Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02808

- STAT_HUMAN

UniProt

P02808 - STAT_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Statherin

Gene

STATH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. extracellular matrix constituent, lubricant activity Source: UniProtKB
  2. hydroxyapatite binding Source: UniProtKB
  3. structural constituent of tooth enamel Source: UniProtKB

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. negative regulation of bone mineralization Source: UniProtKB
  3. ossification Source: ProtInc
  4. saliva secretion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Biomineralization

Protein family/group databases

TCDBi1.C.79.1.2. the channel-forming histatin antimicrobial peptide (histatin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Statherin
Gene namesi
Name:STATH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11369. STATH.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36187.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 6243StatherinPRO_0000022422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei22 – 221Phosphoserine1 Publication
Cross-linki25 ↔ 58Isoglutamyl lysine isopeptide (Lys-Gln); in form cyclo-statherin Q-39
Cross-linki25 ↔ 56Isoglutamyl lysine isopeptide (Lys-Gln); in form cyclo-statherin Q-37

Post-translational modificationi

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.
Sulfated on tyrosine residues.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP02808.
PaxDbiP02808.
PeptideAtlasiP02808.
PRIDEiP02808.

PTM databases

PhosphoSiteiP02808.

Expressioni

Tissue specificityi

Secreted by parotid and submandibular glands.

Gene expression databases

BgeeiP02808.
CleanExiHS_STATH.
GenevestigatoriP02808.

Organism-specific databases

HPAiHPA044569.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MUC7Q8TAX72EBI-738687,EBI-738582

Protein-protein interaction databases

BioGridi112656. 2 interactions.
IntActiP02808. 1 interaction.
STRINGi9606.ENSP00000246895.

Structurei

3D structure databases

ProteinModelPortaliP02808.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 256Hydroxyapatite-binding; inhibits crystal growth
Regioni38 – 6225Hydrophobic; inhibits precipitation of calcium phosphate saltsAdd
BLAST

Sequence similaritiesi

Belongs to the histatin/statherin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG255838.
GeneTreeiENSGT00390000011757.
HOGENOMiHOG000293326.
InParanoidiP02808.
KOiK13914.
OMAiEIATERW.
OrthoDBiEOG7J183D.
PhylomeDBiP02808.
TreeFamiTF341588.

Family and domain databases

InterProiIPR005575. Statherin.
[Graphical view]
PfamiPF03875. Statherin. 1 hit.
[Graphical view]
PIRSFiPIRSF002565. Statherin. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Both isoforms can occur with the Phe-62 deletion.

Isoform 1 (identifier: P02808-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKFLVFAFIL ALMVSMIGAD SSEEKFLRRI GRFGYGYGPY QPVPEQPLYP
60
QPYQPQYQQY TF
Length:62
Mass (Da):7,304
Last modified:July 1, 1989 - v2
Checksum:iCFE32EC235CA3A22
GO
Isoform 2 (identifier: P02808-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     25-34: Missing.

Show »
Length:52
Mass (Da):6,073
Checksum:iC94F2FE112DAA733
GO

Mass spectrometryi

Molecular mass is 5380.0±0.3 Da from positions 20 - 62. Determined by ESI. With phosphorylated Ser-21 and Ser-22.1 Publication
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.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621Missing.1 Publication
VAR_069065

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 3410Missing in isoform 2. CuratedVSP_045744

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18078 mRNA. Translation: AAA60594.1.
M18371 mRNA. Translation: AAA60600.1.
M32639 Genomic DNA. Translation: AAA60593.1.
AK311812 mRNA. Translation: BAG34755.1.
AC063956 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05604.1.
CH471057 Genomic DNA. Translation: EAX05605.1.
BC067219 mRNA. Translation: AAH67219.1.
CCDSiCCDS33998.1. [P02808-2]
CCDS3533.1. [P02808-1]
PIRiJH0153. SBHUP.
RefSeqiNP_001009181.1. NM_001009181.1. [P02808-2]
NP_003145.1. NM_003154.2. [P02808-1]
UniGeneiHs.654495.

Genome annotation databases

EnsembliENST00000246895; ENSP00000246895; ENSG00000126549. [P02808-1]
ENST00000381060; ENSP00000370448; ENSG00000126549. [P02808-2]
ENST00000615994; ENSP00000484341; ENSG00000126549. [P02808-1]
GeneIDi6779.
KEGGihsa:6779.
UCSCiuc003heu.1. human. [P02808-1]
uc003hev.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18078 mRNA. Translation: AAA60594.1 .
M18371 mRNA. Translation: AAA60600.1 .
M32639 Genomic DNA. Translation: AAA60593.1 .
AK311812 mRNA. Translation: BAG34755.1 .
AC063956 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05604.1 .
CH471057 Genomic DNA. Translation: EAX05605.1 .
BC067219 mRNA. Translation: AAH67219.1 .
CCDSi CCDS33998.1. [P02808-2 ]
CCDS3533.1. [P02808-1 ]
PIRi JH0153. SBHUP.
RefSeqi NP_001009181.1. NM_001009181.1. [P02808-2 ]
NP_003145.1. NM_003154.2. [P02808-1 ]
UniGenei Hs.654495.

3D structure databases

ProteinModelPortali P02808.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112656. 2 interactions.
IntActi P02808. 1 interaction.
STRINGi 9606.ENSP00000246895.

Protein family/group databases

TCDBi 1.C.79.1.2. the channel-forming histatin antimicrobial peptide (histatin) family.

PTM databases

PhosphoSitei P02808.

Proteomic databases

MaxQBi P02808.
PaxDbi P02808.
PeptideAtlasi P02808.
PRIDEi P02808.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000246895 ; ENSP00000246895 ; ENSG00000126549 . [P02808-1 ]
ENST00000381060 ; ENSP00000370448 ; ENSG00000126549 . [P02808-2 ]
ENST00000615994 ; ENSP00000484341 ; ENSG00000126549 . [P02808-1 ]
GeneIDi 6779.
KEGGi hsa:6779.
UCSCi uc003heu.1. human. [P02808-1 ]
uc003hev.1. human.

Organism-specific databases

CTDi 6779.
GeneCardsi GC04P070861.
HGNCi HGNC:11369. STATH.
HPAi HPA044569.
MIMi 184470. gene.
neXtProti NX_P02808.
PharmGKBi PA36187.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255838.
GeneTreei ENSGT00390000011757.
HOGENOMi HOG000293326.
InParanoidi P02808.
KOi K13914.
OMAi EIATERW.
OrthoDBi EOG7J183D.
PhylomeDBi P02808.
TreeFami TF341588.

Miscellaneous databases

ChiTaRSi STATH. human.
GeneWikii STATH.
GenomeRNAii 6779.
NextBioi 26462.
PROi P02808.
SOURCEi Search...

Gene expression databases

Bgeei P02808.
CleanExi HS_STATH.
Genevestigatori P02808.

Family and domain databases

InterProi IPR005575. Statherin.
[Graphical view ]
Pfami PF03875. Statherin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002565. Statherin. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Trachea.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Thyroid.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-62 (ISOFORM 1), PHOSPHORYLATION AT SER-21 AND SER-22.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-62 (ISOFORMS 1 AND 2), VARIANT PHE-62 DEL, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE OF 1-16.
  11. Cited for: PROTEIN SEQUENCE OF 20-62 (ISOFORM 1), SULFATION.
  12. "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] [Europe PMC] [Abstract]
    Cited for: TRANSGLUTAMINATION, MASS SPECTROMETRY.

Entry informationi

Entry nameiSTAT_HUMAN
AccessioniPrimary (citable) accession number: P02808
Secondary accession number(s): A6NKE9, B2R4F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3