CD44_HUMAN - dbPTM
CD44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD44_HUMAN
UniProt AC P16070
Protein Name CD44 antigen
Gene Name CD44
Organism Homo sapiens (Human).
Sequence Length 742
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, microvillus . Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli.
Protein Description Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events. Receptor for LGALS9; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity)..
Protein Sequence MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTADETRNLQNVDMKIGV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
21Pyrrolidone_carboxylic_acidLVPLSLAQIDLNITC
HHCHHHHHCCCCEEE
34.71-
25N-linked_GlycosylationSLAQIDLNITCRFAG
HHHHCCCCEEEEEEE
24.63UniProtKB CARBOHYD
45PhosphorylationKNGRYSISRTEAADL
ECCEEEEEHHHHHHH
27.4918669648
45 (in isoform 10)Phosphorylation-27.49-
45 (in isoform 12)Phosphorylation-27.49-
45 (in isoform 19)Phosphorylation-27.49-
45 (in isoform 4)Phosphorylation-27.49-
54UbiquitinationTEAADLCKAFNSTLP
HHHHHHHHHHHCCCH
64.4121963094
57N-linked_GlycosylationADLCKAFNSTLPTMA
HHHHHHHHCCCHHHH
38.6617623646
57N-linked_GlycosylationADLCKAFNSTLPTMA
HHHHHHHHCCCHHHH
38.6616335952
57 (in isoform 10)N-linked_Glycosylation-38.66-
57 (in isoform 12)N-linked_Glycosylation-38.66-
57 (in isoform 19)N-linked_Glycosylation-38.66-
57 (in isoform 4)N-linked_Glycosylation-38.66-
58PhosphorylationDLCKAFNSTLPTMAQ
HHHHHHHCCCHHHHH
25.5218669648
58 (in isoform 10)Phosphorylation-25.52-
58 (in isoform 12)Phosphorylation-25.52-
58 (in isoform 19)Phosphorylation-25.52-
58 (in isoform 4)Phosphorylation-25.52-
62PhosphorylationAFNSTLPTMAQMEKA
HHHCCCHHHHHHHHH
28.4018669648
62 (in isoform 10)Phosphorylation-28.40-
62 (in isoform 12)Phosphorylation-28.40-
62 (in isoform 19)Phosphorylation-28.40-
62 (in isoform 4)Phosphorylation-28.40-
77S-palmitoylationLSIGFETCRYGFIEG
HHHCCCCCCCCEEEC
2.1929575903
79PhosphorylationIGFETCRYGFIEGHV
HCCCCCCCCEEECEE
20.6628152594
100N-linked_GlycosylationPNSICAANNTGVYIL
CCCEEECCCCEEEEE
28.24UniProtKB CARBOHYD
102 (in isoform 19)Phosphorylation-28.0324275748
110N-linked_GlycosylationGVYILTSNTSQYDTY
EEEEEECCCCCCCEE
38.2219159218
120N-linked_GlycosylationQYDTYCFNASAPPEE
CCCEEEEECCCCCHH
29.44UniProtKB CARBOHYD
130O-linked_GlycosylationAPPEEDCTSVTDLPN
CCCHHHCCCCCCCCC
38.26OGP
133O-linked_GlycosylationEEDCTSVTDLPNAFD
HHHCCCCCCCCCCCC
31.42OGP
155PhosphorylationVNRDGTRYVQKGEYR
ECCCCCEEEECCCCC
13.6828152594
1582-HydroxyisobutyrylationDGTRYVQKGEYRTNP
CCCEEEECCCCCCCH
43.60-
158UbiquitinationDGTRYVQKGEYRTNP
CCCEEEECCCCCCCH
43.6021963094
158 (in isoform 10)Ubiquitination-43.60-
163PhosphorylationVQKGEYRTNPEDIYP
EECCCCCCCHHHCCC
54.9823927012
169PhosphorylationRTNPEDIYPSNPTDD
CCCHHHCCCCCCCCC
16.9623927012
171PhosphorylationNPEDIYPSNPTDDDV
CHHHCCCCCCCCCCC
38.1728985074
174O-linked_GlycosylationDIYPSNPTDDDVSSG
HCCCCCCCCCCCCCC
57.2055830835
174PhosphorylationDIYPSNPTDDDVSSG
HCCCCCCCCCCCCCC
57.2028450419
179PhosphorylationNPTDDDVSSGSSSER
CCCCCCCCCCCCCCC
35.6628450419
180PhosphorylationPTDDDVSSGSSSERS
CCCCCCCCCCCCCCC
42.4128450419
182PhosphorylationDDDVSSGSSSERSST
CCCCCCCCCCCCCCC
32.4123927012
183PhosphorylationDDVSSGSSSERSSTS
CCCCCCCCCCCCCCC
39.4823927012
184PhosphorylationDVSSGSSSERSSTSG
CCCCCCCCCCCCCCC
38.4323927012
188 (in isoform 16)Phosphorylation-32.5822210691
188 (in isoform 3)Phosphorylation-32.5822210691
196 (in isoform 16)Phosphorylation-9.4122210691
196 (in isoform 3)Phosphorylation-9.4122210691
197O-linked_GlycosylationSGGYIFYTFSTVHPI
CCCEEEEEEEEECCC
10.6055833039
199O-linked_GlycosylationGYIFYTFSTVHPIPD
CEEEEEEEEECCCCC
23.0155833043
199 (in isoform 16)Phosphorylation-23.0122210691
199 (in isoform 3)Phosphorylation-23.0122210691
200O-linked_GlycosylationYIFYTFSTVHPIPDE
EEEEEEEEECCCCCC
20.7455833047
222PhosphorylationSTDRIPATTLMSTSA
CCCCCCCHHEECCCC
18.33-
271O-linked_GlycosylationMAGTSSNTISAGWEP
ECCCCCCCCCCCCCC
20.46OGP
277UbiquitinationNTISAGWEPNEENED
CCCCCCCCCCCCCCC
37.0123000965
278UbiquitinationTISAGWEPNEENEDE
CCCCCCCCCCCCCCC
47.2023000965
279UbiquitinationISAGWEPNEENEDER
CCCCCCCCCCCCCCC
58.6723000965
286S-palmitoylationNEENEDERDRHLSFS
CCCCCCCCHHCCCCC
59.5924512624
291PhosphorylationDERDRHLSFSGSGID
CCCHHCCCCCCCCCC
15.9612032545
291 (in isoform 12)Phosphorylation-15.96-
293UbiquitinationRDRHLSFSGSGIDDD
CHHCCCCCCCCCCCC
28.7727667366
295S-palmitoylationRHLSFSGSGIDDDED
HCCCCCCCCCCCCHH
31.2324512624
298UbiquitinationSFSGSGIDDDEDFIS
CCCCCCCCCCHHHHH
61.9123000965
299UbiquitinationFSGSGIDDDEDFISS
CCCCCCCCCHHHHHH
60.3123000965
300UbiquitinationSGSGIDDDEDFISST
CCCCCCCCHHHHHHH
54.3323000965
300 (in isoform 12)Ubiquitination-54.3321906983
303UbiquitinationGIDDDEDFISSTIST
CCCCCHHHHHHHCCC
5.7021963094
305PhosphorylationDDDEDFISSTISTTP
CCCHHHHHHHCCCCC
22.7920068231
305 (in isoform 12)Phosphorylation-22.79-
311PhosphorylationISSTISTTPRAFDHT
HHHHCCCCCCCCCCC
12.18-
313UbiquitinationSTISTTPRAFDHTKQ
HHCCCCCCCCCCCCC
45.8827667366
314UbiquitinationTISTTPRAFDHTKQN
HCCCCCCCCCCCCCC
18.5427667366
314 (in isoform 12)Ubiquitination-18.5421906983
316 (in isoform 12)Phosphorylation-47.78-
318O-linked_GlycosylationTPRAFDHTKQNQDWT
CCCCCCCCCCCCCCC
35.8555824437
323 (in isoform 12)Phosphorylation-58.92-
324UbiquitinationHTKQNQDWTQWNPSH
CCCCCCCCCCCCCCC
4.8221963094
324 (in isoform 12)Ubiquitination-4.8221906983
325O-linked_GlycosylationTKQNQDWTQWNPSHS
CCCCCCCCCCCCCCC
31.8155828631
325 (in isoform 12)Phosphorylation-31.81-
330O-linked_GlycosylationDWTQWNPSHSNPEVL
CCCCCCCCCCCHHHE
36.0155831243
332O-linked_GlycosylationTQWNPSHSNPEVLLQ
CCCCCCCCCHHHEEE
59.4255831247
334UbiquitinationWNPSHSNPEVLLQTT
CCCCCCCHHHEEEEE
35.7727667366
334 (in isoform 12)Ubiquitination-35.7721906983
335 (in isoform 14)Ubiquitination-50.4721906983
336 (in isoform 12)Phosphorylation-7.34-
337UbiquitinationSHSNPEVLLQTTTRM
CCCCHHHEEEEECCE
2.5327667366
337 (in isoform 12)Phosphorylation-2.53-
338 (in isoform 10)Phosphorylation-5.26-
339 (in isoform 12)Phosphorylation-32.42-
340UbiquitinationNPEVLLQTTTRMTDV
CHHHEEEEECCEEEE
30.0623000965
341UbiquitinationPEVLLQTTTRMTDVD
HHHEEEEECCEEEEC
10.2323000965
342UbiquitinationEVLLQTTTRMTDVDR
HHEEEEECCEEEECC
23.1023000965
349 (in isoform 14)Ubiquitination-43.2421906983
350N-linked_GlycosylationRMTDVDRNGTTAYEG
CEEEECCCCCCCCCC
47.93UniProtKB CARBOHYD
356UbiquitinationRNGTTAYEGNWNPEA
CCCCCCCCCCCCCCC
43.5227667366
358UbiquitinationGTTAYEGNWNPEAHP
CCCCCCCCCCCCCCC
24.3427667366
358 (in isoform 12)Ubiquitination-24.3421906983
359 (in isoform 14)Ubiquitination-32.3921906983
362UbiquitinationYEGNWNPEAHPPLIH
CCCCCCCCCCCCCCC
57.2923000965
363UbiquitinationEGNWNPEAHPPLIHH
CCCCCCCCCCCCCCC
23.0323000965
364UbiquitinationGNWNPEAHPPLIHHE
CCCCCCCCCCCCCCC
23.8923000965
364 (in isoform 13)Ubiquitination-23.8921906983
366UbiquitinationWNPEAHPPLIHHEHH
CCCCCCCCCCCCCCC
33.8023000965
367UbiquitinationNPEAHPPLIHHEHHE
CCCCCCCCCCCCCCC
7.3923000965
368UbiquitinationPEAHPPLIHHEHHEE
CCCCCCCCCCCCCCC
3.7223000965
368 (in isoform 11)Ubiquitination-3.7221906983
369 (in isoform 14)Ubiquitination-28.1521906983
376UbiquitinationHHEHHEEEETPHSTS
CCCCCCCCCCCCCCC
65.2727667366
378UbiquitinationEHHEEEETPHSTSTI
CCCCCCCCCCCCCCE
29.5827667366
378 (in isoform 13)Ubiquitination-29.5821906983
382UbiquitinationEEETPHSTSTIQATP
CCCCCCCCCCEEECC
27.1927667366
382 (in isoform 11)Ubiquitination-27.1921906983
383UbiquitinationEETPHSTSTIQATPS
CCCCCCCCCEEECCC
26.9123000965
384UbiquitinationETPHSTSTIQATPSS
CCCCCCCCEEECCCC
19.7323000965
385UbiquitinationTPHSTSTIQATPSST
CCCCCCCEEECCCCC
2.3523000965
388UbiquitinationSTSTIQATPSSTTEE
CCCCEEECCCCCCCC
13.8221963094
388 (in isoform 13)Ubiquitination-13.8221906983
392UbiquitinationIQATPSSTTEETATQ
EEECCCCCCCCCCCH
42.4321963094
392 (in isoform 11)Ubiquitination-42.4321906983
393 (in isoform 14)Ubiquitination-33.5021906983
398O-linked_GlycosylationSTTEETATQKEQWFG
CCCCCCCCHHHHHHC
47.82OGP
398UbiquitinationSTTEETATQKEQWFG
CCCCCCCCHHHHHHC
47.8227667366
398 (in isoform 13)Ubiquitination-47.8221906983
399UbiquitinationTTEETATQKEQWFGN
CCCCCCCHHHHHHCC
44.8427667366
400UbiquitinationTEETATQKEQWFGNR
CCCCCCHHHHHHCCC
47.7421963094
402UbiquitinationETATQKEQWFGNRWH
CCCCHHHHHHCCCCC
48.0827667366
402 (in isoform 11)Ubiquitination-48.0821906983
409UbiquitinationQWFGNRWHEGYRQTP
HHHCCCCCCCCCCCC
18.5021963094
412O-linked_GlycosylationGNRWHEGYRQTPKED
CCCCCCCCCCCCCCC
9.14142619
412PhosphorylationGNRWHEGYRQTPKED
CCCCCCCCCCCCCCC
9.14-
419UbiquitinationYRQTPKEDSHSTTGT
CCCCCCCCCCCCCCC
58.7527667366
420PhosphorylationRQTPKEDSHSTTGTA
CCCCCCCCCCCCCCC
22.04-
422O-linked_GlycosylationTPKEDSHSTTGTAAA
CCCCCCCCCCCCCCH
31.4555835023
422PhosphorylationTPKEDSHSTTGTAAA
CCCCCCCCCCCCCCH
31.45-
422UbiquitinationTPKEDSHSTTGTAAA
CCCCCCCCCCCCCCH
31.4521963094
422 (in isoform 13)Ubiquitination-31.4521906983
423O-linked_GlycosylationPKEDSHSTTGTAAAS
CCCCCCCCCCCCCHH
24.6655835027
423PhosphorylationPKEDSHSTTGTAAAS
CCCCCCCCCCCCCHH
24.66-
423 (in isoform 10)Phosphorylation-24.66-
424O-linked_GlycosylationKEDSHSTTGTAAASA
CCCCCCCCCCCCHHC
35.2355835033
424PhosphorylationKEDSHSTTGTAAASA
CCCCCCCCCCCCHHC
35.23-
426O-linked_GlycosylationDSHSTTGTAAASAHT
CCCCCCCCCCHHCCC
15.8455835037
426PhosphorylationDSHSTTGTAAASAHT
CCCCCCCCCCHHCCC
15.84-
426UbiquitinationDSHSTTGTAAASAHT
CCCCCCCCCCHHCCC
15.8427667366
426 (in isoform 11)Ubiquitination-15.8421906983
430O-linked_GlycosylationTTGTAAASAHTSHPM
CCCCCCHHCCCCCCC
18.8255835043
430UbiquitinationTTGTAAASAHTSHPM
CCCCCCHHCCCCCCC
18.8223000965
431UbiquitinationTGTAAASAHTSHPMQ
CCCCCHHCCCCCCCC
12.7823000965
432UbiquitinationGTAAASAHTSHPMQG
CCCCHHCCCCCCCCC
25.9623000965
432 (in isoform 10)Ubiquitination-25.9621906983
433O-linked_GlycosylationTAAASAHTSHPMQGR
CCCHHCCCCCCCCCC
28.5755835049
434O-linked_GlycosylationAAASAHTSHPMQGRT
CCHHCCCCCCCCCCC
18.7455835053
437 (in isoform 10)Phosphorylation-5.74-
443UbiquitinationPMQGRTTPSPEDSSW
CCCCCCCCCCCCCCC
47.4721963094
446UbiquitinationGRTTPSPEDSSWTDF
CCCCCCCCCCCCHHC
74.9027667366
446 (in isoform 10)Ubiquitination-74.9021906983
448PhosphorylationTTPSPEDSSWTDFFN
CCCCCCCCCCHHCCC
26.5520068231
448 (in isoform 10)Phosphorylation-26.55-
455 (in isoform 10)Phosphorylation-32.75-
456UbiquitinationSWTDFFNPISHPMGR
CCHHCCCCCCCCCCC
25.0521963094
456 (in isoform 10)Ubiquitination-25.0521906983
457 (in isoform 10)Phosphorylation-6.57-
458O-linked_GlycosylationTDFFNPISHPMGRGH
HHCCCCCCCCCCCCC
23.8555833737
466UbiquitinationHPMGRGHQAGRRMDM
CCCCCCCCCCCCCCC
48.6227667366
466 (in isoform 10)Ubiquitination-48.6221906983
468 (in isoform 10)Phosphorylation-15.91-
469 (in isoform 10)Phosphorylation-33.49-
471 (in isoform 10)Phosphorylation-4.89-
472UbiquitinationHQAGRRMDMDSSHSI
CCCCCCCCCCCCCCE
35.6123000965
473UbiquitinationQAGRRMDMDSSHSIT
CCCCCCCCCCCCCEE
3.8323000965
474UbiquitinationAGRRMDMDSSHSITL
CCCCCCCCCCCCEEE
42.6023000965
475UbiquitinationGRRMDMDSSHSITLQ
CCCCCCCCCCCEEEC
24.2623000965
476UbiquitinationRRMDMDSSHSITLQP
CCCCCCCCCCEEECC
19.5923000965
478O-linked_GlycosylationMDMDSSHSITLQPTA
CCCCCCCCEEECCCC
21.15OGP
480O-linked_GlycosylationMDSSHSITLQPTANP
CCCCCCEEECCCCCC
23.50OGP
484O-linked_GlycosylationHSITLQPTANPNTGL
CCEEECCCCCCCCCC
26.55OGP
488UbiquitinationLQPTANPNTGLVEDL
ECCCCCCCCCCCCCH
46.7327667366
489O-linked_GlycosylationQPTANPNTGLVEDLD
CCCCCCCCCCCCCHH
32.90OGP
490UbiquitinationPTANPNTGLVEDLDR
CCCCCCCCCCCCHHC
34.0727667366
490 (in isoform 10)Ubiquitination-34.0721906983
498UbiquitinationLVEDLDRTGPLSMTT
CCCCHHCCCCCCEEE
42.7021963094
500UbiquitinationEDLDRTGPLSMTTQQ
CCHHCCCCCCEEECC
22.2021963094
508UbiquitinationLSMTTQQSNSQSFST
CCEEECCCCCCCCCC
28.7327667366
510UbiquitinationMTTQQSNSQSFSTSH
EEECCCCCCCCCCCC
32.2327667366
514O-linked_GlycosylationQSNSQSFSTSHEGLE
CCCCCCCCCCCCCCC
33.9655830889
515O-linked_GlycosylationSNSQSFSTSHEGLEE
CCCCCCCCCCCCCCC
31.9055830895
515UbiquitinationSNSQSFSTSHEGLEE
CCCCCCCCCCCCCCC
31.9023000965
516UbiquitinationNSQSFSTSHEGLEED
CCCCCCCCCCCCCCC
20.5323000965
517UbiquitinationSQSFSTSHEGLEEDK
CCCCCCCCCCCCCCC
32.9823000965
518UbiquitinationQSFSTSHEGLEEDKD
CCCCCCCCCCCCCCC
66.3023000965
519UbiquitinationSFSTSHEGLEEDKDH
CCCCCCCCCCCCCCC
32.7223000965
528O-linked_GlycosylationEEDKDHPTTSTLTSS
CCCCCCCCCCCCCCC
29.9355830901
529O-linked_GlycosylationEDKDHPTTSTLTSSN
CCCCCCCCCCCCCCC
24.9455830907
531UbiquitinationKDHPTTSTLTSSNRN
CCCCCCCCCCCCCCC
31.7827667366
532UbiquitinationDHPTTSTLTSSNRND
CCCCCCCCCCCCCCC
4.3621963094
533UbiquitinationHPTTSTLTSSNRNDV
CCCCCCCCCCCCCCC
30.1427667366
534UbiquitinationPTTSTLTSSNRNDVT
CCCCCCCCCCCCCCC
28.8221963094
541O-linked_GlycosylationSSNRNDVTGGRRDPN
CCCCCCCCCCCCCCC
36.4655823915
541UbiquitinationSSNRNDVTGGRRDPN
CCCCCCCCCCCCCCC
36.4621963094
543UbiquitinationNRNDVTGGRRDPNHS
CCCCCCCCCCCCCCC
16.4621963094
544 (in isoform 4)Phosphorylation-40.97-
548N-linked_GlycosylationTGGRRDPNHSEGSTT
CCCCCCCCCCCCCCE
56.45UniProtKB CARBOHYD
550O-linked_GlycosylationGRRDPNHSEGSTTLL
CCCCCCCCCCCCEEE
50.7455826893
551UbiquitinationRRDPNHSEGSTTLLE
CCCCCCCCCCCEEEE
50.0027667366
553O-linked_GlycosylationDPNHSEGSTTLLEGY
CCCCCCCCCEEEEEC
17.7355826897
553UbiquitinationDPNHSEGSTTLLEGY
CCCCCCCCCEEEEEC
17.7327667366
554O-linked_GlycosylationPNHSEGSTTLLEGYT
CCCCCCCCEEEEECH
32.1155826901
555O-linked_GlycosylationNHSEGSTTLLEGYTS
CCCCCCCEEEEECHH
30.9255826907
560O-linked_GlycosylationSTTLLEGYTSHYPHT
CCEEEEECHHCCCCC
8.8355826913
561O-linked_GlycosylationTTLLEGYTSHYPHTK
CEEEEECHHCCCCCC
21.6455826919
562O-linked_GlycosylationTLLEGYTSHYPHTKE
EEEEECHHCCCCCCC
16.7355826925
567O-linked_GlycosylationYTSHYPHTKESRTFI
CHHCCCCCCCCCCEE
31.8155826929
567PhosphorylationYTSHYPHTKESRTFI
CHHCCCCCCCCCCEE
31.81-
570O-linked_GlycosylationHYPHTKESRTFIPVT
CCCCCCCCCCEEEEC
37.8755827197
570PhosphorylationHYPHTKESRTFIPVT
CCCCCCCCCCEEEEC
37.87-
572O-linked_GlycosylationPHTKESRTFIPVTSA
CCCCCCCCEEEECCC
34.8846183939
572PhosphorylationPHTKESRTFIPVTSA
CCCCCCCCEEEECCC
34.88-
575UbiquitinationKESRTFIPVTSAKTG
CCCCCEEEECCCCCC
21.1021963094
577O-linked_GlycosylationSRTFIPVTSAKTGSF
CCCEEEECCCCCCCC
20.0155829011
577PhosphorylationSRTFIPVTSAKTGSF
CCCEEEECCCCCCCC
20.01-
577UbiquitinationSRTFIPVTSAKTGSF
CCCEEEECCCCCCCC
20.0121963094
578O-linked_GlycosylationRTFIPVTSAKTGSFG
CCEEEECCCCCCCCC
28.1855829017
578PhosphorylationRTFIPVTSAKTGSFG
CCEEEECCCCCCCCC
28.18-
581O-linked_GlycosylationIPVTSAKTGSFGVTA
EEECCCCCCCCCEEE
37.4655835133
583O-linked_GlycosylationVTSAKTGSFGVTAVT
ECCCCCCCCCEEEEE
24.8655835139
587PhosphorylationKTGSFGVTAVTVGDS
CCCCCCEEEEEECCC
18.7818452278
593UbiquitinationVTAVTVGDSNSNVNR
EEEEEECCCCCCCCC
40.0723000965
594UbiquitinationTAVTVGDSNSNVNRS
EEEEECCCCCCCCCH
35.9123000965
595UbiquitinationAVTVGDSNSNVNRSL
EEEECCCCCCCCCHH
42.2023000965
596UbiquitinationVTVGDSNSNVNRSLS
EEECCCCCCCCCHHC
46.2123000965
597UbiquitinationTVGDSNSNVNRSLSG
EECCCCCCCCCHHCC
39.0623000965
599N-linked_GlycosylationGDSNSNVNRSLSGDQ
CCCCCCCCCHHCCCC
31.88UniProtKB CARBOHYD
607 (in isoform 16)Ubiquitination-56.9621906983
609UbiquitinationLSGDQDTFHPSGGSH
HCCCCCCCCCCCCCC
12.2627667366
610UbiquitinationSGDQDTFHPSGGSHT
CCCCCCCCCCCCCCC
20.0827667366
611UbiquitinationGDQDTFHPSGGSHTT
CCCCCCCCCCCCCCC
30.4027667366
612UbiquitinationDQDTFHPSGGSHTTH
CCCCCCCCCCCCCCC
47.4123000965
613UbiquitinationQDTFHPSGGSHTTHG
CCCCCCCCCCCCCCC
46.1823000965
613 (in isoform 8)Ubiquitination-46.1821906983
614UbiquitinationDTFHPSGGSHTTHGS
CCCCCCCCCCCCCCC
22.1623000965
619UbiquitinationSGGSHTTHGSESDGH
CCCCCCCCCCCCCCC
38.6521963094
620UbiquitinationGGSHTTHGSESDGHS
CCCCCCCCCCCCCCC
30.8921963094
621UbiquitinationGSHTTHGSESDGHSH
CCCCCCCCCCCCCCC
26.7321963094
621 (in isoform 16)Ubiquitination-26.7321906983
627O-linked_GlycosylationGSESDGHSHGSQEGG
CCCCCCCCCCCCCCC
34.76OGP
627 (in isoform 8)Ubiquitination-34.7621906983
628UbiquitinationSESDGHSHGSQEGGA
CCCCCCCCCCCCCCC
33.9627667366
629UbiquitinationESDGHSHGSQEGGAN
CCCCCCCCCCCCCCC
33.7627667366
629 (in isoform 4)Phosphorylation-33.76-
630UbiquitinationSDGHSHGSQEGGANT
CCCCCCCCCCCCCCC
21.4527667366
630 (in isoform 17)Ubiquitination-21.4521906983
631UbiquitinationDGHSHGSQEGGANTT
CCCCCCCCCCCCCCC
58.9327667366
631 (in isoform 16)Ubiquitination-58.9321906983
636N-linked_GlycosylationGSQEGGANTTSGPIR
CCCCCCCCCCCCCCC
47.35UniProtKB CARBOHYD
636UbiquitinationGSQEGGANTTSGPIR
CCCCCCCCCCCCCCC
47.3523000965
637O-linked_GlycosylationSQEGGANTTSGPIRT
CCCCCCCCCCCCCCC
23.08UniProtKB CARBOHYD
637UbiquitinationSQEGGANTTSGPIRT
CCCCCCCCCCCCCCC
23.0823000965
637 (in isoform 8)Ubiquitination-23.0821906983
638O-linked_GlycosylationQEGGANTTSGPIRTP
CCCCCCCCCCCCCCC
31.34UniProtKB CARBOHYD
638UbiquitinationQEGGANTTSGPIRTP
CCCCCCCCCCCCCCC
31.3423000965
638 (in isoform 4)Ubiquitination-31.3421906983
638 (in isoform 6)Ubiquitination-31.3421906983
639UbiquitinationEGGANTTSGPIRTPQ
CCCCCCCCCCCCCCC
40.3023000965
640UbiquitinationGGANTTSGPIRTPQI
CCCCCCCCCCCCCCC
21.4023000965
641UbiquitinationGANTTSGPIRTPQIP
CCCCCCCCCCCCCCH
16.8023000965
641 (in isoform 16)Ubiquitination-16.8021906983
642UbiquitinationANTTSGPIRTPQIPE
CCCCCCCCCCCCCHH
9.7523000965
643 (in isoform 4)Phosphorylation-43.41-
644 (in isoform 17)Ubiquitination-21.9221906983
647 (in isoform 8)Ubiquitination-3.3421906983
648UbiquitinationPIRTPQIPEWLIILA
CCCCCCCHHHHHHHH
22.8227667366
650 (in isoform 3)Ubiquitination-6.3621906983
652UbiquitinationPQIPEWLIILASLLA
CCCHHHHHHHHHHHH
2.2527667366
652 (in isoform 4)Ubiquitination-2.2521906983
652 (in isoform 6)Ubiquitination-2.2521906983
652 (in isoform 7)Ubiquitination-2.2521906983
653UbiquitinationQIPEWLIILASLLAL
CCHHHHHHHHHHHHH
2.1727667366
654UbiquitinationIPEWLIILASLLALA
CHHHHHHHHHHHHHH
1.7821963094
654 (in isoform 17)Ubiquitination-1.7821906983
654 (in isoform 4)Phosphorylation-1.78-
655UbiquitinationPEWLIILASLLALAL
HHHHHHHHHHHHHHH
6.4227667366
656UbiquitinationEWLIILASLLALALI
HHHHHHHHHHHHHHH
22.0727667366
661 (in isoform 4)Phosphorylation-6.22-
662UbiquitinationASLLALALILAVCIA
HHHHHHHHHHHHHHH
3.2421963094
662 (in isoform 4)Ubiquitination-3.2421906983
662 (in isoform 6)Ubiquitination-3.2421906983
663UbiquitinationSLLALALILAVCIAV
HHHHHHHHHHHHHHH
1.6121963094
663 (in isoform 4)Phosphorylation-1.61-
664 (in isoform 17)Ubiquitination-2.8021906983
664 (in isoform 3)Ubiquitination-2.8021906983
665UbiquitinationLALALILAVCIAVNS
HHHHHHHHHHHHHHC
6.2721963094
665 (in isoform 16)Ubiquitination-6.2721906983
666UbiquitinationALALILAVCIAVNSR
HHHHHHHHHHHHHCC
1.8621963094
666 (in isoform 7)Ubiquitination-1.8621906983
671 (in isoform 8)Ubiquitination-22.3021906983
672PhosphorylationAVCIAVNSRRRCGQK
HHHHHHHCCCCCCCC
22.1412032545
672UbiquitinationAVCIAVNSRRRCGQK
HHHHHHHCCCCCCCC
22.1427667366
672 (in isoform 4)Ubiquitination-22.1421906983
672 (in isoform 6)Ubiquitination-22.1421906983
673UbiquitinationVCIAVNSRRRCGQKK
HHHHHHCCCCCCCCC
25.5127667366
673 (in isoform 5)Ubiquitination-25.5121906983
674 (in isoform 3)Ubiquitination-37.7521906983
674 (in isoform 4)Phosphorylation-37.75-
675UbiquitinationIAVNSRRRCGQKKKL
HHHHCCCCCCCCCCE
28.0127667366
675 (in isoform 4)Phosphorylation-28.01-
676UbiquitinationAVNSRRRCGQKKKLV
HHHCCCCCCCCCCEE
6.8527667366
676 (in isoform 7)Ubiquitination-6.8521906983
677 (in isoform 4)Phosphorylation-40.30-
678UbiquitinationNSRRRCGQKKKLVIN
HCCCCCCCCCCEEEE
59.0023000965
679UbiquitinationSRRRCGQKKKLVINS
CCCCCCCCCCEEEEC
36.8423000965
680UbiquitinationRRRCGQKKKLVINSG
CCCCCCCCCEEEECC
43.3723000965
681MalonylationRRCGQKKKLVINSGN
CCCCCCCCEEEECCC
55.8326320211
681UbiquitinationRRCGQKKKLVINSGN
CCCCCCCCEEEECCC
55.8323000965
681 (in isoform 1)Ubiquitination-55.8321906983
682UbiquitinationRCGQKKKLVINSGNG
CCCCCCCEEEECCCC
6.8423000965
684 (in isoform 3)Ubiquitination-5.0021906983
686PhosphorylationKKKLVINSGNGAVED
CCCEEEECCCCCCCC
23.6329255136
686 (in isoform 7)Ubiquitination-23.6321906983
687 (in isoform 5)Ubiquitination-31.9121906983
688 (in isoform 17)Ubiquitination-34.7621906983
694UbiquitinationGNGAVEDRKPSGLNG
CCCCCCCCCCCCCCC
39.0027667366
695UbiquitinationNGAVEDRKPSGLNGE
CCCCCCCCCCCCCCC
56.7221906983
695 (in isoform 1)Ubiquitination-56.7221906983
696UbiquitinationGAVEDRKPSGLNGEA
CCCCCCCCCCCCCCC
34.2327667366
696 (in isoform 4)Ubiquitination-34.2321906983
696 (in isoform 6)Ubiquitination-34.2321906983
697PhosphorylationAVEDRKPSGLNGEAS
CCCCCCCCCCCCCCC
59.9723927012
697UbiquitinationAVEDRKPSGLNGEAS
CCCCCCCCCCCCCCC
59.9721963094
697 (in isoform 5)Ubiquitination-59.9721906983
699UbiquitinationEDRKPSGLNGEASKS
CCCCCCCCCCCCCCC
9.7521963094
700UbiquitinationDRKPSGLNGEASKSQ
CCCCCCCCCCCCCCH
50.1921963094
704PhosphorylationSGLNGEASKSQEMVH
CCCCCCCCCCHHHHH
28.6526846344
704UbiquitinationSGLNGEASKSQEMVH
CCCCCCCCCCHHHHH
28.6521963094
705UbiquitinationGLNGEASKSQEMVHL
CCCCCCCCCHHHHHH
64.3121906983
705 (in isoform 1)Ubiquitination-64.3121906983
706DephosphorylationLNGEASKSQEMVHLV
CCCCCCCCHHHHHHH
28.9512032545
706PhosphorylationLNGEASKSQEMVHLV
CCCCCCCCHHHHHHH
28.9529255136
706UbiquitinationLNGEASKSQEMVHLV
CCCCCCCCHHHHHHH
28.9521963094
707 (in isoform 5)Ubiquitination-46.6821906983
708 (in isoform 3)Ubiquitination-50.7121906983
709SulfoxidationEASKSQEMVHLVNKE
CCCCCHHHHHHHCCC
1.4630846556
710 (in isoform 7)Ubiquitination-2.8821906983
714UbiquitinationQEMVHLVNKESSETP
HHHHHHHCCCCCCCC
49.0627667366
7152-HydroxyisobutyrylationEMVHLVNKESSETPD
HHHHHHCCCCCCCCC
52.04-
715AcetylationEMVHLVNKESSETPD
HHHHHHCCCCCCCCC
52.0426051181
715MalonylationEMVHLVNKESSETPD
HHHHHHCCCCCCCCC
52.0426320211
715UbiquitinationEMVHLVNKESSETPD
HHHHHHCCCCCCCCC
52.0427667366
715 (in isoform 1)Ubiquitination-52.0421906983
716UbiquitinationMVHLVNKESSETPDQ
HHHHHCCCCCCCCCC
55.0527667366
717PhosphorylationVHLVNKESSETPDQF
HHHHCCCCCCCCCCC
34.7723401153
718PhosphorylationHLVNKESSETPDQFM
HHHCCCCCCCCCCCC
46.7329255136
720PhosphorylationVNKESSETPDQFMTA
HCCCCCCCCCCCCCH
33.8323401153
725SulfoxidationSETPDQFMTADETRN
CCCCCCCCCHHHHCC
2.2228183972
726PhosphorylationETPDQFMTADETRNL
CCCCCCCCHHHHCCC
32.0424732914
730PhosphorylationQFMTADETRNLQNVD
CCCCHHHHCCCCCCC
25.9624732914
731 (in isoform 5)Ubiquitination-39.5521906983
738UbiquitinationRNLQNVDMKIGV---
CCCCCCCCCCCC---
2.7221963094
7392-HydroxyisobutyrylationNLQNVDMKIGV----
CCCCCCCCCCC----
31.67-
739UbiquitinationNLQNVDMKIGV----
CCCCCCCCCCC----
31.6727667366
739 (in isoform 1)Ubiquitination-31.6721906983
740UbiquitinationLQNVDMKIGV-----
CCCCCCCCCC-----
5.5321963094

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
291SPhosphorylationKinasePKC-FAMILY-GPS
291SPhosphorylationKinasePKC_GROUP-PhosphoELM
672SPhosphorylationKinasePRKCAP17252
GPS
672SPhosphorylationKinasePKC-Uniprot
697SPhosphorylationKinasePRKACAP17612
GPS
706SPhosphorylationKinaseCAMK2AQ9UQM7
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
637TGlycosylation

22171320
638TGlycosylation

22171320
672SPhosphorylation

12032545
706SPhosphorylation

9580567

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CD44_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARHG1_HUMANARHGEF1physical
12748184
LCK_HUMANLCKphysical
8576267
ERBB4_HUMANERBB4physical
11825873
TIAM1_HUMANTIAM1physical
10636882
TGFR1_HUMANTGFBR1physical
12145287
VAV2_HUMANVAV2physical
11606575
FINC_HUMANFN1physical
1730778
EGFR_HUMANEGFRphysical
12093135
ERBB2_HUMANERBB2physical
12093135
HBEGF_HUMANHBEGFphysical
7532176
EZRI_HUMANEZRphysical
12032545
CSPG2_HUMANVCANphysical
10950950
SRC_HUMANSRCphysical
11084024
PTPRC_HUMANPTPRCphysical
9573028
LCK_HUMANLCKphysical
9573028
FYN_HUMANFYNphysical
9573028
MOES_HUMANMSNphysical
9472040
MERL_HUMANNF2physical
17891137
KPCZ_HUMANPRKCZphysical
22610405
ITB1_HUMANITGB1physical
21701559
SRC_HUMANSRCphysical
21701559
FLOT2_HUMANFLOT2physical
21701559
CAV1_HUMANCAV1physical
21701559
EP300_HUMANEP300physical
21701559
STAT3_HUMANSTAT3physical
21701559
SRC_HUMANSRCphysical
9519902
BAG1_HUMANBAG1physical
22863883
MERL_HUMANNF2physical
24912773
CRBG1_HUMANAIM1physical
26496610
SQSTM_HUMANSQSTM1physical
26496610
CHERP_HUMANCHERPphysical
26496610
PHRF1_HUMANPHRF1physical
26496610
CDC73_HUMANCDC73physical
26496610
TGFR1_HUMANTGFBR1physical
15597342
CD44_HUMANCD44physical
15597342
EGFR_HUMANEGFRphysical
15597342
FGFR1_HUMANFGFR1physical
15597342
EGFR_HUMANEGFRphysical
23265944
CSPG2_HUMANVCANphysical
28514442
GMEB2_HUMANGMEB2physical
28514442
FGF2_HUMANFGF2physical
28514442
GMEB1_HUMANGMEB1physical
28514442
DHRS2_HUMANDHRS2physical
28514442
TCAF2_HUMANFAM115Cphysical
28514442
AMPD2_HUMANAMPD2physical
28514442
SNX33_HUMANSNX33physical
28514442
CAMKV_HUMANCAMKVphysical
28514442
ATG9A_HUMANATG9Aphysical
28514442
PRD10_HUMANPRDM10physical
28514442
CQ080_HUMANC17orf80physical
28514442
SNX18_HUMANSNX18physical
28514442
FGFR2_HUMANFGFR2physical
28514442
FGRL1_HUMANFGFRL1physical
28514442
VANG1_HUMANVANGL1physical
28514442
PARP2_HUMANPARP2physical
28514442
TEFM_HUMANTEFMphysical
28514442
LAMA3_HUMANLAMA3physical
28514442
MTCH2_HUMANMTCH2physical
28514442
ECHB_HUMANHADHBphysical
28514442
CLCN7_HUMANCLCN7physical
28514442
SYF1_HUMANXAB2physical
28514442
TF3C2_HUMANGTF3C2physical
28514442
PRP17_HUMANCDC40physical
28514442
TF3C3_HUMANGTF3C3physical
28514442
AQR_HUMANAQRphysical
28514442
TF3C1_HUMANGTF3C1physical
28514442
TF3C6_HUMANGTF3C6physical
28514442
ECHA_HUMANHADHAphysical
28514442
TM160_HUMANTMEM160physical
28514442
OSBL8_HUMANOSBPL8physical
28514442
FGFR1_HUMANFGFR1physical
28514442
CDC5L_HUMANCDC5Lphysical
28514442
TNPO2_HUMANTNPO2physical
28514442
KPCI_HUMANPRKCIphysical
28514442
MAN1_HUMANLEMD3physical
28514442
LEG1_HUMANLGALS1physical
28514442
RBM22_HUMANRBM22physical
28514442
VANG2_HUMANVANGL2physical
28514442
SQSTM_HUMANSQSTM1physical
28514442
MBOA7_HUMANMBOAT7physical
28514442
ISY1_HUMANISY1physical
28514442
NIPS2_HUMANGBASphysical
28514442

Drug and Disease Associations
Kegg Disease
H00018 Gastric cancer
H00021 Renal cell carcinoma
H00043 Neuroblastoma
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD44_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-110, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57, AND MASS SPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-637 AND THR-638, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686; SER-697; SER-706AND THR-720, AND MASS SPECTROMETRY.
"A novel PKC-regulated mechanism controls CD44 ezrin association anddirectional cell motility.";
Legg J.W., Lewis C.A., Parsons M., Ng T., Isacke C.M.;
Nat. Cell Biol. 4:399-407(2002).
Cited for: PHOSPHORYLATION AT SER-672.
"Hyaluronan-dependent cell migration can be blocked by a CD44cytoplasmic domain peptide containing a phosphoserine at position325.";
Peck D., Isacke C.M.;
J. Cell Sci. 111:1595-1601(1998).
Cited for: PHOSPHORYLATION AT SER-706.

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