wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-glycine alpha-amidating monooxygenase (PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase (PHM) (EC 1.14.17.3); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5) (Peptidylamidoglycolate lyase) (PAL)] (P10731)
Organism: Bos taurus (Bovine)
Function: Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides. Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate. The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate. Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:2059626}; Single-pass membrane protein {ECO:0000269|PubMed:2059626}. Note=Secretory granules. {ECO:0000269|PubMed:2059626}.
Interaction partners:
- Kalirin RhoGEF kinase
- Carboxypeptidase E
- Copper-transporting ATPase 1
Sequence:
MAGFRSLLVLLLVFPSGCVGFRSPLSVFKRFKETTRSFSNECLGTTRPVIPIDSSDFALDIRMPGVTPKQSDTYFCMSVRLPMDEEAFVIDFKPRASMDTVHHMLLFGCNMPASTGNYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPPGGKVVNSDISCHYKKYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVEHPVDVSFGDILAARCVFTGEGRTEVTHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDIFRTIPPEANIPIPVKSDMVMMHGHHKETENKDKTSLLQQPKREEEGVLEQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDTRESAEQERGNAILVRDRIHKFHRLVSTLRPAESRVLSLQQPLPGEGTWEPEHTGDFHVEEALDWPGVYLLPGQVSGVALDPQNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPKSKEGPLLTLGRSMQPGSDQNHFCQPTDVAVDPDTGTIYVSDGYCNSRLVQFSPSGKFITQWGEASLESSPKPGQFRVPHSLALVPPLGQLCVADRENGRIQCFKTDTKEFVREIKHPSFGRNVFAISYIPGLLFAVNGKPYFEDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIAASEDGTVYVGDAHTNTVWKFTSTEKMEHRSVKKAGIEVQEIKESEAVVETKMENKPASSELQKIQEKQKLVKEPGSGVPAVLITTLLVIPVVVLLAIALFIRWKKSRAFGDSERKLEASSGRVLGRLRGKGGGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKDEDASESEEEYSAPPPAPAPSS
Protein: Septation protein 7 (Seventh homolog of septin 1) (Q59VX8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation. SEP7 is required to convert hyphal septin rings into the hyphal-specific state and is necessary for CDC10 turnover during hyphal growth.
Subcellular location: Bud neck {ECO:0000269|PubMed:18234840, ECO:0000269|PubMed:22687514}. Note=Present at the bud neck during cell division.
Interaction partners:
- Septin
- Septin
- Septin CDC11
- Cell division control protein 10
- Serine/threonine-protein kinase GIN4
- Septin
- Cyclin-dependent kinase 1
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
Sequence:
MSRFDYRNTSKNTSVVDPDHSSPIINYRKDAKKGIKFTFMVVGESGTGKTTFINSLLNKKVLNHRYEKLSPTVGDTKTLMFTSAKSVALPNTSILTKNEFNPRTINEEPGIALTETHIEIIDDDNQKLLLNIIDTPGFGENLNNELCFIEIENYLKQQFDLVLAEETRIKRNPRFVDTRVHVMLYFITPTGHGLREIDIQCMKRLSKYVNIIPVIGKADSFTLNELQHFKQQIRIDIQKFNVPTFQFDNSLNDYDEDEDYDLIQECKFLTNLQPFAVVTSEDVFEVRESTTSTKGNNDKPKIIRARKYPWGLVDINDTRYSDFPILKSVLLGSHLQDLKDLTHDFLYETYRTERLTKVTGNGQAFDDEENEDAEFHDTVEHQLNDSNRGVGGDDNNNNNNNNNNASTIPSMSNLAQLTTSTNEHDASHIDNNSITSTSSSIKKSTSMLIDDHPSSSPKLKNISSFTSSTSTVSLEGGEKEGGHHDRGANSTSTNNNNNNNAFKRLSIGPQRNQLRQISETVPYVLRHERILERQQKLEEMEQASARELANRAALLEKKAAQLKAKEKALRQLELNRQKQEESATSSLHRKDSDISGSVQSGGVDDGKSESTNNNNNNRNGYGYGHGHGHGQSHEYDNSEYHHDDSTPNYETSRLQKDETLTDLHSIVSNH
Protein: Myb/SANT-like DNA-binding domain-containing protein 4 (Myb/SANT-like DNA-binding domain containing 4 with coiled-coils) (Q8NCY6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKQLKRKRKSNFSVQETQTLLKEITKRKEVIFSKQLNTTINVMKRMAWEEIAQCVNAVGEGEQRTGTEVKRRYLDWRALMKRKRMKANIKLVGSGFPLPSSDLDDSLTEEIDEKIGFRNDANFDWQNVADFRDAGGSLTEVKVEEEERDPQSPEFEIEEEEEMLSSVIPDSRRENELPDFPHIDEFFTLNSTPSRSAYDEPHLLVNIEKQKLELEKRRLDIEAERLQVEKERLQIEKERLRHLDMEHERLQLEKERLQIEREKLRLQIVNSEKPSLENELGQGEKSMLQPQDIETEKLKLERERLQLEKDRLQFLKFESEKLQIEKERLQVEKDRLRIQKEGHLQ
Protein: Galectin (F8W2U6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zinc finger protein 710
- PHD finger protein 20, b
- Putative sodium-coupled neutral amino acid transporter 11
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- DALR anticodon-binding domain-containing protein 3
Sequence:
MVFTIKDMSFKAGMEMKISGKVKPGCDAFSINIGHDDDAIALHFNPRFNAHGDSNTIVCNSKQGGWGSEHREHCFPFQQGEEFKLSITFNNETFYIKLPEGTMMSFPNRFGDDAFSHVHVKGDVKIISVKAK
Protein: C-C motif chemokine 27 (CC chemokine ILC) (Cutaneous T-cell-attracting chemokine) (CTACK) (ESkine) (IL-11 R-alpha-locus chemokine) (Skinkine) (Small-inducible cytokine A27) (Q9Y4X3)
Organism: Homo sapiens (Human)
Function: Chemotactic factor that attracts skin-associated memory T-lymphocytes. May play a role in mediating homing of lymphocytes to cutaneous sites. Binds to CCR10.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9Z1X0}.
Interaction partners:
- C-C chemokine receptor type 10
- C-C motif chemokine 5
- Atypical chemokine receptor 4
- Atypical chemokine receptor 2
- Eotaxin
- Platelet factor 4 variant
- C-C chemokine receptor type 7
- C-C chemokine receptor type 2
- C-C motif chemokine 21
- C-C chemokine receptor type 3
Sequence:
MKGPPTFCSLLLLSLLLSPDPTAAFLLPPSTACCTQLYRKPLSDKLLRKVIQVELQEADGDCHLQAFVLHLAQRSICIHPQNPSLSQWFEHQERKLHGTLPKLNFGMLRKMG
Protein: Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase (EC 3.2.2.-) (EC 3.2.2.10) (AMP nucleosidase) (EC 3.2.2.4) (CMP nucleosidase) (GMP nucleosidase) (IMP nucleosidase) (UMP nucleosidase) (dTMP nucleosidase) (P0ADR8)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5-phosphate and the corresponding free base. Can use AMP, GMP, IMP, CMP, dTMP and UMP as substrates. Cannot catalyze the reverse reactions. Is required for optimal growth in glucose minimal medium, possibly because it contributes to nucleoside pool homeostasis by degrading excess nucleotides and feeding back the ribose moiety to catabolism.
Interaction partners:
- Protein UshA
- GMP/IMP nucleotidase YrfG
- AMP nucleosidase
- Pyrimidine/purine nucleoside phosphorylase
- 5'/3'-nucleotidase SurE
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- Adenylate kinase
- Cytosine deaminase
- 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
Sequence:
MITHISPLGSMDMLSQLEVDMLKRTASSDLYQLFRNCSLAVLNSGSLTDNSKELLSRFENFDINVLRRERGVKLELINPPEEAFVDGRIIRALQANLFAVLRDILFVYGQIHNTVRFPNLNLDNSVHITNLVFSILRNARALHVGEAPNMVVCWGGHSINENEYLYARRVGNQLGLRELNICTGCGPGAMEAPMKGAAVGHAQQRYKDSRFIGMTEPSIIAAEPPNPLVNELIIMPDIEKRLEAFVRIAHGIIIFPGGVGTAEELLYLLGILMNPANKDQVLPLILTGPKESADYFRVLDEFVVHTLGENARRHYRIIIDDAAEVARQMKKSMPLVKENRRDTGDAYSFNWSMRIAPDLQMPFEPSHENMANLKLYPDQPVEVLAADLRRAFSGIVAGNVKEVGIRAIEEFGPYKINGDKEIMRRMDDLLQGFVAQHRMKLPGSAYIPCYEICT
Protein: Olfactory receptor (A0A2I3BR00)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
Sequence:
MKDRTQIWKNQSATNSAVCLSSSVTMFIFLGFSDHPELRIFLFLTFLSIYLVTLTWNLALIFLIRGDIHLHTPMYFFLSNLSFVDICYSSSVAPKMLSDFFREQKTISFLGCGAQFFFFVGLGLTECFLLTAMAYDRYAAISNPLLYTTIMPQGLCMRMVAGAYLGGFLSSFIQASSIFQLHFCGPNVINHFFCDLPPILALSCSNTFLSQVVNFLIVITVGGTSFLILLISYSYIVSAVLKIHSVRGRWKAFNTCASHLMAVTMLFGTALFMYLRPSSSYSFSRDKVVSVFYSLVIPMLNPLIYSLRNKEIKDALWKVMERKKVFPNL
Protein: Ubiquitin-associated protein 2-like (RNA polymerase II degradation factor Ubap2l) (Q80X50)
Organism: Mus musculus (Mouse)
Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled nucleotide excision repair (TC-NER) machinery fails to resolve DNA damage (By similarity). Plays an important role in the activity of long-term repopulating hematopoietic stem cells (LT-HSCs). Required for efficient formation of stress granules (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q14157}. Chromosome {ECO:0000250|UniProtKB:Q14157}. Cytoplasm {ECO:0000250|UniProtKB:Q14157}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q14157}. Note=Associates with nuclear chromatin. {ECO:0000250|UniProtKB:Q14157}.
Interaction partners:
- Protein PRRC2C
- Regulatory-associated protein of mTOR
- Serine/threonine-protein kinase mTOR
- Thyroid hormone receptor-associated protein 3
- Ras GTPase-activating protein-binding protein 1
- Histone-binding protein RBBP4
- Caprin-1
- Ras GTPase-activating protein-binding protein 2
- Polycomb complex protein BMI-1
- Casein kinase II subunit alpha
Sequence:
MMTSVGTNRARGNWEQPQNQNQTQHKQRPQATAEQIRLAQMISDHNDADFEEKVKQLIDITGKNQDECVIALHDCNGDVNRAINVLLEGNPDTHSWEMVGKKKGVSGQKDGGQTESNEEGKENRDRDRDYSRRRGGPPRRGRGASRGREFRGQENGLDGTKSGGPSGRGTDRGRRGRGRGRGSSGRRGGRFSAQGMGTFNPADYAEPANTDDNYGNSSGNTWNNTGHFEPDDGTRLDFIGVEGSNYPRKFETAPGAWRTATEEWGTEDWNEDLSETKIFTASNVSSVPLPAENVTITAGQRIDLAVLLGKTPSSMENDSSNLDPSQAPSLAQPLVFSNSKQNAISQPASGSTFSHHSMVSMLGKGFGDVGEAKGGSTTGSQFLEQFKTAQALAQLAAQHSQSGSTTTSSWDMGSTTQSPSLVQYDLKSANDSTVHSPFTKRQAFTPSSTMMEVFLQEKPPAVATSTAAPPPPSSPLPSKSTSAPQMSPGSSDNQSSSPQPAQQKLKQQKKKTSLTSKIPALAVEMPGSADISGLNLQFGALQFGSEPVLSDYESTPTTSASSSQAPSSLYTSTASESSSTVSSNQSQESGYQSGPIQSTTYTSQNNAQGPLYEQRSTQTRRYPSSISSSPQKDLTQAKNGFSSVQATQLQTTQSVEGATGSAVKSESPSTSSIPSLNETVPAASLLTTANQHSSSLSGLSHTEEIPNTTTTQHSSALSTQQNTLSSSTSSGRTSTSTLLHTSVESEANLHSSSSTFSTTSSTVSAPPPVVSVSSSLNSGSSLGLSLGSNSTVTASTRSSVATTSGKAPPNLPPGVPPLLPNPYIMAPGLLHAYPPQVYGYDDLQMLQTRFPLDYYSIPFPTPTTPLTGRDGSLASNPYSGDLTKFGRGDASSPAPATTLAQPQQNQTQTHHTTQQTFLNPALPPGYSYTSLPYYTGVPGLPSTFQYGPAVFPVAPTSSKQHGVNVSVNASATPFQQPSGYGSHGYNTGVSVTSSNTGVPDISGSVYSKTQQSFEKQGFHSGTPAASFNLPSALGSGGPINPATAAAYPPAPFMHILTPHQQPHSQILHHHLQQDGQTGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN
Protein: E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) (A4D1L5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSPSPGKRRMDTDVVKLIESKHEVTILGGLNEFVVKFYGPQGTPYEGGVWKVRVDLPDKYPFKSPSIGFMNKIFHPNIDEASGTVCLDVINQTWTALYDLTNIFESFLPQLLAYPNPIDPLNGDAAAMYLHRPEEYKQKIKEYIQKYATEEALKEQEEGTGDSSSESSMSDFSEDEAQDMEL
Protein: AT16263p (RE34385p) (Steppke, isoform A) (Q9V9Q6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISAMDNFDNRSYGAISKGRSEFSMPELTPEQQKLLIELRRKKQELLLEIQQIKDELCEVVSEMEALDVPEDCKHSNKDKQMSIGRKKFNMDPKKGIEYLVENRLLRHDPQDVAHFLYKGEGLNKTAIGDYLGEKNDFNEDVLKAFVALHDFTNLILVQALRQFLWSFRLPGEAQKIDRMMETFAQRYCQLNPDIFTNTDTCYVLSFAIIMLNTSLHNPSVKDKPTVDQFISMNRGINNGGDLPRGLLESLYESIRTEPFKIPQDDGNDLMHTFFNPDKEGWLWKQGGRYKSWKRRWFILNDNCLYYFEYTTDKEPRGIIPLENISVREIHDRSKPHCFELFATGGADIIKACKTDSEGKVVEGKHTVYRMSAATEEDQQEWIKRLTQSISHNPFYDILVQRKKKALSKS
Protein: Eukaryotic translation initiation factor 4 gamma 2 (eIF-4-gamma 2) (eIF-4G 2) (eIF4G 2) (Novel APOBEC-1 target 1) (Translation repressor NAT1) (p97) (Q62448)
Organism: Mus musculus (Mouse)
Function: Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases.
Interaction partners:
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 4E
- YTH domain-containing family protein 3
- Eukaryotic initiation factor 4A-II
- Eukaryotic translation initiation factor 4E type 1B
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4E type 2
- Eukaryotic translation initiation factor 4 gamma 3
- Eukaryotic translation initiation factor 4E type 3
- Eukaryotic translation initiation factor 5
Sequence:
MESAIAEGGASRFSASSGGGGSRGAPQHYPKTAGNSEFLGKTPGQNAQKWIPARSTRRDDNSAANNSANEKERHDAIFRKVRGILNKLTPEKFDKLCLELLNVGVESKLILKGVILLIVDKALEEPKYSSLYAQLCLRLAEDAPNFDGPAAEGQPGQKQSTTFRRLLISKLQDEFENRTRNVDVYDKRENPLLPEEEEQRAIAKIKMLGNIKFIGELGKLDLIHESILHKCIKTLLEKKKRVQLKDMGEDLECLCQIMRTVGPRLDHERAKSLMDQYFARMCSLMLSKELPARIRFLLQDTVELREHHWVPRKAFLDNGPKTINQIRQDAVKDLGVFIPAPMAQGRSDFFLEGPFMPPRMKMDRDPLGGLADMFGQMPGSGIGTGPGVIQDRFSPTMGRHRSNQLFNGHGGHIMPPTQSQFGEMGGKFMKSQGLSQLYHNQSQGLLSQLQGQSKDMPPRFSKKGQLNADEISLRPAQSFLMNKNQVPKLQPQITMIPPSAQPPRTQTPPLGQTPQLGLKTNPPLIQEKPAKTSKKPPPSKEELLKLTEAVVTDYLNSGNANDAVSGVREMRAPKHFLPEMLSKVIILSLDRSDEDKEKASSLISLLKQEGIATSDNFMQAFLNVLEQCPKLEVDIPLVKSYLAQFAARAIISELVSISELAQPLESGTHFPLFLLCLQQLAKLQDREWLTELFQQSKVNMQKMLPEIDQNKDRMLEILEGKGLSFLFPLLKLEKELLKQIKLDPSPQTIYKWIKDNISPKLHVDKGFVNILMTSFLQYISSEVSPPSDETDSSSAPSKEQLEQEKQLLLSFKPVMQKFLHDHVDLQVSALYALQVHCYNSSFPKGMLLRFFVHFYDMEIIEEEAFLAWKEDITQEFPGKGKALFQVNQWLTWLETAEEEESEEEAD
Protein: rRNA-processing protein cgrA (Q9Y708)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Ribosome biogenesis regulatory protein
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein nsa2
- Nucleolar GTP-binding protein 2
- Ribosome assembly protein 4
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
- Myosin-related protein homolog MlpA
- Transcription factor domain-containing protein
- Ribosome biogenesis protein RLP24
Sequence:
MSSAAPAPSTHAAKSIRKNGKNWHDNKKPFRPNGGLTSYTKRAAARKEQEAIKEYEKELREEREAERQAHIQRIKERRAAKEEKERYEKMAEKMHRKRVERLKKREKRNKLLNS
Protein: Drebrin-like protein (Cervical SH3P7) (Cervical mucin-associated protein) (Drebrin-F) (HPK1-interacting protein of 55 kDa) (HIP-55) (SH3 domain-containing protein 7) (Q9UJU6)
Organism: Homo sapiens (Human)
Function: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes (By similarity). May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q62418}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q62418}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHL4}. Synapse {ECO:0000250|UniProtKB:Q62418}. Perikaryon {ECO:0000250|UniProtKB:Q62418}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62418}. Cell membrane {ECO:0000269|PubMed:14729663}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side {ECO:0000250|UniProtKB:Q62418}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side {ECO:0000250|UniProtKB:Q62418}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62418}; Cytoplasmic side {ECO:0000250|UniProtKB:Q62418}. Cell projection, podosome {ECO:0000250|UniProtKB:Q62418}. Early endosome {ECO:0000269|PubMed:14729663}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9JHL4}. Postsynaptic density {ECO:0000250|UniProtKB:Q9JHL4}. Note=Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes. {ECO:0000250|UniProtKB:Q62418, ECO:0000250|UniProtKB:Q9JHL4}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase kinase 1
- Mitogen-activated protein kinase kinase kinase kinase 3
- Caspase-3
- Adenylyl cyclase-associated protein 1
- SH3 domain-binding protein 2
- Adenylyl cyclase-associated protein 2
- SH3 and multiple ankyrin repeat domains protein 3
- Tyrosine-protein kinase ZAP-70
- FYVE, RhoGEF and PH domain-containing protein 1
Sequence:
MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESGRFQDVGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEAQRQLEQERRERELREAARREQRYQEQGGEASPQRTWEQQQEVVSRNRNEQESAVHPREIFKQKERAMSTTSISSPQPGKLRSPFLQKQLTQPETHFGREPAAAISRPRADLPAEEPAPSTPPCLVQAEEEAVYEEPPEQETFYEQPPLVQQQGAGSEHIDHHIQGQGLSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE
Protein: Dapper homolog 2 (Dapper antagonist of catenin 2) (Q5SW24)
Organism: Homo sapiens (Human)
Function: Involved in regulation of intracellular signaling pathways during development. Negatively regulates the Nodal signaling pathway, possibly by promoting the lysosomal degradation of Nodal receptors, such as TGFBR1. May be involved in control of the morphogenetic behavior of kidney ureteric bud cells by keeping cells epithelial and restraining their mesenchymal character. May play an inhibitory role in the re-epithelialization of skin wounds by attenuating TGF-beta signaling (By similarity).
Interaction partners:
- Dapper homolog 3
- Catenin beta-1
Sequence:
MWTPGGPPGSAGWDRRRLGARLRAAFAGLQELQGLRATQQERVRGALALQPPPAPAAPCGPHGLHGPEQQLEAALAALQEQLSRLRQQDIGLKTHLDQLDLQISKLQLDVGTASGEALDSDSRPSSGFYEMSDGGSCSLSTSCASVCSDHISPSLGSLLPVAQAHKARPSMGDWRPRSVDETTVPAWRPQATEEGARPPGSVEDAGQPWGTFWPRPVSTGDLDRALPADTGLQKASADAELLGLLCQGVDIPLHVPDPKYRQDLVSQGGREVYPYPSPLHAVALQSPLFVLTKETPQRGGPSFPRESPRGPAGLNTIQTGPVLEAGPARARAYIDRLLHLWGRETPAKGSEGEQGPLRHAASPSPQRQGGWSTDGGGRLLVFAPGREDEGGPAQSRGAGRGGPQQQGYMPLEGPQQSGSLPEEGSKPSNSCVLRETMVQASPSSKAQQTPSAQDYGRGNIISPSRMLDKSPSPASGHFAHPSFAASLKMGPPKSKAEKIKRSPMDKVLRFARQPLLLLDRPEGAHAAPQPSLEWDPAHWPTGRGGLQRRPALAWEAPGRSCSESTLYPMPVLVPLAVAPQESHRTSAQALFPFEASLLTSVARRKHRRWQSTVEISARARLASCPESNLGPPRPVARRAGGPLARGRPSLVRQDAYTRSDSEPSKHSAECDPRFPSVIPETSEGESSDHTTNRFGDRESSSSDEEGGAQSRDCDLALGYVAAGHAELAWTQEAPVSSGPLLSPVPKLCRIKASKALKKKIRRFQPTALKVMTMV
Protein: Ubiquitin-like domain-containing CTD phosphatase 1 (EC 3.1.3.16) (Nuclear proteasome inhibitor UBLCP1) (Q8WVY7)
Organism: Homo sapiens (Human)
Function: Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.
Subcellular location: Nucleus {ECO:0000269|PubMed:15883030, ECO:0000269|PubMed:21949367, ECO:0000269|PubMed:28539385}. Note=Colocalizes with nuclear proteasomes.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 8
Sequence:
MALPIIVKWGGQEYSVTTLSEDDTVLDLKQFLKTLTGVLPERQKLLGLKVKGKPAENDVKLGALKLKPNTKIMMMGTREESLEDVLGPPPDNDDVVNDFDIEDEVVEVENREENLLKISRRVKEYKVEILNPPREGKKLLVLDVDYTLFDHRSCAETGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKELGVSTNANYKITFMLDSAAMITVHTPRRGLIDVKPLGVIWGKFSEFYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMKAHLNRDKDKELLKLTQYLKEIAKLDDFLDLNHKYWERYLSKKQGQ
Protein: Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (Q9P6Q1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- L-2-aminoadipate reductase
- Uncharacterized protein C18B11.08c
- Uncharacterized protein C56F8.13
- Uncharacterized protein C56F8.15
- Putative uncharacterized transmembrane protein SPBC713.13.
- Uncharacterized protein SPBC713.14c
- Amino-acid permease 1
- Uncharacterized protein C887.16
- Telobox protein 1
- Uncharacterized protein C1565.03
Sequence:
MSTIHSCLDLIRSQIQQSANGRNVLLVAVSKFHPVETLMEAYNAGQRHFGENYMQEFLKKVELMPDDVQWHFIGSLQSSKCKKIASVKNLYSIETIDTEKKARLVNSAREALQLPLNVYIQVNTSGEENKGGVTPSKVLELCKQVQDMKYLRLKGLMTIGSISNSQLSDHNPDFQVLSDLRESLQNELGIPLQLSMGMSSDYLLAIKYGSDSVRVGSSIFGSRPTEKPSDVHISASK
Protein: Protocadherin gamma subfamily B, 1 (Q7TQF1)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MENQVLLHFLVPLFCGALSQPIHYSIPEELAKVSLVGSLAKDLGLSIQELPARKLRVSAEDYFSVSAESGDLLVSGRIDREKICGRKSECALEFESVTENPMNIFHVTVAIQDINDNAPHFFGKSIELEICESALAGAKFPLDSARDADVGSNSLKMYTVSPNPHFSLSTKESPDGSKYPELLLETPLDREHQSSHHLILTAMDGGDPPLSSTTQVWIKVTDANDNAPVFSQDTYKVSLRENIPPGTLVLQVTASDQDESIHGEITYAFLNAPASTNLVFNLNPNTGAITTNGTLDFEEKNRYTLGVEAKDGGVHTAHCNVQIEILDDNDNAPEVTFMSFSNQVPEDSVLGTVIALIKVRDKDSGQNGLVACHIQEELPFKLQPTSKNYYKLVIDKALNREQTPEYNVTITATDSGKPSLSSKTCVTVHITDINDNAPVFHQASYLVHVAENNPPGASIAQVSASDPDLGSNGLISYSIIASDLEPRALSSFVSVNQDSGVVFAQRAFDHEQLRSFQLTLQARDHGSPTLSANVSMRVLVGDRNDNAPRVLYPTLEPDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASDPGLFSLGLRTGEVRTARALGDRDSARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDDPLPSDPQSELQFYLVVALALISVLFLLAVILAIALRLRHSSRSAAWGCFQPGLSLKSQPVVPPNYNEGTLPYSYNLCVASHSTTMAGFNFHHVAPEVAPPQDLLCDDPSVVVCGNNEDPQVSDDSAFQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Odontogenic ameloblast-associated protein (Apin) (A1E959)
Organism: Homo sapiens (Human)
Function: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q3HS83}. Cytoplasm {ECO:0000269|PubMed:25911094}. Nucleus {ECO:0000269|PubMed:25911094}.
Interaction partners:
- Amelotin
- Enamelin
- Ameloblastin
- Matrix metalloproteinase-20
- Follicular dendritic cell secreted peptide
Sequence:
MKIIILLGFLGATLSAPLIPQRLMSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPLTGEASFAQGAQAGQVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMVLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPAISGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLQKEAINFRHDSAGVFMPSTSPKPSTTNVFTSAVDQTITPELPEEKDKTDSLREP