ADAM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ADAM2_HUMAN
• UniProt AC: Q99965
• Protein Name: Disintegrin and metalloproteinase domain-containing protein 2
• Gene Name: ADAM2
• Organism: Homo sapiens (Human).
• Sequence Length: 735
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein..
• Protein Sequence: MWRVLFLLSGLGGLRMDSNFDSLPVQITVPEKIRSIIKEGIESQASYKIVIEGKPYTVNLMQKNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGYIEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLESSVGFEHVIYQVKHKKADVSLYNEKDIESRDLSFKLQSVEPQQDFAKYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSYLVLRPHDVAFLLVYREKSNYVGATFQGKMCDANYAGGVVLHPRTISLESLAVILAQLLSLSMGITYDDINKCQCSGAVCIMNPEAIHFSGVKIFSNCSFEDFAHFISKQKSQCLHNQPRLDPFFKQQAVCGNAKLEAGEECDCGTEQDCALIGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHYVQTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVGKFLLQIPRATIIYANISGHLCIAVEFASDHADSQKMWIKDGTSCGSNKVCRNQRCVSSSYLGYDCTTDKCNDRGVCNNKKHCHCSASYLPPDCSVQSDLWPGGSIDSGNFPPVAIPARLPERRYIENIYHSKPMRWPFFLFIPFFIIFCVLIAIMVKVNFQRKKWRTEDYSSDEQPESESEPKG

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
35	Phosphorylation	TVPEKIRSIIKEGIE ECCHHHHHHHHHCHH	31.94	24719451
122	N-linked_Glycosylation	RGVLQFENVSYGIEP CCEEEEECEEEECEE	29.35	UniProtKB CARBOHYD
151	Phosphorylation	KHKKADVSLYNEKDI ECCCCCEECCCHHHC	26.19	46159047
153	Phosphorylation	KKADVSLYNEKDIES CCCCEECCCHHHCCC	17.48	6872551
164	Phosphorylation	DIESRDLSFKLQSVE HCCCCCCEEEEECCC	25.32	24719451
220	N-linked_Glycosylation	NAIFVSFNITIILSS CEEEEECCEEEEHHH	24.00	UniProtKB CARBOHYD
301	Phosphorylation	GVVLHPRTISLESLA CEEECCCCCCHHHHH	21.26	24043423
303	Phosphorylation	VLHPRTISLESLAVI EECCCCCCHHHHHHH	26.02	24043423
306	Phosphorylation	PRTISLESLAVILAQ CCCCCHHHHHHHHHH	27.24	24043423
316	Phosphorylation	VILAQLLSLSMGITY HHHHHHHHHHCCCCH	27.30	24043423
318	Phosphorylation	LAQLLSLSMGITYDD HHHHHHHHCCCCHHH	16.16	24043423
322	Phosphorylation	LSLSMGITYDDINKC HHHHCCCCHHHHHCC	18.37	24043423
323	Phosphorylation	SLSMGITYDDINKCQ HHHCCCCHHHHHCCC	15.08	24043423
332	Phosphorylation	DINKCQCSGAVCIMN HHHCCCCCCEEEECC	12.15	30631047
353	N-linked_Glycosylation	SGVKIFSNCSFEDFA CCCEEECCCCHHHHH	18.07	UniProtKB CARBOHYD
459	N-linked_Glycosylation	CDLPEYCNGSSASCP CCCCHHCCCCCCCCC	53.10	UniProtKB CARBOHYD
566	N-linked_Glycosylation	RATIIYANISGHLCI CCEEEEEECCCCEEE	16.40	UniProtKB CARBOHYD
568	Phosphorylation	TIIYANISGHLCIAV EEEEEECCCCEEEEE	21.70	46159051
721	Phosphorylation	KKWRTEDYSSDEQPE CCCCCCCCCCCCCCC	12.11	46159057
729	Phosphorylation	SSDEQPESESEPKG- CCCCCCCCCCCCCC-	53.78	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ADAM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ADAM2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ADAM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CRYAB_HUMAN	CRYAB	physical	16049941
DYN1_HUMAN	DNM1	physical	16049941
ASPH2_HUMAN	ASPHD2	physical	28514442
CF120_HUMAN	C6orf120	physical	28514442
ATS2_HUMAN	ADAMTS2	physical	28514442
LRRC3_HUMAN	LRRC3	physical	28514442
TITIN_HUMAN	TTN	physical	28514442
LCLT1_HUMAN	LCLAT1	physical	28514442

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.