ID PALD_HUMAN Reviewed; 856 AA.
AC Q9ULE6; B2RMS1; B9EGC6; Q5JTK7; Q5JTK8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Paladin;
GN Name=PALD1; Synonyms=KIAA1274, PALD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-141.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-141.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22354871; DOI=10.1002/dvdy.23753;
RA Wallgard E., Nitzsche A., Larsson J., Guo X., Dieterich L.C., Dimberg A.,
RA Olofsson T., Ponten F.C., Makinen T., Kalen M., Hellstrom M.;
RT "Paladin (X99384) is expressed in the vasculature and shifts from
RT endothelial to vascular smooth muscle cells during mouse development.";
RL Dev. Dyn. 241:770-786(2012).
CC -!- INTERACTION:
CC Q9ULE6; Q92985: IRF7; NbExp=2; IntAct=EBI-3957166, EBI-968267;
CC Q9ULE6; A2APF7: Zbp1; Xeno; NbExp=2; IntAct=EBI-3957166, EBI-6115394;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22354871}.
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells, and in certain
CC larger vessels, in mural cells. In the brain, possibly expressed in
CC microglia. Expressed in peripheral blood mononuclear cells (at protein
CC level). {ECO:0000269|PubMed:22354871}.
CC -!- SIMILARITY: Belongs to the paladin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86588.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB033100; BAA86588.2; ALT_INIT; mRNA.
DR EMBL; AC022532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136375; AAI36376.1; -; mRNA.
DR EMBL; BC136376; AAI36377.1; -; mRNA.
DR CCDS; CCDS31215.1; -.
DR RefSeq; NP_055246.2; NM_014431.2.
DR RefSeq; XP_011537939.1; XM_011539637.2.
DR RefSeq; XP_011537940.1; XM_011539638.2.
DR RefSeq; XP_016871561.1; XM_017016072.1.
DR AlphaFoldDB; Q9ULE6; -.
DR BioGRID; 118028; 100.
DR ELM; Q9ULE6; -.
DR IntAct; Q9ULE6; 18.
DR MINT; Q9ULE6; -.
DR STRING; 9606.ENSP00000263563; -.
DR DEPOD; PALD1; -.
DR GlyGen; Q9ULE6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULE6; -.
DR PhosphoSitePlus; Q9ULE6; -.
DR BioMuta; PALD1; -.
DR DMDM; 146325028; -.
DR EPD; Q9ULE6; -.
DR jPOST; Q9ULE6; -.
DR MassIVE; Q9ULE6; -.
DR MaxQB; Q9ULE6; -.
DR PaxDb; 9606-ENSP00000263563; -.
DR PeptideAtlas; Q9ULE6; -.
DR ProteomicsDB; 85011; -.
DR Pumba; Q9ULE6; -.
DR Antibodypedia; 2835; 107 antibodies from 20 providers.
DR DNASU; 27143; -.
DR Ensembl; ENST00000263563.7; ENSP00000263563.5; ENSG00000107719.10.
DR GeneID; 27143; -.
DR KEGG; hsa:27143; -.
DR MANE-Select; ENST00000263563.7; ENSP00000263563.5; NM_014431.3; NP_055246.2.
DR UCSC; uc001jrd.5; human.
DR AGR; HGNC:23530; -.
DR CTD; 27143; -.
DR DisGeNET; 27143; -.
DR GeneCards; PALD1; -.
DR HGNC; HGNC:23530; PALD1.
DR HPA; ENSG00000107719; Low tissue specificity.
DR MIM; 614656; gene.
DR neXtProt; NX_Q9ULE6; -.
DR OpenTargets; ENSG00000107719; -.
DR PharmGKB; PA134986569; -.
DR VEuPathDB; HostDB:ENSG00000107719; -.
DR eggNOG; ENOG502QQ90; Eukaryota.
DR GeneTree; ENSGT00390000005448; -.
DR HOGENOM; CLU_008167_0_0_1; -.
DR InParanoid; Q9ULE6; -.
DR OMA; WLCTHPE; -.
DR OrthoDB; 49159at2759; -.
DR PhylomeDB; Q9ULE6; -.
DR TreeFam; TF332292; -.
DR PathwayCommons; Q9ULE6; -.
DR SignaLink; Q9ULE6; -.
DR BioGRID-ORCS; 27143; 8 hits in 1140 CRISPR screens.
DR ChiTaRS; PALD1; human.
DR GenomeRNAi; 27143; -.
DR Pharos; Q9ULE6; Tbio.
DR PRO; PR:Q9ULE6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9ULE6; Protein.
DR Bgee; ENSG00000107719; Expressed in tendon of biceps brachii and 127 other cell types or tissues.
DR ExpressionAtlas; Q9ULE6; baseline and differential.
DR Genevisible; Q9ULE6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR CDD; cd17659; PTP_paladin_1; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR23339:SF96; PALADIN; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF14566; PTPlike_phytase; 2.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM01301; PTPlike_phytase; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipoprotein; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..856
FT /note="Paladin"
FT /id="PRO_0000286130"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70261"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681"
FT VARIANT 141
FT /note="S -> L (in dbSNP:rs2275060)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_032076"
FT VARIANT 721
FT /note="R -> C (in dbSNP:rs3740447)"
FT /id="VAR_032077"
FT VARIANT 828
FT /note="G -> R (in dbSNP:rs10999406)"
FT /id="VAR_062188"
SQ SEQUENCE 856 AA; 96754 MW; BFCDD78DB2D4BE3B CRC64;
MGTTASTAQQ TVSAGTPFEG LQGSGTMDSR HSVSIHSFQS TSLHNSKAKS IIPNKVAPVV
ITYNCKEEFQ IHDELLKAHY TLGRLSDNTP EHYLVQGRYF LVRDVTEKMD VLGTVGSCGA
PNFRQVQGGL TVFGMGQPSL SGFRRVLQKL QKDGHRECVI FCVREEPVLF LRADEDFVSY
TPRDKQNLHE NLQGLGPGVR VESLELAIRK EIHDFAQLSE NTYHVYHNTE DLWGEPHAVA
IHGEDDLHVT EEVYKRPLFL QPTYRYHRLP LPEQGSPLEA QLDAFVSVLR ETPSLLQLRD
AHGPPPALVF SCQMGVGRTN LGMVLGTLIL LHRSGTTSQP EAAPTQAKPL PMEQFQVIQS
FLRMVPQGRR MVEEVDRAIT ACAELHDLKE VVLENQKKLE GIRPESPAQG SGSRHSVWQR
ALWSLERYFY LILFNYYLHE QYPLAFALSF SRWLCAHPEL YRLPVTLSSA GPVAPRDLIA
RGSLREDDLV SPDALSTVRE MDVANFRRVP RMPIYGTAQP SAKALGSILA YLTDAKRRLR
KVVWVSLREE AVLECDGHTY SLRWPGPPVA PDQLETLEAQ LKAHLSEPPP GKEGPLTYRF
QTCLTMQEVF SQHRRACPGL TYHRIPMPDF CAPREEDFDQ LLEALRAALS KDPGTGFVFS
CLSGQGRTTT AMVVAVLAFW HIQGFPEVGE EELVSVPDAK FTKGEFQVVM KVVQLLPDGH
RVKKEVDAAL DTVSETMTPM HYHLREIIIC TYRQAKAAKE AQEMRRLQLR SLQYLERYVC
LILFNAYLHL EKADSWQRPF STWMQEVASK AGIYEILNEL GFPELESGED QPFSRLRYRW
QEQSCSLEPS APEDLL
//
