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P21579

- SYT1_HUMAN

UniProt

P21579 - SYT1_HUMAN

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Protein

Synaptotagmin-1

Gene

SYT1

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

Functioni

May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca2+-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca2+-independent manner; these are neurexins, syntaxin and AP2.

Cofactori

Binds 3 calcium ions per subunit. The ions are bound to the C2 domains (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi173 – 1731Calcium 1By similarity
Metal bindingi173 – 1731Calcium 2By similarity
Metal bindingi179 – 1791Calcium 1By similarity
Metal bindingi231 – 2311Calcium 1By similarity
Metal bindingi231 – 2311Calcium 2By similarity
Metal bindingi232 – 2321Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi233 – 2331Calcium 1By similarity
Metal bindingi233 – 2331Calcium 2By similarity
Metal bindingi233 – 2331Calcium 3By similarity
Metal bindingi236 – 2361Calcium 3By similarity
Metal bindingi237 – 2371Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi239 – 2391Calcium 2By similarity
Metal bindingi239 – 2391Calcium 3By similarity

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: UniProtKB
  2. calcium-dependent phospholipid binding Source: ParkinsonsUK-UCL
  3. calcium ion binding Source: Ensembl
  4. low-density lipoprotein particle receptor binding Source: MGI
  5. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl
  6. phosphatidylserine binding Source: Ensembl
  7. SNARE binding Source: ParkinsonsUK-UCL
  8. syntaxin-1 binding Source: UniProtKB
  9. transporter activity Source: InterPro

GO - Biological processi

  1. calcium ion-dependent exocytosis of neurotransmitter Source: ParkinsonsUK-UCL
  2. detection of calcium ion Source: UniProtKB
  3. glutamate secretion Source: Reactome
  4. neurotransmitter secretion Source: UniProtKB
  5. positive regulation of calcium ion-dependent exocytosis Source: Ensembl
  6. positive regulation of synaptic transmission Source: ParkinsonsUK-UCL
  7. positive regulation of vesicle fusion Source: Ensembl
  8. protein homooligomerization Source: UniProtKB
  9. regulation of exocytosis Source: UniProtKB
  10. regulation of regulated secretory pathway Source: ParkinsonsUK-UCL
  11. regulation of synaptic transmission, glutamatergic Source: ParkinsonsUK-UCL
  12. synaptic transmission Source: Reactome
  13. synaptic vesicle exocytosis Source: Ensembl
  14. vesicle docking Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_200743. Toxicity of botulinum toxin type G (BoNT/G).
REACT_200782. Toxicity of botulinum toxin type B (BoNT/B).
REACT_23947. GABA synthesis, release, reuptake and degradation.

Protein family/group databases

TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-1
Alternative name(s):
Synaptotagmin I
Short name:
SytI
p65
Gene namesi
Name:SYT1
Synonyms:SVP65, SYT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11509. SYT1.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. clathrin-sculpted acetylcholine transport vesicle membrane Source: Reactome
  3. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
  4. clathrin-sculpted glutamate transport vesicle membrane Source: Reactome
  5. clathrin-sculpted monoamine transport vesicle membrane Source: Reactome
  6. dense core granule Source: Ensembl
  7. endocytic vesicle membrane Source: Reactome
  8. excitatory synapse Source: Ensembl
  9. integral component of membrane Source: UniProtKB-KW
  10. neuron projection Source: ParkinsonsUK-UCL
  11. plasma membrane Source: Reactome
  12. presynaptic membrane Source: Ensembl
  13. synaptic vesicle Source: UniProtKB
  14. synaptic vesicle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36290.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Synaptotagmin-1PRO_0000183936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
Lipidationi75 – 751S-palmitoyl cysteineBy similarity
Lipidationi76 – 761S-palmitoyl cysteineBy similarity
Lipidationi78 – 781S-palmitoyl cysteineBy similarity
Lipidationi80 – 801S-palmitoyl cysteineBy similarity
Lipidationi83 – 831S-palmitoyl cysteineBy similarity
Modified residuei129 – 1291Phosphothreonine1 Publication
Modified residuei230 – 2301PhosphotyrosineBy similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP21579.
PRIDEiP21579.

PTM databases

PhosphoSiteiP21579.

Miscellaneous databases

PMAP-CutDBP21579.

Expressioni

Gene expression databases

BgeeiP21579.
CleanExiHS_SYT1.
ExpressionAtlasiP21579. baseline and differential.
GenevestigatoriP21579.

Organism-specific databases

HPAiHPA008394.
HPA064788.

Interactioni

Subunit structurei

Homotetramer (Probable). Interacts with SCAMP5, STON2, SV2A, SV2B, SV2C and RIMS1. Forms a complex with SV2B, syntaxin 1 and SNAP25 (By similarity).By similarityCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
CACNB4O00305-22EBI-524909,EBI-714855
IKBKGQ9Y6K93EBI-524909,EBI-81279

Protein-protein interaction databases

BioGridi112723. 29 interactions.
DIPiDIP-34042N.
IntActiP21579. 16 interactions.
MINTiMINT-1400342.
STRINGi9606.ENSP00000261205.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 4711
Beta strandi145 – 1539
Turni154 – 1574
Beta strandi158 – 16710
Helixi173 – 1753
Beta strandi180 – 1889
Beta strandi206 – 2138
Helixi217 – 2204
Beta strandi224 – 2318
Beta strandi234 – 2363
Beta strandi239 – 2479
Helixi248 – 2503
Beta strandi257 – 2626
Beta strandi276 – 2849
Turni285 – 2884
Beta strandi289 – 29911
Beta strandi311 – 3199
Beta strandi322 – 3287
Beta strandi333 – 3375
Beta strandi339 – 3479
Turni350 – 3523
Helixi353 – 3553
Beta strandi356 – 3649
Beta strandi367 – 3693
Beta strandi373 – 3808
Helixi385 – 39612
Beta strandi402 – 4076
Helixi411 – 4188

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K45NMR-A141-268[»]
2K4ANMR-A141-268[»]
2K8MNMR-A/D141-268[»]
2KI6NMR-A/F141-268[»]
2LHANMR-A272-422[»]
2R83X-ray2.70A/B141-422[»]
3F00X-ray1.36A141-266[»]
3F01X-ray1.70A141-266[»]
3F04X-ray1.35A141-266[»]
3F05X-ray1.40A141-266[»]
4ISQX-ray2.65D/E/F33-53[»]
ProteinModelPortaliP21579.
SMRiP21579. Positions 141-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21579.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757VesicularSequence AnalysisAdd
BLAST
Topological domaini81 – 422342CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei58 – 8023HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini157 – 24589C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini287 – 37892C2 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 382247Phospholipid bindingCuratedAdd
BLAST

Domaini

The first C2 domain mediates Ca2+-dependent phospholipid binding.
The second C2 domain mediates interaction with SV2A and STN2.By similarity

Sequence similaritiesi

Belongs to the synaptotagmin family.Curated
Contains 2 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292488.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP21579.
KOiK15290.
OMAiHDIIGEY.
PhylomeDBiP21579.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
PANTHERiPTHR10024:SF183. PTHR10024:SF183. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21579-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVSESHHEAL AAPPVTTVAT VLPSNATEPA SPGEGKEDAF SKLKEKFMNE
60 70 80 90 100
LHKIPLPPWA LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN
110 120 130 140 150
AINMKDVKDL GKTMKDQALK DDDAETGLTD GEEKEEPKEE EKLGKLQYSL
160 170 180 190 200
DYDFQNNQLL VGIIQAAELP ALDMGGTSDP YVKVFLLPDK KKKFETKVHR
210 220 230 240 250
KTLNPVFNEQ FTFKVPYSEL GGKTLVMAVY DFDRFSKHDI IGEFKVPMNT
260 270 280 290 300
VDFGHVTEEW RDLQSAEKEE QEKLGDICFS LRYVPTAGKL TVVILEAKNL
310 320 330 340 350
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT IKKNTLNPYY NESFSFEVPF
360 370 380 390 400
EQIQKVQVVV TVLDYDKIGK NDAIGKVFVG YNSTGAELRH WSDMLANPRR
410 420
PIAQWHTLQV EEEVDAMLAV KK
Length:422
Mass (Da):47,573
Last modified:May 1, 1991 - v1
Checksum:i467F7C58E411AFA9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55047 mRNA. Translation: AAA60609.1.
AK094616 mRNA. Translation: BAG52897.1.
AK126908 mRNA. Translation: BAG54392.1.
CR627387 mRNA. Translation: CAH10483.1.
CH471054 Genomic DNA. Translation: EAW97343.1.
BC058917 mRNA. Translation: AAH58917.1.
CCDSiCCDS9017.1.
PIRiA39052. BMHU1Y.
RefSeqiNP_001129277.1. NM_001135805.1.
NP_001129278.1. NM_001135806.1.
NP_005630.1. NM_005639.2.
UniGeneiHs.310545.

Genome annotation databases

EnsembliENST00000261205; ENSP00000261205; ENSG00000067715.
ENST00000393240; ENSP00000376932; ENSG00000067715.
ENST00000552744; ENSP00000447575; ENSG00000067715.
GeneIDi6857.
KEGGihsa:6857.
UCSCiuc001sys.3. human.

Polymorphism databases

DMDMi135086.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55047 mRNA. Translation: AAA60609.1 .
AK094616 mRNA. Translation: BAG52897.1 .
AK126908 mRNA. Translation: BAG54392.1 .
CR627387 mRNA. Translation: CAH10483.1 .
CH471054 Genomic DNA. Translation: EAW97343.1 .
BC058917 mRNA. Translation: AAH58917.1 .
CCDSi CCDS9017.1.
PIRi A39052. BMHU1Y.
RefSeqi NP_001129277.1. NM_001135805.1.
NP_001129278.1. NM_001135806.1.
NP_005630.1. NM_005639.2.
UniGenei Hs.310545.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K45 NMR - A 141-268 [» ]
2K4A NMR - A 141-268 [» ]
2K8M NMR - A/D 141-268 [» ]
2KI6 NMR - A/F 141-268 [» ]
2LHA NMR - A 272-422 [» ]
2R83 X-ray 2.70 A/B 141-422 [» ]
3F00 X-ray 1.36 A 141-266 [» ]
3F01 X-ray 1.70 A 141-266 [» ]
3F04 X-ray 1.35 A 141-266 [» ]
3F05 X-ray 1.40 A 141-266 [» ]
4ISQ X-ray 2.65 D/E/F 33-53 [» ]
ProteinModelPortali P21579.
SMRi P21579. Positions 141-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112723. 29 interactions.
DIPi DIP-34042N.
IntActi P21579. 16 interactions.
MINTi MINT-1400342.
STRINGi 9606.ENSP00000261205.

Protein family/group databases

TCDBi 1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSitei P21579.

Polymorphism databases

DMDMi 135086.

Proteomic databases

PaxDbi P21579.
PRIDEi P21579.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261205 ; ENSP00000261205 ; ENSG00000067715 .
ENST00000393240 ; ENSP00000376932 ; ENSG00000067715 .
ENST00000552744 ; ENSP00000447575 ; ENSG00000067715 .
GeneIDi 6857.
KEGGi hsa:6857.
UCSCi uc001sys.3. human.

Organism-specific databases

CTDi 6857.
GeneCardsi GC12P079232.
HGNCi HGNC:11509. SYT1.
HPAi HPA008394.
HPA064788.
MIMi 185605. gene.
neXtProti NX_P21579.
PharmGKBi PA36290.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292488.
GeneTreei ENSGT00760000118973.
HOGENOMi HOG000232127.
HOVERGENi HBG005010.
InParanoidi P21579.
KOi K15290.
OMAi HDIIGEY.
PhylomeDBi P21579.
TreeFami TF315600.

Enzyme and pathway databases

Reactomei REACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_200743. Toxicity of botulinum toxin type G (BoNT/G).
REACT_200782. Toxicity of botulinum toxin type B (BoNT/B).
REACT_23947. GABA synthesis, release, reuptake and degradation.

Miscellaneous databases

ChiTaRSi SYT1. human.
EvolutionaryTracei P21579.
GeneWikii SYT1.
GenomeRNAii 6857.
NextBioi 26767.
PMAP-CutDB P21579.
PROi P21579.
SOURCEi Search...

Gene expression databases

Bgeei P21579.
CleanExi HS_SYT1.
ExpressionAtlasi P21579. baseline and differential.
Genevestigatori P21579.

Family and domain databases

Gene3Di 2.60.40.150. 2 hits.
InterProi IPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view ]
PANTHERi PTHR10024:SF183. PTHR10024:SF183. 1 hit.
Pfami PF00168. C2. 2 hits.
[Graphical view ]
PRINTSi PR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTi SM00239. C2. 2 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 2 hits.
PROSITEi PS50004. C2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans."
    Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U., Suedhof T.C.
    J. Biol. Chem. 266:615-622(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Amygdala and Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: PNS.
  6. "Human SCAMP5, a novel secretory carrier membrane protein, facilitates calcium-triggered cytokine secretion by interaction with SNARE machinery."
    Han C., Chen T., Yang M., Li N., Liu H., Cao X.
    J. Immunol. 182:2986-2996(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAMP5.
  7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYT1_HUMAN
AccessioniPrimary (citable) accession number: P21579
Secondary accession number(s): Q6AI31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 29, 2014
This is version 158 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3