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Protein

Syntaxin-binding protein 2

Gene

STXBP2

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

Functioni

Involved in intracellular vesicle trafficking and vesicle fusion with membranes. Contributes to the granule exocytosis machinery through interaction with soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins that regulate membrane fusion. Regulates cytotoxic granule exocytosis in natural killer (NK) cells.2 Publications

GO - Molecular functioni

  • syntaxin-3 binding Source: UniProtKB

GO - Biological processi

  • leukocyte mediated cytotoxicity Source: UniProtKB
  • neutrophil degranulation Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of mast cell degranulation Source: UniProtKB
  • vesicle docking involved in exocytosis Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-binding protein 2
Alternative name(s):
Protein unc-18 homolog 2
Short name:
Unc18-2
Protein unc-18 homolog B
Short name:
Unc-18B
Gene namesi
Name:STXBP2
Synonyms:UNC18B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11445. STXBP2.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • azurophil granule Source: UniProtKB
  • cytolytic granule Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • specific granule Source: UniProtKB
  • tertiary granule Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Familial hemophagocytic lymphohistiocytosis 5 (FHL5)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare disorder characterized by immune dysregulation with hypercytokinemia, defective function of natural killer cell, and massive infiltration of several organs by activated lymphocytes and macrophages. The clinical features of the disease include fever, hepatosplenomegaly, cytopenia, and less frequently neurological abnormalities ranging from irritability and hypotonia to seizures, cranial nerve deficits and ataxia.

See also OMIM:613101
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091L → P in FHL5. 1 Publication
VAR_063814
Natural varianti232 – 2321Missing in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063815
Natural varianti292 – 2921R → H in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063816
Natural varianti405 – 4051R → Q in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063817
Natural varianti405 – 4051R → W in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063818
Natural varianti477 – 4771P → L in FHL5; leads to a complete loss of the ability to interact with STX11. 2 Publications
VAR_063819

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613101. phenotype.
Orphaneti540. Familial hemophagocytic lymphohistiocytosis.
PharmGKBiPA36242.

Polymorphism and mutation databases

DMDMi313104015.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Syntaxin-binding protein 2PRO_0000206281Add
BLAST

Proteomic databases

MaxQBiQ15833.
PaxDbiQ15833.
PRIDEiQ15833.

2D gel databases

OGPiQ15833.

PTM databases

PhosphoSiteiQ15833.

Expressioni

Tissue specificityi

Placenta, lung, liver, kidney and pancreas, as well as in peripheral blood lymphocytes.

Gene expression databases

BgeeiQ15833.
CleanExiHS_STXBP2.
ExpressionAtlasiQ15833. baseline and differential.
GenevisibleiQ15833. HS.

Organism-specific databases

HPAiHPA015564.

Interactioni

Subunit structurei

Interacts with STX1A, STX2 and STX3 (By similarity). Interacts with STX11.By similarity2 Publications

Protein-protein interaction databases

BioGridi112682. 13 interactions.
IntActiQ15833. 1 interaction.
MINTiMINT-4718353.
STRINGi9606.ENSP00000221283.

Structurei

Secondary structure

1
593
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510Combined sources
Turni16 – 227Combined sources
Beta strandi29 – 335Combined sources
Helixi35 – 428Combined sources
Helixi47 – 515Combined sources
Turni52 – 543Combined sources
Beta strandi55 – 584Combined sources
Beta strandi71 – 777Combined sources
Helixi81 – 899Combined sources
Beta strandi102 – 1087Combined sources
Helixi112 – 1198Combined sources
Helixi123 – 1264Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi141 – 1466Combined sources
Helixi152 – 1576Combined sources
Helixi159 – 1646Combined sources
Helixi165 – 18218Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi193 – 1953Combined sources
Helixi196 – 21520Combined sources
Turni217 – 2204Combined sources
Helixi225 – 2273Combined sources
Beta strandi229 – 2335Combined sources
Helixi235 – 2373Combined sources
Helixi241 – 2433Combined sources
Helixi249 – 2568Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi276 – 2805Combined sources
Beta strandi282 – 2843Combined sources
Helixi286 – 2916Combined sources
Turni296 – 2983Combined sources
Helixi299 – 31416Combined sources
Helixi327 – 3315Combined sources
Helixi333 – 35725Combined sources
Helixi360 – 37314Combined sources
Helixi385 – 3939Combined sources
Helixi400 – 41415Combined sources
Helixi419 – 42810Combined sources
Helixi432 – 4343Combined sources
Helixi435 – 4395Combined sources
Helixi440 – 4434Combined sources
Helixi478 – 48710Combined sources
Turni493 – 4953Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi533 – 5386Combined sources
Helixi544 – 55613Combined sources
Turni557 – 5593Combined sources
Beta strandi562 – 5709Combined sources
Helixi573 – 58210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CCAX-ray2.60A1-593[»]
ProteinModelPortaliQ15833.
SMRiQ15833. Positions 5-593.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the STXBP/unc-18/SEC1 family.Curated

Phylogenomic databases

eggNOGiCOG5158.
GeneTreeiENSGT00390000005206.
HOGENOMiHOG000232146.
HOVERGENiHBG052710.
InParanoidiQ15833.
KOiK15300.
OMAiPRERMEP.
OrthoDBiEOG78PV8M.
PhylomeDBiQ15833.
TreeFamiTF313242.

Family and domain databases

Gene3Di3.40.50.1910. 2 hits.
InterProiIPR027482. Sec-1-like_dom2.
IPR001619. Sec1-like.
[Graphical view]
PANTHERiPTHR11679. PTHR11679. 1 hit.
PfamiPF00995. Sec1. 1 hit.
[Graphical view]
PIRSFiPIRSF005715. VPS45_Sec1. 1 hit.
SUPFAMiSSF56815. SSF56815. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15833-1) [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
MAPSGLKAVV GEKILSGVIR SVKKDGEWKV LIMDHPSMRI LSSCCKMSDI
60 70 80 90 100
LAEGITIVED INKRREPIPS LEAIYLLSPT EKSVQALIKD FQGTPTFTYK
110 120 130 140 150
AAHIFFTDTC PEPLFSELGR SRLAKVVKTL KEIHLAFLPY EAQVFSLDAP
160 170 180 190 200
HSTYNLYCPF RAEERTRQLE VLAQQIATLC ATLQEYPAIR YRKGPEDTAQ
210 220 230 240 250
LAHAVLAKLN AFKADTPSLG EGPEKTRSQL LIMDRAADPV SPLLHELTFQ
260 270 280 290 300
AMAYDLLDIE QDTYRYETTG LSEAREKAVL LDEDDDLWVE LRHMHIADVS
310 320 330 340 350
KKVTELLRTF CESKRLTTDK ANIKDLSQIL KKMPQYQKEL NKYSTHLHLA
360 370 380 390 400
DDCMKHFKGS VEKLCSVEQD LAMGSDAEGE KIKDSMKLIV PVLLDAAVPA
410 420 430 440 450
YDKIRVLLLY ILLRNGVSEE NLAKLIQHAN VQAHSSLIRN LEQLGGTVTN
460 470 480 490 500
PGGSGTSSRL EPRERMEPTY QLSRWTPVIK DVMEDAVEDR LDRNLWPFVS
510 520 530 540 550
DPAPTASSQA AVSARFGHWH KNKAGIEARA GPRLIVYVMG GVAMSEMRAA
560 570 580 590
YEVTRATEGK WEVLIGSSHI LTPTRFLDDL KALDKKLEDI ALP
Length:593
Mass (Da):66,453
Last modified:November 30, 2010 - v2
Checksum:i98E27B55309168A9
GO
Isoform 2 (identifier: Q15833-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-85: Missing.

Show »
Length:590
Mass (Da):66,138
Checksum:iC9A58E0240FCF3B2
GO
Isoform 3 (identifier: Q15833-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-82: K → KAQAQRVIHLPQ

Note: No experimental confirmation available.
Show »
Length:604
Mass (Da):67,695
Checksum:i66F535E773C359DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481H → R in BAG64687 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091L → P in FHL5. 1 Publication
VAR_063814
Natural varianti232 – 2321Missing in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063815
Natural varianti292 – 2921R → H in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063816
Natural varianti405 – 4051R → Q in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063817
Natural varianti405 – 4051R → W in FHL5; leads to a complete loss of the ability to interact with STX11. 1 Publication
VAR_063818
Natural varianti477 – 4771P → L in FHL5; leads to a complete loss of the ability to interact with STX11. 2 Publications
VAR_063819
Natural varianti526 – 5261I → V.2 Publications
Corresponds to variant rs6791 [ dbSNP | Ensembl ].
VAR_014934

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei82 – 821K → KAQAQRVIHLPQ in isoform 3. 1 PublicationVSP_055157
Alternative sequencei83 – 853Missing in isoform 2. 2 PublicationsVSP_040121

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63533 mRNA. Translation: AAC50762.1.
BT006915 mRNA. Translation: AAP35561.1.
AK303701 mRNA. Translation: BAG64687.1.
AC008763 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69018.1.
BC002869 mRNA. Translation: AAH02869.1.
CCDSiCCDS12181.1. [Q15833-1]
CCDS45948.1. [Q15833-2]
CCDS62522.1. [Q15833-3]
RefSeqiNP_001120868.1. NM_001127396.2. [Q15833-2]
NP_001258963.1. NM_001272034.1. [Q15833-3]
NP_008880.2. NM_006949.3. [Q15833-1]
UniGeneiHs.515104.

Genome annotation databases

EnsembliENST00000221283; ENSP00000221283; ENSG00000076944.
ENST00000414284; ENSP00000409471; ENSG00000076944. [Q15833-2]
ENST00000441779; ENSP00000413606; ENSG00000076944. [Q15833-3]
GeneIDi6813.
KEGGihsa:6813.
UCSCiuc002mha.5. human. [Q15833-1]
uc002mhb.5. human. [Q15833-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63533 mRNA. Translation: AAC50762.1.
BT006915 mRNA. Translation: AAP35561.1.
AK303701 mRNA. Translation: BAG64687.1.
AC008763 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69018.1.
BC002869 mRNA. Translation: AAH02869.1.
CCDSiCCDS12181.1. [Q15833-1]
CCDS45948.1. [Q15833-2]
CCDS62522.1. [Q15833-3]
RefSeqiNP_001120868.1. NM_001127396.2. [Q15833-2]
NP_001258963.1. NM_001272034.1. [Q15833-3]
NP_008880.2. NM_006949.3. [Q15833-1]
UniGeneiHs.515104.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CCAX-ray2.60A1-593[»]
ProteinModelPortaliQ15833.
SMRiQ15833. Positions 5-593.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112682. 13 interactions.
IntActiQ15833. 1 interaction.
MINTiMINT-4718353.
STRINGi9606.ENSP00000221283.

PTM databases

PhosphoSiteiQ15833.

Polymorphism and mutation databases

DMDMi313104015.

2D gel databases

OGPiQ15833.

Proteomic databases

MaxQBiQ15833.
PaxDbiQ15833.
PRIDEiQ15833.

Protocols and materials databases

DNASUi6813.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221283; ENSP00000221283; ENSG00000076944.
ENST00000414284; ENSP00000409471; ENSG00000076944. [Q15833-2]
ENST00000441779; ENSP00000413606; ENSG00000076944. [Q15833-3]
GeneIDi6813.
KEGGihsa:6813.
UCSCiuc002mha.5. human. [Q15833-1]
uc002mhb.5. human. [Q15833-2]

Organism-specific databases

CTDi6813.
GeneCardsiGC19P007701.
GeneReviewsiSTXBP2.
H-InvDBHIX0021726.
HGNCiHGNC:11445. STXBP2.
HPAiHPA015564.
MIMi601717. gene.
613101. phenotype.
neXtProtiNX_Q15833.
Orphaneti540. Familial hemophagocytic lymphohistiocytosis.
PharmGKBiPA36242.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5158.
GeneTreeiENSGT00390000005206.
HOGENOMiHOG000232146.
HOVERGENiHBG052710.
InParanoidiQ15833.
KOiK15300.
OMAiPRERMEP.
OrthoDBiEOG78PV8M.
PhylomeDBiQ15833.
TreeFamiTF313242.

Miscellaneous databases

ChiTaRSiSTXBP2. human.
GeneWikiiSyntaxin_binding_protein_2.
GenomeRNAii6813.
NextBioi26589.
PROiQ15833.
SOURCEiSearch...

Gene expression databases

BgeeiQ15833.
CleanExiHS_STXBP2.
ExpressionAtlasiQ15833. baseline and differential.
GenevisibleiQ15833. HS.

Family and domain databases

Gene3Di3.40.50.1910. 2 hits.
InterProiIPR027482. Sec-1-like_dom2.
IPR001619. Sec1-like.
[Graphical view]
PANTHERiPTHR11679. PTHR11679. 1 hit.
PfamiPF00995. Sec1. 1 hit.
[Graphical view]
PIRSFiPIRSF005715. VPS45_Sec1. 1 hit.
SUPFAMiSSF56815. SSF56815. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-526.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "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 3), VARIANT VAL-526.
    Tissue: Kidney.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung.
  7. "Familial hemophagocytic lymphohistiocytosis type 5 (FHL-5) is caused by mutations in Munc18-2 and impaired binding to syntaxin 11."
    zur Stadt U., Rohr J., Seifert W., Koch F., Grieve S., Pagel J., Strauss J., Kasper B., Nuernberg G., Becker C., Maul-Pavicic A., Beutel K., Janka G., Griffiths G., Ehl S., Hennies H.C.
    Am. J. Hum. Genet. 85:482-492(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STX11, VARIANTS FHL5 PRO-209; ILE-232 DEL; HIS-292; TRP-405; GLN-405 AND LEU-477, CHARACTERIZATION OF VARIANTS FHL5 ILE-232 DEL; HIS-292; TRP-405; GLN-405 AND LEU-477.
  8. "Munc18-2 deficiency causes familial hemophagocytic lymphohistiocytosis type 5 and impairs cytotoxic granule exocytosis in patient NK cells."
    Cote M., Menager M.M., Burgess A., Mahlaoui N., Picard C., Schaffner C., Al-Manjomi F., Al-Harbi M., Alangari A., Le Deist F., Gennery A.R., Prince N., Cariou A., Nitschke P., Blank U., El-Ghazali G., Menasche G., Latour S., Fischer A., de Saint Basile G.
    J. Clin. Invest. 119:3765-3773(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STX11, VARIANT FHL5 LEU-477.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTXB2_HUMAN
AccessioniPrimary (citable) accession number: Q15833
Secondary accession number(s): B4E175, E7EQD5, Q9BU65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 30, 2010
Last modified: July 22, 2015
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.