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P02808 (STAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Statherin
Gene names
Name:STATH
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length62 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface.

Subcellular location

Secreted.

Tissue specificity

Secreted by parotid and submandibular glands.

Post-translational modification

Substrate for transglutaminase-2. More than 95% of the cyclized peptide is cyclo-statherin Q-37, and less than 5% is cyclo-statherin Q-39. Cyclized forms account for about 1% of total statherin in saliva.

Sequence similarities

Belongs to the histatin/statherin family.

Mass spectrometry

Molecular mass is 5380.0±0.3 Da from positions 20 - 62. Determined by ESI. With phosphorylated Ser-21 and Ser-22. Ref.10

Molecular mass is 5363.0±0.3 Da from positions 20 - 62. Determined by ESI. With phosphorylated Ser-21 and Ser-22 and transglutamine cross-link. Ref.10

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MUC7Q8TAX72EBI-738687,EBI-738582

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7 Ref.8 Ref.9
Chain20 – 6243Statherin
PRO_0000022422

Regions

Region20 – 256Hydroxyapatite-binding; inhibits crystal growth
Region38 – 6225Hydrophobic; inhibits precipitation of calcium phosphate salts

Amino acid modifications

Modified residue211Phosphoserine Ref.7
Modified residue221Phosphoserine Ref.7
Cross-link25 ↔ 58Isoglutamyl lysine isopeptide (Lys-Gln); in form cyclo-statherin Q-39
Cross-link25 ↔ 56Isoglutamyl lysine isopeptide (Lys-Gln); in form cyclo-statherin Q-37

Natural variations

Natural variant25 – 3410Missing in statherin variants SV2 and SV3.
VAR_063167
Natural variant621Missing in statherin variants SV1 and SV3.
VAR_063168

Sequences

Sequence LengthMass (Da)Tools
P02808 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: CFE32EC235CA3A22

FASTA627,304
        10         20         30         40         50         60 
MKFLVFAFIL ALMVSMIGAD SSEEKFLRRI GRFGYGYGPY QPVPEQPLYP QPYQPQYQQY 


TF 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and chromosomal localization (4q11-13) of a gene for statherin, a regulator of calcium in saliva."
Sabatinai L., Carlock L., Johnson G., Azen E.
Am. J. Hum. Genet. 41:1048-1060(1987) [PubMed: 3502720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence."
Dickinson D.P., Ridall A.L., Levine M.J.
Biochem. Biophys. Res. Commun. 149:784-790(1987) [PubMed: 3426601] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure and sequence determination of the gene encoding human salivary statherin."
Sabatini L.M., He Y.-Z., Azen E.A.
Gene 89:245-251(1990) [PubMed: 2373369] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Trachea.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thyroid.
[7]"Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva."
Schlesinger D.H., Hay D.I.
J. Biol. Chem. 252:1689-1695(1977) [PubMed: 838735] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-62, PHOSPHORYLATION AT SER-21 AND SER-22.
[8]"Multiple forms of statherin in human salivary secretions."
Jensen J.L., Lamkin M.S., Troxler R.F., Oppenheim F.G.
Arch. Oral Biol. 36:529-534(1991) [PubMed: 1663737] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-62, VARIANTS 25-LYS--GLY-34 DEL AND PHE-62 DEL, MASS SPECTROMETRY.
[9]"Molecular basis of salivary proline-rich protein and peptide synthesis: cell-free translations and processing of human and macaque statherin mRNAs and partial amino acid sequence of their signal peptides."
Oppenheim F.G., Hay D.I., Smith D.J., Offner G.D., Troxler R.F.
J. Dent. Res. 66:462-466(1987) [PubMed: 3476566] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 1-16.
[10]"HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclization product of human salivary statherin generated by transglutaminase 2."
Cabras T., Inzitari R., Fanali C., Scarano E., Patamia M., Sanna M.T., Pisano E., Giardina B., Castagnola M., Messana I.
J. Sep. Sci. 29:2600-2608(2006) [PubMed: 17313100] [Abstract]
Cited for: TRANSGLUTAMINATION, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18078 mRNA. Translation: AAA60594.1.
M18371 mRNA. Translation: AAA60600.1.
M32639 Genomic DNA. Translation: AAA60593.1.
AK311812 mRNA. Translation: BAG34755.1.
CH471057 Genomic DNA. Translation: EAX05604.1.
BC067219 mRNA. Translation: AAH67219.1.
IPIIPI00022990.
PIRSBHUP. JH0153.
RefSeqNP_001009181.1. NM_001009181.1.
NP_003145.1. NM_003154.2.
UniGeneHs.654495.

3D structure databases

ProteinModelPortalP02808.
ModBaseSearch...

Protein-protein interaction databases

IntActP02808. 1 interaction.
STRINGP02808.

Protein family/group databases

TCDB1.C.79.1.2. channel-forming histatin antimicrobial peptide (Histatin) family.

PTM databases

PhosphoSiteP02808.

Polymorphism databases

DMDM134947.

Proteomic databases

PeptideAtlasP02808.
PRIDEP02808.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246895; ENSP00000246895; ENSG00000126549.
GeneID6779.
KEGGhsa:6779.
UCSCuc003heu.1. human.

Organism-specific databases

CTD6779.
GeneCardsGC04P070861.
H-InvDBHIX0024611.
HGNCHGNC:11369. STATH.
HPAHPA044569.
MIM184470. gene.
neXtProtNX_P02808.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00390000011757.
InParanoidP02808.
OMAGYGPYQP.
OrthoDBEOG4NKBXC.

Gene expression databases

ArrayExpressP02808.
BgeeP02808.
CleanExHS_STATH.
GenevestigatorP02808.
GermOnlineENSG00000126549. Homo sapiens.

Family and domain databases

InterProIPR005575. Statherin.
[Graphical view]
KOK13914.
PfamPF03875. Statherin. 1 hit.
[Graphical view]
PIRSFPIRSF002565. Statherin. 1 hit.
ProtoNetSearch...

Other

NextBio26462.
SOURCESearch...

Entry information

Entry nameSTAT_HUMAN
AccessionPrimary (citable) accession number: P02808
Secondary accession number(s): B2R4F8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families