wanglab/gogpt-training-data huggingface dataset:
Protein: Cell division cycle-associated 7-like protein (Protein JPO2) (Transcription factor RAM2) (Q96GN5)
Organism: Homo sapiens (Human)
Function: Plays a role in transcriptional regulation as a repressor that inhibits monoamine oxidase A (MAOA) activity and gene expression by binding to the promoter. Plays an important oncogenic role in mediating the full transforming effect of MYC in medulloblastoma cells. Involved in apoptotic signaling pathways; May act downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as well as CCND1/cyclin D1 and E2F1.
Subcellular location: Cytoplasm. Nucleus. Note=Associates with chromatin. Translocates from cytoplasm to nucleus under dexamethasone induction.
Interaction partners:
- Myc proto-oncogene protein
- PC4 and SFRS1-interacting protein
- Cell cycle checkpoint protein RAD1
- Cell cycle checkpoint protein RAD17
- DNA topoisomerase 2-binding protein 1
- Amine oxidase [flavin-containing] A
- Replication factor C subunit 2
Sequence:
MELATRYQIPKEVADIFNAPSDDEEFVGFRDDVPMETLSSEESCDSFDSLESGKQQDVRFHSKYFTEELRRIFIEDTDSETEDFAGFTQSDLNGKTNPEVMVVESDLSDDGKASLVSEEEEDEEEDKATPRRSRSRRSSIGLRVAFQFPTKKLANKPDKNSSSEQLFSSARLQNEKKTILERKKDCRQVIQREDSTSESEDDSRDESQESSDALLKRTMNIKENKAMLAQLLAELNSMPDFFPVRTPTSASRKKTVRRAFSEGQITRRMNPTRSARPPEKFALENFTVSAAKFAEEFYSFRRRKTIGGKCREYRRRHRISSFRPVEDITEEDLENVAITVRDKIYDKVLGNTCHQCRQKTIDTKTVCRNQGCCGVRGQFCGPCLRNRYGEDVRSALLDPDWVCPPCRGICNCSYCRKRDGRCATGILIHLAKFYGYDNVKEYLESLQKELVEDN
Protein: DegV domain-containing protein Rv2417c (P9WP05)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
Interaction partners:
- Glucosyl-3-phosphoglycerate phosphatase
- Diglucosylglycerate octanoyltransferase
- Conserved hypothetical alanine rich protein
- Monoacylglycerol lipase
- Glucosyl-3-phosphoglycerate synthase
- Probable nicotinate-nucleotide adenylyltransferase
- Ribosomal silencing factor RsfS
- DhaL domain-containing protein
Sequence:
MTVVVVTDTSCRLPADLREQWSIRQVPLHILLDGLDLRDGVDEIPDDIHKRHATTAGATPVELSAAYQRALADSGGDGVVAVHISSALSGTFRAAELTAAELGPAVRVIDSRSAAMGVGFAALAAGRAAAAGDELDTVARAAAAAVSRIHAFVAVARLDNLRRSGRISGAKAWLGTALALKPLLSVDDGKLVLVQRVRTVSNATAVMIDRVCQLVGDRPAALAVHHVADPAAANDVAAALAERLPACEPAMVTAMGPVLALHVGAGAVGVCVDVGASPPA
Protein: Ubiquinone biosynthesis protein COQ4, mitochondrial (4-hydroxy-3-methoxy-5-polyprenylbenzoate decarboxylase) (EC 4.1.1.-) (Coenzyme Q biosynthesis protein 4) (O13525)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of COQ3, COQ4, COQ6, COQ7 and COQ9 polypeptides.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03111, ECO:0000269|PubMed:11469793, ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03111, ECO:0000269|PubMed:11469793, ECO:0000269|PubMed:14562095}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03111, ECO:0000269|PubMed:11469793, ECO:0000269|PubMed:14562095}.
Interaction partners:
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Atypical kinase COQ8, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- Hexaprenyl pyrophosphate synthase, mitochondrial
- MIOREX complex component 2
- Adrenodoxin homolog, mitochondrial
Sequence:
MLRLSLLRSTATLPVKCQRRGLILPAAAMYTLGSLIFGKEARLADAMERGELHNKNVDYAKEAEERTELRIRALANTRPMEPRYNGHVPLHRYEKLLLFAISGWNSFFHPEDGYNIVQLGEATALPVFLENLKQTMLSDSSGRRILKEQPNITTEILHMDKLAKLPHNTFGYVYYQWLKRENVSPDTRAPVKFIDDPMHAYIFKRYRQCHDFYHAITNMPIIIEGEITIKALEGANLGVPMAILGGILAPLRLKKVQRKRLYNIYLPWAVRTGLSCKPLINVYWEEMLEKDVTALRKELKITLPPDLRTMRKERAALRKEIDAKYNSQKRATTPA
Protein: Protein dispatched homolog 3 (Patched domain-containing protein 2) (Thyroid hormone receptor up-regulated protein 1) (TRUP1) (B9U3F2)
Organism: Gallus gallus (Chicken)
Function: Plays a role in neuronal proliferation and differentiation (By similarity). Plays a role in the accumulation of cellular cholesterol. Involved in intracellular lipid droplet formation. May contribute to cholesterol homeostasis in neuronal cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Note=Predominantly localized to cholesterol-enriched domains within membranes (PubMed:19179482). Localizes to cytoplasmic punctate vesicular structures (PubMed:19179482). {ECO:0000269|PubMed:19179482}.
Interaction partners:
- SSD domain-containing protein.
- Sonic hedgehog protein
- Patched domain containing 1.
- Indian hedgehog protein
- Protein kintoun
- Hedgehog protein
Sequence:
MDTEDDPLLQDAWLDEEDEEVAFSSRKRREGALLCGKSSCRVRPLRVTLPVSGFWNIVGWIFTNPYCAGFILFLGCAIPAVLAVVMFLHYPALDIDISYNAFEIRNHESSQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLIFEQLQQLHLNASHLQVSTRAKRSAPQGRTSSPEPRAHPHPGNETSRVTRGAPRWDYSNTYISANTQTHAHWRIELIFLARGDSENNIFTTERLVTIHEVERKIMDHPRFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIQGSLELAMTHPEFYWYVDEGLSAENKKSSLLRSEILFGAPLPNYYSVEDRWEEQRHKFQNFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAVLVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLKDLRLRMIHTIQTAGKATFFTSLTTAAAYAANIFSQIPAVHDFGLFMSLIVSCCWVAVLFTMPAALGIWTLYVSPLESSCQNSCSQKCTKKSTLHLAEDLFVASEGTSRAGRETLPYLDDDIPLLSVEEEPVSLEMGDVPLVSVMPENLQLPVEKSNRGHLIAHLQELLEHWVLWSAVKSRWVIVGLFLLVLLLSIFFASRLRPASRAPVLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNNFRTSLEKKKRGSASPWGSKGSISDTGQQDLQGTVYISKSRSKGRPAIYRFSLNASIPAPWQMVSPGDGEVPSFQVYRVPFGNFTRKLTACVSTVGLLKQTSPRKWMMTTLSCDSKRGWKFDFSFYVAAKEQQRTRKLYFAQSHKPPYHGRVCVAPPGCLLSSSPDGPTKGILYVPSEKAAPKARLSATSGFNPCMNMGCGKPAVRPLVDTGAMVFVVFGIRGVNRTKNSDNHVIGDMGSVIYDDSFDLFKEIGNLCRLCKAIASNTELVKPGGAQCLPSGYSISSFLQMLHPECKNIPEPNLLPGQLSHGAVGVKDGKVQWISMAFESTTYKGKSSFQTYADYLKWETFLQQQLQLFPEGSALRHGFQTCEHWKQIFMEIIGVQSALYGLILSLVICVAAVAVFTTHILLLLPVLLSILGVVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPLHHAEDPTACRQWRTIEAIRHVGVAIVSSAVTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLSIMGPGTFTRSRTSCLKAVAGVLLAGLLGLCICLALLKGGFKIPLPNGTAL
Protein: Protein Iojap, chloroplastic (Q9LDY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a ribosome silencing factor (Potential). Involved in plastid biogenesis (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Protein Iojap-related
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein uS10c
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- Fructokinase-like 2, chloroplastic
- Protein PLASTID REDOX INSENSITIVE 2
- Prohibitin-5, mitochondrial
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- Small ribosomal subunit protein eS1z
Sequence:
MASSTGLTVAGALLAGDFRLPAVSSLIPRKTSSSLSCLSNRDLSSPYNCCWRLSRGKILTSLSNSRKFAVGKEAEDGFLSNVSEDTDEMFDDLFNKYGKVVFRSTDVKSPTAEVDDDAESLAFAVELAKVASDVKAGDIKVLFVKPLVYWTRFFIIATAFSRPQIDAIGSRMRDLAEKKYGKVANGDVKPNSWTLLDFGDVVIHLFLPPQRTFYNLEDFYGNAMQIELPFEDQSQPRN
Protein: YEATS domain-containing protein 4 (Glioma-amplified sequence 41) (Gas41) (NuMA-binding protein 1) (NuBI-1) (NuBI1) (O95619)
Organism: Homo sapiens (Human)
Function: Chromatin reader component of the NuA4 histone acetyltransferase (HAT) complex, a complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. Specifically recognizes and binds acylated histone H3, with a preference for histone H3 diacetylated at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac). Also able to recognize and bind crotonylated histone H3. May also recognize and bind histone H3 succinylated at 'Lys-122' (H3K122succ); additional evidences are however required to confirm this result in vivo. Plays a key role in histone variant H2AZ1/H2A.Z deposition into specific chromatin regions: recognizes and binds H3K14ac and H3K27ac on the promoters of actively transcribed genes and recruits NuA4-related complex to deposit H2AZ1/H2A.Z. H2AZ1/H2A.Z deposition is required for maintenance of embryonic stem cell (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376, ECO:0000269|PubMed:10913114, ECO:0000269|PubMed:18445686}.
Interaction partners:
- Histone acetyltransferase KAT5
- DNA methyltransferase 1-associated protein 1
- Mortality factor 4-like protein 1
- RuvB-like 1
- Chromatin modification-related protein MEAF6
- E1A-binding protein p400
- Vacuolar protein sorting-associated protein 72 homolog
- RuvB-like 2
- Enhancer of polycomb homolog 1
- MRG/MORF4L-binding protein
Sequence:
MFKRMAEFGPDSGGRVKGVTIVKPIVYGNVARYFGKKREEDGHTHQWTVYVKPYRNEDMSAYVKKIQFKLHESYGNPLRVVTKPPYEITETGWGEFEIIIKIFFIDPNERPVTLYHLLKLFQSDTNAMLGKKTVVSEFYDEMIFQDPTAMMQQLLTTSRQLTLGAYKHETEFAELEVKTREKLEAAKKKTSFEIAELKERLKASRETINCLKNEIRKLEEDDQAKDI
Protein: Fork head transcription factor short isoform (A0JL24)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MAATTTTTTTTLATTTGNSSSTNNSSSNNNNSIASSHNNNNNIVTVHTVLNNPPTNTAGGGVADAATVAIAKDMLQLHHGAAAAATAALNNYNNSSNNNNNSADQLTGNSNNSANHPPATSSTTNSSSSSTTSANTNNPSANAASTLTSSSPPYGELRFNQEVLPITDAVTVIGRNSSTSLVHFNVAENNLVSRKHFQVLYDVELRAFFVQCLSKNGIFVDDFLQRRNVDPLRLPQRCYFRFPSTEIRIEFESYVPATSSDAIDGHSPSLVVGGGGGVAGGGAHVIITPLPRDELHQQQLHHHQQQPHLQQQQHPHHPPAHHLPLQQQQQQQQPAHHPLPHTPHHPLHHTALHQQQQRSGSIVVAPPAGAAAHLIAGDGPGIYSPLKISIPKKEQKSPYLSPTGNCPASPRQGFIQNQPNNYNNYGNNNTQDLFQTPSTASYNHNEKPPYSYAQLIVQAISAAPDKQLTLSGIYSFIVKHYPYYRKETNKGWQNSIRHNLSLNRYFIKVARSQDEPGKGSFWRIDPDSGAKLIDHSYKKRRQRSSQGFRPPYGMPRSAPVSPSHMDNSRESSPLQDIVLQSAPGSPGMSLEQRAADPEIIYNSQNAHQQQHSEIIYEELPTDYSGHIEASEEECVTTATDATVAKRPKYVSEVL
Protein: Ceinsulin-1 (INSulin related) (G5ECC6)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein
- Probable insulin-like peptide beta-type 5
- Insulin-like peptide 7
- Probable insulin-like peptide beta-type 1
- INSulin related
- INSulin related
- Putative insulin-like peptide beta-type 6
- Insulin-like peptide 17
- Insulin-like peptide INSL5
- INSulin related
Sequence:
MVHRLFIVLIAIILVAKSTAISLQQADGRMKMCPPGGSTFTMAWSMSCSMRRRKRDVGRYFEKRALIAPSIRQLQTICCQVGCNVEDLLAYCAPI
Protein: Dally-like protein (Q9GPL5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU003519}.
Interaction partners:
Sequence:
MLHQEQQQQHLHCRRKVTATTTARLVIFSSPLLLLLLTTHLPSTLQADNSPAPQVAALAAPNPAGGVAGSSIIDQFSPNCSAVTHIFQARGIDAIEIPQKPSNERVLRYCESPSVGTCCTYNMETRMAMQSRQQLEGHTKDQISRMSGILGSKATKFKDIFTALLKESRTQFNSMFIRTYGVIYERNSYVFSDLFKELETYFANGRVDLLEVMDKFFNTLYQKMFTVLNTQYTFDENYMRCVSEHMKELKPFGDVPDKLSVQIKRSFVATRTYGQALTTASEVAKKVLNVRLNADCTGALTKMQHCGACKGYTEKPCTNYCVNVIKGCLHYQHEFDSEWENFAMAMDKVAERLLGSFNIVMVVEPLNIKISEAIMNFQDSGQDITNRVFQGCGRPKLKKMKRSISPKLQGVQILNARSPVEADTLDIDETLDEAIVLRERRAAEPGSQETSSQQSQEQGVGKSGNGGGGGGGNNRRQQQRRKQQQQRRKQQNNRDDNDDDDNESGGGREPILDRIVRDIRQRVKDYKKFWSNLPHSVCSNEDIASSSDVDGMCWNGHTIDRYMHSITTEHGSNPEFTGNPASTKQTAQMASQLSHLKNAIVHLRNAYNGQDVEWSEQEELPYAGSGAGSGSGSEDDEDDDEGSGLGPFEPSHKPDVERPSVDADNDDDEDAGGRGHMPTHTSRPTSGVDDKNPLIHTTHFDQDHNDLDEDHRQLDEDEDTDAGHDGANDNRSSDAPEKMTLRRALVVYLLPLYMAWFGGVCADLL
Protein: Scinderin (Adseverin) (Q5ZIV9)
Organism: Gallus gallus (Chicken)
Function: Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+). Severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2) (By similarity). Required for megakaryocyte differentiation, maturation, polyploidization and apoptosis with the release of platelet-like particles (By similarity). Plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts (By similarity). Regulates chondrocyte proliferation and differentiation. Inhibits cell proliferation and tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q60604}. Cell projection, podosome {ECO:0000250|UniProtKB:Q60604}.
Interaction partners:
- Actin, cytoplasmic 1
- Gelsolin
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- PIPK domain-containing protein.
- Phosphatidylinositol-4-phosphate 5-kinase, type I, gamma
- 1-phosphatidylinositol 3-phosphate 5-kinase
- 1-phosphatidylinositol-5-phosphate 4-kinase
- Cofilin-2
- Profilin
Sequence:
MAPERHPPAFEGAGQESGLQVWRVERLELVPVPPSRHGDFFVGDAYLVLHTVRRGAAVAYRLHYWLGKECTQDESTAAAIFTVQLDDYLGGKPVQSREIQGYESNEFVSYFKGGIKYKAGGVASGFNHVVTNDLSAQRLLHIKGRRVVRATEVPLTWASFNKGDCFIIDLGNEIYQWCGSSCNKYERLKATQVAVGIRDNERNGRSRLITVEEGSEPDELITVLGEKPELPECSDDDDEMADIANRKSAKLYMVSDASGSMKLSVVAEENPFSMAMLLSEECFILDNGAARKIFVWKGKDANPQERKAAMKNAETFVQQMNYPANTQIQVLPEGGETPIFKQFFKDWKDKDQSDGFGKVYVTERVAKIEQIEFDATKLHESPQMAAQHNMIDDGSGKVQIWRVESSGRVPVEPETYGQFYGGDCYIILYTYPKGQIIYTWQGACATKDELTASAFLTVQLDRSLNDQAVQIRVSQGKEPPHLLSLFKNKPLIVYKNGTSKKEGQKPAPPTRLFQIRRNLMSVTRIAEVDVDAMSLNSNDAFVLKLPNNTGYTWVGKGVNKEEEQGAQYIASVLKCQTAKINEGQEPEEFWKALGGKKKYQTSSQLLTKAEDHPPRLFGCSNKTGRFIIEEVPGEFTQDDLAEDDVMLLDAWEQVFVWIGKEANETERQESVKSAKRYIETDPSGRDKGTPIVIVKQGHEPPTFTGWFLAWDSNKWKN
Protein: tRNA-specific adenosine deaminase TAD1 (AtTAD1) (EC 3.5.4.34) (tRNA-specific adenosine-37 deaminase TAD1) (F4HU58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA editing. Catalyzes the specific deamination of adenosine-37 in the cytosolic tRNA-Ala. Generates inosine at the position 3'-adjacent to the anticodon tRNA-Ala.
Subcellular location: Nucleus {ECO:0000269|PubMed:23355609}.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- tRNA-specific adenosine deaminase TAD3
- tRNA
- tRNA wybutosine-synthesizing protein 2/3/4
- Holliday junction resolvase MOC1, chloroplastic
- tRNA-specific adenosine deaminase TAD2
- tRNA
- tRNA
- tRNA
- Anaphase-promoting complex subunit 10
Sequence:
MEEDWGKTVSEKVISAYMSLPKKGKPQGREVTVLSAFLVSSPSQDPKVIALGTGTKCVSGSLLSPRGDIVNDSHAEVVARRALIRFFYSEIQRMQLTSGKSNEAKRQRIDSETSSILESADSSCPGEVKYKLKSGCLLHLYISQLPCGYASTSSPLYALKKIPSTQVDDSLLVQASDICSSRHSDVPEIGSNSNKGNGSQVADMVQRKPGRGETTLSVSCSDKIARWNVLGVQGALLYQVLQPVYISTITVGQSLHSPDNFSLADHLRRSLYERILPLSDELLTSFRLNKPLFFVAPVPPSEFQHSETAQATLTCGYSLCWNYSGLHEVILGTTGRKQGTSAKGALYPSTQSSICKQRLLELFLKETHGHKRESSKSKKSYRELKNKATEYYLMSKIFKGKYPFNNWLRKPLNCEDFLIN
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (Q6CNR3)
Organism: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Interaction partners:
- mitogen-activated protein kinase kinase
- protein-tyrosine-phosphatase
- Protein STE12
- KLLA0F12023p
- Transcription factor
- KLLA0B07469p
- Mitogen-activated protein kinase
- protein-tyrosine-phosphatase
- Mitochondrial import inner membrane translocase subunit
- KLLA0D06611p
Sequence:
MGKRIVFNISSEFQLQSLLGEGAYGVVCSAKHKPSGEIVAIKKIEPFEKPLFSIRTLREIKILKHFQHENIISIFDVQKPSSFEQFNEVYIIQELMQTDLHRVIVTQELSEDHVQYFVYQTLRALKVLHGSNVIHRDLKPSNLLLNSNCDLKICDFGLARIVSERATDGDAHVDADDTDDNSPSSAANDGDPAISGMTEYVATRWYRAPEVMLTAAQYSKSMDVWSCGCILAELLGKQPLFPGKDYRDQLILIFQTLGTPTEQELVELVENRRAREYIRSLPKHPKINWRRRFPNASAAALDLLDRMLQFDPRLRITATEALSHPYLVSYHDPDDEPEGTPIPSSFFQFDQWKSRLNTKDLKRLLWNEIVS
Protein: Junctional adhesion molecule 3B (Jam3b) (Junctional adhesion molecule C) (JAM-C) (A3KPA0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Junctional adhesion protein that mediates heterotypic cell-cell interactions to regulate different cellular processes (By similarity). During myogenesis, it is involved in myocyte fusion through the binding of jam2a on neighboring myocytes.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9BX67}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX67}. Cell junction {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9BX67}.
Interaction partners:
- Junctional adhesion molecule 2A
- Tight junction protein 1a
- Par-3 family cell polarity regulator.
- Par-3 family cell polarity regulator alpha, b.
- Junctional adhesion molecule A
- Junctional adhesion molecule A
- Integrin beta
- Junctional adhesion molecule 2b
- Si:dkey-32n7.4
- Junctional adhesion molecule 3a
Sequence:
MALTPLACVLLLLSMQCYISTLAVLLKSTNSKPWVNEFESIELSCMIESITTTKPRIEWKKIKNGDPSYVYFDNQISGDLERRAKIREPATLVILNATRSDSADYRCEVTAPNDQKSFDEILISLTVRVKPVVPRCSVPKSIPVGKPAELHCLEDEGYPKSQYQWFRNKEEIPLDPKSSPKFFNSTYTLDGEMGTLKFSAVRKEDAGEYYCRAKNEAGISECGPQMMEVYDINIAGIILGVVVVVMVLLCITVGIFCAYKRGYFTSQKQTGNNYKPPAKGDGVDYVRTEDEGDFRHKSSFVI
Protein: Vesicle-associated membrane protein-associated protein A (VAMP-A) (VAMP-associated protein A) (VAP-A) (33 kDa VAMP-associated protein) (VAP-33) (Q9P0L0)
Organism: Homo sapiens (Human)
Function: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With OSBPL3, may regulate ER morphology. May play a role in vesicle trafficking.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:19289470, ECO:0000269|PubMed:25447204, ECO:0000269|PubMed:30741634, ECO:0000269|PubMed:32344433, ECO:0000269|PubMed:33124732}; Single-pass type IV membrane protein {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19289470}. Cell membrane {ECO:0000269|PubMed:25447204}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000269|PubMed:10523508}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Z270}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000269|PubMed:10523508}.
Interaction partners:
- Oxysterol-binding protein 1
- Acyl-CoA-binding domain-containing protein 5
- StAR-related lipid transfer protein 3
- Ceramide transfer protein
- Oxysterol-binding protein-related protein 9
- Vesicle-associated membrane protein-associated protein B/C
- Oxysterol-binding protein 2
- STARD3 N-terminal-like protein
- Protrudin
- Acyl-CoA-binding domain-containing protein 4
Sequence:
MASASGAMAKHEQILVLDPPTDLKFKGPFTDVVTTNLKLRNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSTVTVSVMLQPFDYDPNEKSKHKFMVQTIFAPPNTSDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPMPKPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSTASFRDNVTSPLPSLLVVIAAIFIGFFLGKFIL
Protein: Alpha-1-antitrypsin (Alpha-1 protease inhibitor) (Alpha-1-antiproteinase) (Serpin A1) [Cleaved into: Short peptide from AAT (SPAAT)] (P01009)
Organism: Homo sapiens (Human)
Function: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.
Subcellular location: Secreted. Endoplasmic reticulum. Note=The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Short peptide from AAT]: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Neutrophil elastase
- Albumin
- Alpha-2-macroglobulin
- Alpha-1-acid glycoprotein 1
- Trypsin-2
- Alpha-1-acid glycoprotein 2
- Alpha-2-HS-glycoprotein
- Chymotrypsin-like elastase family member 1
- Transthyretin
- Haptoglobin
Sequence:
MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Protein: Achaete-scute complex protein T3 (Protein lethal of scute) (Lethal of sc) (P09774)
Organism: Drosophila melanogaster (Fruit fly)
Function: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system.
Interaction partners:
- Protein daughterless
- Achaete-scute complex protein T5
- Achaete-scute complex protein T4
- Bearded
- Insulin-like peptide 4
- Protein atonal
- Protein deadpan
- Enhancer of split m8 protein
Sequence:
MTSICSSKFQQQHYQLTNSNIFLLQHQHHHQTQQHQLIAPKIPLGTSQLQNMQQSQQSNVGPMLSSQKKKFNYNNMPYGEQLPSVARRNARERNRVKQVNNGFVNLRQHLPQTVVNSLSNGGRGSSKKLSKVDTLRIAVEYIRGLQDMLDDGTASSTRHIYNSADESSNDGSSYNDYNDSLDSSQQFLTGATQSAQSHSYHSASPTPSYSGSEISGGGYIKQELQEQDLKFDSFDSFSDEQPDDEELLDYISSWQEQ
Protein: Carbonic anhydrase (EC 4.2.1.1) (A2IBE2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPHCSLHATVVLLLVILKEQPSSSAPLNGSKWTYIGPAGEKNWSKKYPSCGGLLQSPIDLHSDILQYDASLAPLQFQGYNVSVEKLLNLTNDGHSVRLNLNSDMYIQGLQPHQYRAEQLHLHWGNRNDPHGSEHTVSGKHFAAELHIVHYNSDLYSDFGSASDKSEGLAVLAVLIEIGSVNPSYDKIFSHLQHVKYKGQQVLIPGFNIEELLPESPGEYYRYEGSLTTPPCYPTVLWTVFRNPVQISQEQLLALETALYFTHMDDPSPREMVNNFRQVQKFDERLVYISFRQGLLTDTGLSLGIILSVALAGVLGISIVLAVSVWLFKRKKSKKGDNKGVIYKPAIKKEAEVHA
Protein: 3-hydroxylaminophenol mutase (3HAP mutase) (EC 5.4.4.3) (3-(hydroxyamino)phenol mutase) (Q46ZL2)
Organism: Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134))
Function: Catalyzes the isomerization of 3-hydroxylaminophenol (3HAP) to aminohydroquinone, a step in the degradative pathway of 3-nitrophenol. The enzymatic reaction is regiospecific since it leads to the formation of aminohydroquinone exclusively, without producing the isomeric 4-aminocatechol. Can also isomerize other hydroxylaminoaromatic compounds, such as hydroxylaminobenzene to a mixture of 2-aminophenol and 4-aminophenol, 4-hydroxylaminotoluene to 6-amino-m-cresol, and 2-chloro-5-hydroxylaminophenol to 2-amino-5-chlorohydroquinone. Does not act on 4-hydroxylaminobenzoate.
Interaction partners:
- Glutamate synthase large chain
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- histidine kinase
Sequence:
MAQSVADVMKLVKENDVKFVDFRFTDTKGKEQHVSVPTSHFDDDKFESGHAFDGSSIAGWKGIEASDMLLMPDSNTAFIDPFYEEPTLVLTCDVVEPSDGKGYDRDPRSIAKRAEAYLKSTGLGDTAFFGPEPEFFIFDGVTWNVDMQGCFVKVHSEEAPWSSGKEFEHGNSGHRPGKKGGYFPVAPIDTFQDMRSEMCLILESLGIPVEVHHHEVAGQGQNEIGTRFSTLVQRADWTQLQKYVIQNVAHTYGKTATFMPKPIVGDNGSGMHVHQSVWKDGQNLFAGNGYAGLSEFALYYIGGIIKHARALNAITNPGTNSYKRLVPGFEAPVKLAYSARNRSASIRIPYVANPKGRRIETRFPDPLMNPYLGFSALLMAGLDGVMNKIHPGEAADKNLYDLPPEEDAKIPTVCNSLDQSLEYLDNDREFLTRGGVFSNSMLDAYIELKMEEVTRFRMTTHPVEFEMYYSL