CPLM-005177

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-005177

UniProt Accession

PTPRD_HUMAN; P23468; B1ALA0; Q3KPJ0; Q3KPJ1; Q3KPJ2

Genbank Protein ID

L38929; AL137125; AL356584; AL445926; AL583805; AL590397; AL356584; AL137125; AL445926; AL583805; AL590397; AL445926; AL137125; AL356584; AL583805; AL590397; AL583805; AL137125; AL356584; AL445926; AL590397; AL590397; AL137125; AL356584; AL445926; AL583805; BC106713; BC106714; BC106715; X54133

Genbank Nucleotide ID

AAC41749.1; CAH70912.2; CAH70912.2; CAH70912.2; CAH70912.2; CAH70912.2; CAI16146.2; CAI16146.2; CAI16146.2; CAI16146.2; CAI16146.2; CAH73847.2; CAH73847.2; CAH73847.2; CAH73847.2; CAH73847.2; CAH70443.2; CAH70443.2; CAH70443.2; CAH70443.2; CAH70443.2; CAH73128.2; CAH73128.2; CAH73128.2; CAH73128.2; CAH73128.2; AAI06714.1; AAI06715.1; AAI06716.1; CAA38068.1

Protein Name

Receptor-type tyrosine-protein phosphatase delta

Protein Synonyms/Alias

Protein-tyrosine phosphatase delta; R-PTP-delta

Gene Name

PTPRD

Gene Synonyms/Alias

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
1381	HSNLEVNKPKNRYAN	ubiquitination	[1]
1649	TGMELEFKRLASSKA	ubiquitination	[1]
1670	SANLPCNKFKNRLVN	ubiquitination	[1]

Reference

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

Functional Description

Sequence Annotation

DOMAIN 24 114 Ig-like C2-type 1.
DOMAIN 126 224 Ig-like C2-type 2.
DOMAIN 236 318 Ig-like C2-type 3.
DOMAIN 323 411 Fibronectin type-III 1.
DOMAIN 417 511 Fibronectin type-III 2.
DOMAIN 516 604 Fibronectin type-III 3.
DOMAIN 609 706 Fibronectin type-III 4.
DOMAIN 711 819 Fibronectin type-III 5.
DOMAIN 824 913 Fibronectin type-III 6.
DOMAIN 918 1013 Fibronectin type-III 7.
DOMAIN 1017 1103 Fibronectin type-III 8.
DOMAIN 1357 1612 Tyrosine-protein phosphatase 1.
DOMAIN 1644 1903 Tyrosine-protein phosphatase 2.
REGION 180 189 Interaction with IL1RAPL1 (By
REGION 1553 1559 Substrate binding (By similarity).
ACT_SITE 1553 1553 Phosphocysteine intermediate (By
ACT_SITE 1844 1844 Phosphocysteine intermediate (By
BINDING 1521 1521 Substrate (By similarity).
BINDING 1597 1597 Substrate (By similarity).
CARBOHYD 254 254 N-linked (GlcNAc...) (Potential).
CARBOHYD 299 299 N-linked (GlcNAc...) (Potential).
CARBOHYD 724 724 N-linked (GlcNAc...) (Potential).
CARBOHYD 832 832 N-linked (GlcNAc...) (Potential).
DISULFID 45 98 Potential.
DISULFID 147 207 Potential.
DISULFID 257 302 Potential.

Keyword

3D-structure; Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; Polymorphism; Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1912 AA

Protein Sequence

MVHVARLLLL LLTFFLRTDA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK 60
GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ 120
IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS 180
ESIGGTPIRG ALQIEQSEES DQGKYECVAT NSAGTRYSAP ANLYVRELRE VRRVPPRFSI 240
PPTNHEIMPG GSVNITCVAV GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LNDVRQSANY 300
TCVAMSTLGV IEAIAQITVK ALPKPPGTPV VTESTATSIT LTWDSGNPEP VSYYIIQHKP 360
KNSEELYKEI DGVATTRYSV AGLSPYSDYE FRVVAVNNIG RGPPSEPVLT QTSEQAPSSA 420
PRDVQARMLS STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG 480
NLVPQKTYSV KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR 540
SDTIANYELV YKDGEHGEEQ RITIEPGTSY RLQGLKPNSL YYFRLAARSP QGLGASTAEI 600
SARTMQSKPS APPQDISCTS PSSTSILVSW QPPPVEKQNG IITEYSIKYT AVDGEDDKPH 660
EILGIPSDTT KYLLEQLEKW TEYRITVTAH TDVGPGPESL SVLIRTNEDV PSGPPRKVEV 720
EAVNSTSVKV SWRSPVPNKQ HGQIRGYQVH YVRMENGEPK GQPMLKDVML ADAQWEFDDT 780
TEHDMIISGL QPETSYSLTV TAYTTKGDGA RSKPKLVSTT GAVPGKPRLV INHTQMNTAL 840
IQWHPPVDTF GPLQGYRLKF GRKDMEPLTT LEFSEKEDHF TATDIHKGAS YVFRLSARNK 900
VGFGEEMVKE ISIPEEVPTG FPQNLHSEGT TSTSVQLSWQ PPVLAERNGI ITKYTLLYRD 960
INIPLLPMEQ LIVPADTTMT LTGLKPDTTY DVKVRAHTSK GPGPYSPSVQ FRTLPVDQVF 1020
AKNFHVKAVM KTSVLLSWEI PENYNSAMPF KILYDDGKMV EEVDGRATQK LIVNLKPEKS 1080
YSFVLTNRGN SAGGLQHRVT AKTAPDVLRT KPAFIGKTNL DGMITVQLPE VPANENIKGY 1140
YIIIVPLKKS RGKFIKPWES PDEMELDELL KEISRKRRSI RYGREVELKP YIAAHFDVLP 1200
TEFTLGDDKH YGGFTNKQLQ SGQEYVFFVL AVMEHAESKM YATSPYSDPV VSMDLDPQPI 1260
TDEEEGLIWV VGPVLAVVFI ICIVIAILLY KRKRAESDSR KSSIPNNKEI PSHHPTDPVE 1320
LRRLNFQTPG MASHPPIPIL ELADHIERLK ANDNLKFSQE YESIDPGQQF TWEHSNLEVN 1380
KPKNRYANVI AYDHSRVLLS AIEGIPGSDY VNANYIDGYR KQNAYIATQG SLPETFGDFW 1440
RMIWEQRSAT VVMMTKLEER SRVKCDQYWP SRGTETHGLV QVTLLDTVEL ATYCVRTFAL 1500
YKNGSSEKRE VRQFQFTAWP DHGVPEHPTP FLAFLRRVKT CNPPDAGPMV VHCSAGVGRT 1560
GCFIVIDAML ERIKHEKTVD IYGHVTLMRA QRNYMVQTED QYIFIHDALL EAVTCGNTEV 1620
PARNLYAYIQ KLTQIETGEN VTGMELEFKR LASSKAHTSR FISANLPCNK FKNRLVNIMP 1680
YESTRVCLQP IRGVEGSDYI NASFIDGYRQ QKAYIATQGP LAETTEDFWR MLWEHNSTIV 1740
VMLTKLREMG REKCHQYWPA ERSARYQYFV VDPMAEYNMP QYILREFKVT DARDGQSRTV 1800
RQFQFTDWPE QGVPKSGEGF IDFIGQVHKT KEQFGQDGPI SVHCSAGVGR TGVFITLSIV 1860
LERMRYEGVV DIFQTVKMLR TQRPAMVQTE DQYQFSYRAA LEYLGSFDHY AT 1912

Gene Ontology

GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
GO:0005102; F:receptor binding; ISS:BHF-UCL.
GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
GO:0007157; P:heterophilic cell-cell adhesion; ISS:BHF-UCL.
GO:0030182; P:neuron differentiation; ISS:BHF-UCL.
GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:BHF-UCL.
GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:ProtInc.

Interpro

IPR003961; Fibronectin_type3.
IPR007110; Ig-like_dom.
IPR013783; Ig-like_fold.
IPR013098; Ig_I-set.
IPR003598; Ig_sub2.
IPR000387; Tyr/Dual-sp_Pase.
IPR016130; Tyr_Pase_AS.
IPR000242; Tyr_Pase_rcpt/non-rcpt.

Pfam

PF00041; fn3
PF07679; I-set
PF00102; Y_phosphatase

SMART

SM00060; FN3
SM00408; IGc2
SM00194; PTPc

PROSITE

PS50853; FN3
PS50835; IG_LIKE
PS00383; TYR_PHOSPHATASE_1
PS50056; TYR_PHOSPHATASE_2
PS50055; TYR_PHOSPHATASE_PTP

PRINTS

PR00700; PRTYPHPHTASE.