHEEPKA
Protein: Cytochrome P450 (Q9FHC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g52280
- Putative ion channel POLLUX-like 2
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
Sequence:
MAMIIGLLEIFIAFIFFFVYQCFSLHKKTPKHMVMNWPVLGMLPGVLFQIPRIYDFVTEALEAENMTGCFIGPWLSGTDILLTVDPVNIQYILSSNFVNYPKGKKFNKIFEFLGDGIFNVDSGLWEDMRNSSHAIFSHQDFQSFSVSTSVSKLSQGLVPILDNAVEKHILVDLQDLFQRFLFDTSSTLMAGYDPKSLSVEMPKVEFADAMDGVADAMFYRHLKPAFLWSIQSWIGVGIEKKMRRGLDVFDQMLGKIISAKREEIKNHGIHDSKGEAMDVLTYYMTIDTTKYKHLKPSNDKFIRDTILGLVIAARDTTSSALTWFFWLLSKNPEAMTKIRQEINKKMPKFDPADLDKLVYLDGAVCETLRLYPSVPFNHKSPAKPDVLPSGHKVDKNWRVVIPIYSLGRMKSVWGDDAEDFRPERWISDSGMLRQESSYKFLAFNAGPRTCLGKRLTFLQMKTVAVEIIRNYDIKVVEGHKPKPVPSVLLRMQHGLKVSVTKI
Protein: UPF0114 protein YqhA (P67244)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MERFLENAMYASRWLLAPVYFGLSLALVALALKFFQEIIHVLPNIFSMAESDLILVLLSLVDMTLVGGLLVMVMFSGYENFVSQLDISENKEKLNWLGKMDATSLKNKVAASIVAISSIHLLRVFMDAKNVPDNKLMWYVIIHLTFVLSAFVMGYLDRLTRHNH
Protein: Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (Bone morphogenetic protein 4 receptor) (CD antigen CD292) (Q78EA7)
Organism: Rattus norvegicus (Rat)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction. Mediates induction of adipogenesis by GDF6.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P36898}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P36895}.
Interaction partners:
- Bone morphogenetic protein 2
- Bone morphogenetic protein 4
- Bone morphogenetic protein 7
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein 6
- Growth/differentiation factor 5
- Activin receptor type-2A
- Activin receptor type-1
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog 1
Sequence:
MTQLYTYIRLLGACLFIISHVQGQNLDSMLHGTGMKSDVDQKKPENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLTSGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSVRWLAVLISMAVCIVAMIVFSSCFCYKHYCKSISSRGRYNRDLEQDEAFIPVGESLKDLIDQSQSSGSGSGLPLLVQRTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDIPLNTRVGTRRYMAPEVLDESLSKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI
Protein: 4-hydroxyphenylpyruvate dioxygenase (4HPPD) (HPD) (HPPDase) (EC 1.13.11.27) (L-tyrosine degradation gene cluster protein hppD) (Pyomelanin biosynthesis cluster protein hppD) (Q4WHU1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: 4-hydroxyphenylpyruvate dioxygenase; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin. The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic acid (HGA). The protein hmgX is crucial for this conversion and thus, probably functions as an accessory factor to mediate specific activity of hppD. The homogentisate 1,2-dioxygenase hmgA is then involved in the cleavage of the aromatic ring of HGA and its conversion to 4-maleylacetoacetate. When hmgA activity is lowered by the cell wall integrity (CWI) signaling pathway, HGA accumulates and leads to the production of pyomelanin through benzoquinone acetic acid after oxidation and polymerization. On the opposite, in non-stress conditions, both hppD and hmgA activities are balanced and HGA is degraded into 4-maleylacetoacetate. 4-maleylacetoacetate is further converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase maiA, which is degraded into fumarate and acetoacetate by the fumarylacetoacetase fahA (Probable).
Interaction partners:
- Homogentisate 1,2-dioxygenase hmgA
- homogentisate 1,2-dioxygenase
- histidinol-phosphate transaminase
- aromatic-amino-acid transaminase
- 4-hydroxyphenylpyruvate dioxygenase, putative
- 4-hydroxyphenylpyruvate dioxygenase, putative
- 4-hydroxyphenylpyruvate dioxygenase, putative
- Cytochrome P450 phenylacetate 2-hydroxylase, putative
- Probable 4-hydroxyphenylpyruvate dioxygenase 2
- Transaminase A
Sequence:
MAPSAISTSPPPTDRVSSSLASYKGYDHVHWYVGNAKQAASYYITRMGFKRIAYRGLETGCRSVCSHVVRNGDITFILTSPLRSLDQVDRFPPEEQELLKEIHAHLEKHGDGVKDVAFEVDSVDSVFYAATNNGAKIVSQPRTLEDDNGQVRVATIQTYGETTHTLVERGSYHGAFLPGYRMETGVEDPISQLLPGVHLNRIDHCVGNQDWDEMDKVCEYYEKALGFHRFWSVDDKQICTEYSALKSIVMASPNEVVKMPINEPAKGKKQSQIEEYVDFYNGAGVQHIALLTDDIIRDITNLKARGVEFIKVPDTYYEDIKVRLKKAGLTLHEDFETIRSLDILIDFDEGGYLLQLFTKHLMDRPTVFIEIIQRHNFSGFGAGNFKSLFEAIEREQALRGNLV
Protein: Ankyrin 2 (E9PCH6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MNGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Defensin beta 118 (Beta-defensin 18) (DEFB-18) (Epididymal secretory protein 13.6) (ESP13.6) (Q96PH6)
Organism: Homo sapiens (Human)
Function: Host defense peptide that exhibits antimicrobial activity against both Gram-negative bacteria, such as E.coli and S.typhimurium, and Gram-positive bacteria, such as S.aureus and B.subtilis. Inhibits cell adhesion of E.coli on intestinal epithelial enterocytes. Causes rapid permeabilization of both the outer and inner membrane of E.coli, leading to morphological alterations on the bacterial surface. Binds to bacterial lipopolysaccharides (LPS) with high affinity, and may thereby be involved in immunoregulation through LPS neutralization. May contribute to epididymal innate immunity and protect the sperm against attack by microorganisms.
Subcellular location: Secreted {ECO:0000269|PubMed:12600824}.
Interaction partners:
- Beta-defensin 126
- Beta-defensin 129
- Beta-defensin 114
- Beta-defensin 127
- Beta-defensin 116
- Beta-defensin 115
- Beta-defensin 132
- Beta-defensin 131A
- Beta-defensin 1
- Beta-defensin 125
Sequence:
MKLLLLALPMLVLLPQVIPAYSGEKKCWNRSGHCRKQCKDGEAVKDTCKNLRACCIPSNEDHRRVPATSPTPLSDSTPGIIDDILTVRFTTDYFEVSSKKDMVEESEAGRGTETSLPNVHHSS
Protein: Neuronal acetylcholine receptor subunit alpha-3 (Q8R4G9)
Organism: Mus musculus (Mouse)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000305|PubMed:21659607}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:21659607}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04757}. Golgi apparatus {ECO:0000250|UniProtKB:P04757}. Note=Interaction with UBXN2A/UBXD4 promotes translocation to the plasma membrane. {ECO:0000250|UniProtKB:P04757}.
Interaction partners:
- Class E basic helix-loop-helix protein 23
- Integrin beta-1
- Beta-2-microglobulin
- Gamma-aminobutyric acid receptor subunit alpha-6
- CD151 antigen
- Gephyrin
- Neuronal acetylcholine receptor subunit beta-4
- Fibronectin
- Neuronal acetylcholine receptor subunit alpha-5
- Tyrosine-protein kinase JAK2
Sequence:
MGVVLPPPPLSMLMLVLMLLPVASASEAEHRLFQYLFEDYNEIIRPVANVSHPVIIQFEVSMSQLVKVDEVNQIMETNLWLKQIWNDYKLKWKPSDYQGVEFMRVPAEKIWKPDIVLYNNADGDFQVDDKTKALLKYTGEVTWIPPAIFKSSCKIDVTYFPFDYQNCTMKFGSWSYDKAKIDLVLIGSSMNLKDYWESGEWAIIKAPGYKHEIKYNCCEEIYQDITYSLYIRRLPLFYTINLIIPCLLISFLTVLVFYLPSDCGEKVTLCISVLLSLTVFLLVITETIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHYRTPTTHTMPTWVKAVFLNLLPRVMFMTRPTSTEEDAPKTRNFYGAELSNLNCFSRADSKSCKEGYPCQDGTCGYCHHRRVKISNFSANLTRSSSSESVDAVLSLSALSPEIKEAIQSVKYIAENMKAQNVAKEIQDDWKYVAMVIDRIFLWVFILVCILGTAGLFLQPLMARDDT
Protein: Myb/SANT-like DNA-binding domain-containing protein (A0A384L780)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDGNFPQGGVVRSGASSYGGFDLQGSMRVHHQDSMNQQHRHNPNSRPLHEGLPFTMVTGQTCDHHQNQNMSMSEQQKAEREKNSVSDDDEPSFTEEGGDGVHNEANRSTKGSPWQRVKWTDKMVKLLITAVSYIGDDSSIDSSSRRKFAVLQKKGKWKSVSKVMAERGYHVSPQQCEDKFNDLNKRYKKLNDMLGRGTSCQVVENPALLDSIGYLNDKEKDDVRKIMSSKHLFYEEMCSYHNGNRLHLPHDLALQRSLQLALRSRDDHDNDDSRKHQMEDLDDEDHDGDGDEHDEYEEQHYAYGDCRVNHYGGGGGPLKKIRPSLSHEDGDHPSHVNSLECNKVSLPQIPFSQADVNQGGAESGRAGSVQKQWMESRTLQLEEQKLQIQVELLELEKQRFRWQRFSKKRDQELERMRMENERMKLENDRMGLELKQRELGVEL
Protein: PGAP1-like protein (Q38DX1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVGKRGRRQSPVVPLPVGLLSGSTVVGCFRAWSRKELLVLLLSASFTLFFAFSAVRWLTTTVRTDLQAILVEAEPTFVEVPFDPPTGKFYKLWRYRDNKTDSFRKLQPQAFPNVPVIYIHGNAGCYQDMRFFGRVVGESVVRLRRYNAIHYGERVRNKIFQLYKNEGSELPRAGIQIPKDIQRRAENMVVADTPMLGVELFAPDFLEESNAHSAIVMAREAMYLNHSVHELFRRFLDHYHDVLKQPPGDLRHAAGGNRSEIPVAASVENEYVDSACGTWSEYSPDPSACSTLKKEVAMFSSTERIRQEVQRVEREGIWLWTESIGGVLGVFAALLAPELYAGLVMAGPPLRYSPLLFDLPAVYFQKTIQDAVTVPYANISNTQRNWSKILAGSSTYELLKNLNSVPHADIAGRLERVSLVSVHGGALEDIVPPRSSHIMRTVSRRSTSPEHRPLLATKPPYAGRRDVCTEELRGCGISLSHRGLVYAVQLLDSAGYYTVVASLTGEAGRLVGVESTLPVGRERMFPMVLETLSRNSDAYRAEKFRFTTALHYDSENDKYHMTDGRHFMNGLTRLCADGQSTLNLQDLPVSEDEDTESWSPLHIFVGATTYEAEEVILPELTLVADEENEEPLSQSNLQVRLATKLHLPYRRKDSNVTEGTVLRTALSFQVLRRRREQSSLRLRPRFCFFVRNEKVNVSHFALVQHDVIDPLRELSSPEVHDATLYSQLSGDISVEKYGRFSLIRNMRVSQMETSLSLYVKNRTVYPVTICGSLRSLRVTFRGGEKVALDEPEAQNQYFFGPYVENVSSFTYSWRPFHTTPFNVTNVYVVYVLTPDIQPKMDFEDTKMHQSPEWIKPSYWLWRLNYDSLRWMAIGTTYSVAIQLISCYVLFFFVIIVVFHVPRLARGGGEPEKGVRGFFEVSPTILAIAVGLGIELASLHVVRQTLSVCLDEEPPRVSGGNITDMMSLSEALTLVFLCALPPRLDTCRHSWIRMVAAVPADVTLEHMVHLVFSYCLTVLSVSLMQVQYYLLWPLFKVIRPLLIRRPSGRLAVWPFAFLWLAPMVLHSTVYWMHVYVTTNISCIFALASLWCIPEEMFTNTGRRYQQLCLLVIFPIQLATHFEGSGLLIRNYFMLPTETLTDSERFESLPEQIIALTVAQGCLAVVYGTVYLALLHQDGITDRGSAKKMQYVGGTNCSGGEERREGKKRKQRERLESQEVLGERTIERLEYSMGDLGRRYPKLKLLTKVGSFTFMFVACWMGVVALRRPLEGTVFLFGLSVVAARVAFALLSFW
Protein: Alpha-parvin (Actopaxin) (Q9EPC1)
Organism: Mus musculus (Mouse)
Function: Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development. Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishment of cell polarity, cell adhesion, cell spreading, and directed cell migration.
Subcellular location: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line.
Interaction partners:
- Scaffold protein ILK
- LIM and senescent cell antigen-like-containing domain protein 1
- Paxillin
- Ras suppressor protein 1
- Beta-parvin
- LIM and senescent cell antigen-like-containing domain protein 2
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Dual specificity testis-specific protein kinase 1
- Gamma-parvin
Sequence:
MATSPQKSPLVPKSPTPKSPPSRKKDDSFLGKLGGTLARRKKAKEVSEFQEEGMNAINLPLSPISFELDPEDTLLEENEVRTMVDPNSRNDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKNLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE