HMMR_HUMAN - dbPTM
HMMR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMMR_HUMAN
UniProt AC O75330
Protein Name Hyaluronan mediated motility receptor
Gene Name HMMR
Organism Homo sapiens (Human).
Sequence Length 724
Subcellular Localization Cell surface . Cytoplasm .
Protein Description Receptor for hyaluronic acid (HA) (By similarity). Involved in cell motility (By similarity). When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenisis (By similarity)..
Protein Sequence MSFPKAPLKRFNDPSGCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQKESKQNLNVDKDTTLPASARKVKSSESKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLGIKHFDPSKAFHHESKENFALKTPLKEGNTNCYRAPMECQESWK
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
2Phosphorylation------MSFPKAPLK
------CCCCCCCCC
50.7024719451
15PhosphorylationLKRFNDPSGCAPSPG
CCCCCCCCCCCCCCC
49.7424732914
20PhosphorylationDPSGCAPSPGAYDVK
CCCCCCCCCCCCCCC
19.9023401153
24PhosphorylationCAPSPGAYDVKTLEV
CCCCCCCCCCCEEEH
27.4724732914
28UbiquitinationPGAYDVKTLEVLKGP
CCCCCCCEEEHHCCC
28.1829967540
37PhosphorylationEVLKGPVSFQKSQRF
EHHCCCCCHHHHHHH
25.7024719451
41PhosphorylationGPVSFQKSQRFKQQK
CCCCHHHHHHHHHHH
18.7927422710
52UbiquitinationKQQKESKQNLNVDKD
HHHHHHHHCCCCCCC
69.7629967540
60PhosphorylationNLNVDKDTTLPASAR
CCCCCCCCCCCHHHH
35.6529978859
61PhosphorylationLNVDKDTTLPASARK
CCCCCCCCCCHHHHH
40.6629978859
65PhosphorylationKDTTLPASARKVKSS
CCCCCCHHHHHCCCC
27.0225159151
65 (in isoform 2)Phosphorylation-27.0225849741
65 (in isoform 3)Phosphorylation-27.0225056879
72PhosphorylationSARKVKSSESKESQK
HHHHCCCCCCHHHHC
39.9226657352
99UbiquitinationRVLLQERGAQDRRIQ
HHHHHHCCCCHHHHH
27.1729967540
110PhosphorylationRRIQDLETELEKMEA
HHHHHHHHHHHHHHH
53.8418452278
114UbiquitinationDLETELEKMEARLNA
HHHHHHHHHHHHHHH
55.4529967540
115UbiquitinationLETELEKMEARLNAA
HHHHHHHHHHHHHHH
3.3929967540
123UbiquitinationEARLNAALREKTSLS
HHHHHHHHHHHHCCC
7.2629967540
127PhosphorylationNAALREKTSLSANNA
HHHHHHHHCCCCCCH
30.1022210691
128PhosphorylationAALREKTSLSANNAT
HHHHHHHCCCCCCHH
31.2522210691
129UbiquitinationALREKTSLSANNATL
HHHHHHCCCCCCHHH
7.3029967540
130PhosphorylationLREKTSLSANNATLE
HHHHHCCCCCCHHHH
28.8122210691
133N-linked_GlycosylationKTSLSANNATLEKQL
HHCCCCCCHHHHHHH
33.74UniProtKB CARBOHYD
135PhosphorylationSLSANNATLEKQLIE
CCCCCCHHHHHHHHH
37.2624719451
135UbiquitinationSLSANNATLEKQLIE
CCCCCCHHHHHHHHH
37.2629967540
138UbiquitinationANNATLEKQLIELTR
CCCHHHHHHHHHHHH
54.2229967540
139UbiquitinationNNATLEKQLIELTRT
CCHHHHHHHHHHHHH
37.9929967540
165UbiquitinationGNQKNLRILSLELMK
CCHHHHHHHHHHHHH
3.2729967540
198PhosphorylationMEMKLQVTQRSLEES
HHHHHHHHHHHHHHH
12.8030624053
200UbiquitinationMKLQVTQRSLEESQG
HHHHHHHHHHHHHHH
33.5729967540
201PhosphorylationKLQVTQRSLEESQGK
HHHHHHHHHHHHHHH
30.2530624053
205PhosphorylationTQRSLEESQGKIAQL
HHHHHHHHHHHHHHH
34.5529214152
206UbiquitinationQRSLEESQGKIAQLE
HHHHHHHHHHHHHHH
61.5529967540
215AcetylationKIAQLEGKLVSIEKE
HHHHHHCCEEEEEHH
36.0225953088
215UbiquitinationKIAQLEGKLVSIEKE
HHHHHHCCEEEEEHH
36.0229967540
216UbiquitinationIAQLEGKLVSIEKEK
HHHHHCCEEEEEHHH
5.5529967540
221UbiquitinationGKLVSIEKEKIDEKS
CCEEEEEHHHCCCHH
63.7429967540
222UbiquitinationKLVSIEKEKIDEKSE
CEEEEEHHHCCCHHH
42.3129967540
236PhosphorylationETEKLLEYIEEISCA
HHHHHHHHHHHHHCC
17.3829083192
236UbiquitinationETEKLLEYIEEISCA
HHHHHHHHHHHHHCC
17.3829967540
241PhosphorylationLEYIEEISCASDQVE
HHHHHHHHCCHHHHH
13.6029083192
244PhosphorylationIEEISCASDQVEKYK
HHHHHCCHHHHHHHC
32.6629083192
250PhosphorylationASDQVEKYKLDIAQL
CHHHHHHHCCCHHHH
11.8625884760
251UbiquitinationSDQVEKYKLDIAQLE
HHHHHHHCCCHHHHH
51.2329967540
252UbiquitinationDQVEKYKLDIAQLEE
HHHHHHCCCHHHHHH
5.3729967540
264UbiquitinationLEENLKEKNDEILSL
HHHHHHHCCHHHHHH
69.0229967540
270PhosphorylationEKNDEILSLKQSLEE
HCCHHHHHHHHHHHH
38.9024719451
321UbiquitinationLNAEMQNLKQKFILE
HHHHHHHHHHHHHHH
3.3224816145
323UbiquitinationAEMQNLKQKFILEQQ
HHHHHHHHHHHHHHH
49.4029967540
335UbiquitinationEQQEREKLQQKELQI
HHHHHHHHHHHHHHH
5.8229967540
338UbiquitinationEREKLQQKELQIDSL
HHHHHHHHHHHHHHH
47.6429967540
339UbiquitinationREKLQQKELQIDSLL
HHHHHHHHHHHHHHH
41.3829967540
350UbiquitinationDSLLQQEKELSSSLH
HHHHHHHHHHHHHHH
60.6729967540
351UbiquitinationSLLQQEKELSSSLHQ
HHHHHHHHHHHHHHH
53.8029967540
353PhosphorylationLQQEKELSSSLHQKL
HHHHHHHHHHHHHHH
20.9720068231
354PhosphorylationQQEKELSSSLHQKLC
HHHHHHHHHHHHHHH
49.9320068231
355PhosphorylationQEKELSSSLHQKLCS
HHHHHHHHHHHHHHH
26.8820068231
381PhosphorylationFEEELKQTLDELDKL
CHHHHHHHHHHHHHH
34.2930266825
392UbiquitinationLDKLQQKEEQAERLV
HHHHHHHHHHHHHHH
51.5124816145
403UbiquitinationERLVKQLEEEAKSRA
HHHHHHHHHHHHHHH
51.8329967540
407UbiquitinationKQLEEEAKSRAEELK
HHHHHHHHHHHHHHH
43.6924816145
408UbiquitinationQLEEEAKSRAEELKL
HHHHHHHHHHHHHHH
43.7124816145
419AcetylationELKLLEEKLKGKEAE
HHHHHHHHHCCCHHH
46.2327178108
419UbiquitinationELKLLEEKLKGKEAE
HHHHHHHHHCCCHHH
46.23-
445PhosphorylationTLLLQEKYDSMVQSL
HHHHHHHHHHHHHCH
16.7026074081
447PhosphorylationLLQEKYDSMVQSLED
HHHHHHHHHHHCHHH
20.1226074081
451PhosphorylationKYDSMVQSLEDVTAQ
HHHHHHHCHHHHHHH
23.4726074081
456PhosphorylationVQSLEDVTAQFESYK
HHCHHHHHHHHHHHH
27.3626074081
461PhosphorylationDVTAQFESYKALTAS
HHHHHHHHHHCCCHH
32.9726074081
462PhosphorylationVTAQFESYKALTASE
HHHHHHHHHCCCHHH
7.9626074081
466PhosphorylationFESYKALTASEIEDL
HHHHHCCCHHHHHHH
32.7526074081
468PhosphorylationSYKALTASEIEDLKL
HHHCCCHHHHHHHHC
33.5926074081
474UbiquitinationASEIEDLKLENSSLQ
HHHHHHHHCCCHHHH
67.1029967540
477N-linked_GlycosylationIEDLKLENSSLQEKA
HHHHHCCCHHHHHHH
47.54UniProtKB CARBOHYD
478PhosphorylationEDLKLENSSLQEKAA
HHHHCCCHHHHHHHH
24.0526657352
489UbiquitinationEKAAKAGKNAEDVQH
HHHHHCCCCHHHHHH
58.8229967540
490UbiquitinationKAAKAGKNAEDVQHQ
HHHHCCCCHHHHHHH
47.8729967540
518UbiquitinationMLLDLQTKSALKETE
HHHHHHHHHCCCHHH
22.2929967540
549UbiquitinationNQLKQQEEDFRKQLE
HHHHHCHHHHHHHHH
59.1029967540
567N-linked_GlycosylationGRKAEKENTTAELTE
HHHHHHHCCHHHHHH
54.52UniProtKB CARBOHYD
568PhosphorylationRKAEKENTTAELTEE
HHHHHHCCHHHHHHH
28.6020860994
583PhosphorylationINKWRLLYEELYNKT
HHHHHHHHHHHHCCC
16.3730576142
587PhosphorylationRLLYEELYNKTKPFQ
HHHHHHHHCCCCCEE
20.2130576142
588N-linked_GlycosylationLLYEELYNKTKPFQL
HHHHHHHCCCCCEEE
59.13UniProtKB CARBOHYD
589UbiquitinationLYEELYNKTKPFQLQ
HHHHHHCCCCCEEEE
44.3529967540
597UbiquitinationTKPFQLQLDAFEVEK
CCCEEEECHHHHHHH
7.5333845483
604UbiquitinationLDAFEVEKQALLNEH
CHHHHHHHHHHHHCC
46.1529967540
605UbiquitinationDAFEVEKQALLNEHG
HHHHHHHHHHHHCCC
24.6029967540
610UbiquitinationEKQALLNEHGAAQEQ
HHHHHHHCCCHHHHH
43.6029967540
620UbiquitinationAAQEQLNKIRDSYAK
HHHHHHHHHHHHHHH
47.9429967540
635UbiquitinationLLGHQNLKQKIKHVV
HHCCCCHHHHHHHHH
58.0329967540
636UbiquitinationLGHQNLKQKIKHVVK
HCCCCHHHHHHHHHH
56.7429967540
653PhosphorylationDENSQLKSEVSKLRC
CCCHHHHHHHHHHHH
52.3928555341
656PhosphorylationSQLKSEVSKLRCQLA
HHHHHHHHHHHHHHH
23.1727251275
657AcetylationQLKSEVSKLRCQLAK
HHHHHHHHHHHHHHH
45.1625953088
657PhosphorylationQLKSEVSKLRCQLAK
HHHHHHHHHHHHHHH
45.1627251275
668PhosphorylationQLAKKKQSETKLQEE
HHHHHHHCHHHHHHH
56.9929396449
668UbiquitinationQLAKKKQSETKLQEE
HHHHHHHCHHHHHHH
56.9933845483
670PhosphorylationAKKKQSETKLQEELN
HHHHHCHHHHHHHHH
42.1529396449
681UbiquitinationEELNKVLGIKHFDPS
HHHHHHHCCCCCCHH
29.8629967540
683UbiquitinationLNKVLGIKHFDPSKA
HHHHHCCCCCCHHHC
36.1033845483
684UbiquitinationNKVLGIKHFDPSKAF
HHHHCCCCCCHHHCC
30.3533845483
696UbiquitinationKAFHHESKENFALKT
HCCCCCCCCCCCCCC
54.4129967540
697UbiquitinationAFHHESKENFALKTP
CCCCCCCCCCCCCCC
67.8529967540
702AcetylationSKENFALKTPLKEGN
CCCCCCCCCCCCCCC
44.6725953088
703PhosphorylationKENFALKTPLKEGNT
CCCCCCCCCCCCCCC
34.4022617229
704PhosphorylationENFALKTPLKEGNTN
CCCCCCCCCCCCCCC
39.5924719451
713PhosphorylationKEGNTNCYRAPMECQ
CCCCCCCCCCCCCHH
16.33-

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

Oops, there are no upstream regulatory protein records of HMMR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMMR_HUMAN !!

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 HMMR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK01_HUMANMAPK1physical
11403955
EPHB2_HUMANEPHB2physical
22610405
TPX2_HUMANTPX2physical
22110403
AURKA_HUMANAURKAphysical
22110403
BRCA1_HUMANBRCA1physical
22110403
MORN4_HUMANMORN4physical
25416956
CAD13_HUMANCDH13physical
25640309
GREB1_HUMANGREB1physical
25640309
IL24_HUMANIL24physical
25640309
ITIH5_HUMANITIH5physical
25640309
ARY2_HUMANNAT2physical
25640309
THRSP_HUMANTHRSPphysical
25640309
FA83D_HUMANFAM83Dphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB08818Hyaluronan
Regulatory Network of HMMR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.
"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-20, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-65, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-703, AND MASSSPECTROMETRY.

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