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Protein

Synaptotagmin-like protein 2

Gene

SYTL2

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

Functioni

Isoform 1 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 4 binds phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) and promotes the recruitment of glucagon-containing granules to the cell membrane in pancreatic alpha cells. Binding to PS is inhibited by Ca2+ while binding to PIP2 is Ca2+ insensitive.3 Publications

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: GO_Central
  • calcium ion binding Source: GO_Central
  • clathrin binding Source: GO_Central
  • neurexin family protein binding Source: UniProtKB
  • phosphatase binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • phosphatidylserine binding Source: UniProtKB
  • syntaxin binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Exocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-like protein 2
Alternative name(s):
Breast cancer-associated antigen SGA-72M
Exophilin-4
Gene namesi
Name:SYTL2
Synonyms:KIAA1597, SGA72M, SLP2, SLP2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:15585. SYTL2.

Subcellular locationi

Isoform 1 :
Isoform 4 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • exocytic vesicle Source: UniProtKB
  • extrinsic component of plasma membrane Source: UniProtKB
  • melanosome Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111E → A: Abolishes interaction with RAB27A. 1 Publication
Mutagenesisi32 – 321R → A: Abolishes interaction with RAB27A. 1 Publication

Organism-specific databases

PharmGKBiPA37985.

Polymorphism and mutation databases

BioMutaiSYTL2.
DMDMi257051068.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 934934Synaptotagmin-like protein 2PRO_0000190213Add
BLAST

Post-translational modificationi

Isoform 1 is highly susceptible to proteolytic degradation and is stabilized by the interaction with RAB27A.

Proteomic databases

EPDiQ9HCH5.
MaxQBiQ9HCH5.
PaxDbiQ9HCH5.
PRIDEiQ9HCH5.

PTM databases

PhosphoSiteiQ9HCH5.

Expressioni

Tissue specificityi

Isoform 1 is expressed in hematopoietic lineages with a strong expression in CD4 and CD8 T-lymphocytes. It is also widely expressed in nonhematopoietic tissues. Isoform 5 is expressed only in nonhematopoietic tissues. Isoform 4 is expressed in pancreatic alpha cells.3 Publications

Gene expression databases

BgeeiQ9HCH5.
CleanExiHS_SYTL2.
ExpressionAtlasiQ9HCH5. baseline and differential.
GenevisibleiQ9HCH5. HS.

Organism-specific databases

HPAiHPA039651.

Interactioni

Subunit structurei

Monomer. Binds NRXN1. Interacts with RAB27B (By similarity). Binds RAB27A that has been activated by GTP-binding.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1CAP621362EBI-2690103,EBI-357253

GO - Molecular functioni

  • clathrin binding Source: GO_Central
  • neurexin family protein binding Source: UniProtKB
  • phosphatase binding Source: UniProtKB
  • syntaxin binding Source: GO_Central

Protein-protein interaction databases

BioGridi120194. 10 interactions.
IntActiQ9HCH5. 2 interactions.
MINTiMINT-1192429.
STRINGi9606.ENSP00000346576.

Structurei

Secondary structure

1
934
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3526Combined sources
Helixi36 – 383Combined sources
Helixi43 – 497Combined sources
Helixi52 – 554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC1X-ray1.80B/F10-62[»]
ProteinModelPortaliQ9HCH5.
SMRiQ9HCH5. Positions 10-56, 628-911.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HCH5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5757RabBDPROSITE-ProRule annotationAdd
BLAST
Domaini629 – 733105C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini778 – 880103C2 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi579 – 61941Ser-richAdd
BLAST

Domaini

The RabBD domain mediates interaction with RAB27A and recruitment on to vesicular structures in cytotoxic T-lymphocytes (CTL).
The C2 1 domain mediates binding to phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2) and localization to the cell membrane.

Sequence similaritiesi

Contains 2 C2 domains.PROSITE-ProRule annotation
Contains 1 RabBD (Rab-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00810000125376.
HOVERGENiHBG060218.
InParanoidiQ9HCH5.
KOiK17598.
OMAiEDHLSQQ.
OrthoDBiEOG7JMGDC.
PhylomeDBiQ9HCH5.
TreeFamiTF341184.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR010911. Rab_BD.
IPR027006. SYTL2.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10024:SF10. PTHR10024:SF10. 2 hits.
PfamiPF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HCH5-1) [UniParc]FASTAAdd to basket

Also known as: Hematopoietic form of Slp2a, Slp2a-hem

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
MIDLSFLTEE EQEAIMKVLQ RDAALKRAEE ERVRHLPEKI KDDQQLKNMS
60 70 80 90 100
GQWFYEAKAK RHRDKIHGAD IIRASMRKKR PQIAAEQSKD RENGAKESWV
110 120 130 140 150
NNVNKDAFLP PELAGVVEEP EEDAAPASPS SSVVNPASSV IDMSQENTRK
160 170 180 190 200
PNVSPEKRKN PFNSSKLPEG HSSQQTKNEQ SKNGRTGLFQ TSKEDELSES
210 220 230 240 250
KEKSTVADTS IQKLEKSKQT LPGLSNGSQI KAPIPKARKM IYKSTDLNKD
260 270 280 290 300
DNQSFPRQRT DSLKARGAPR GILKRNSSSS STDSETLRYN HNFEPKSKIV
310 320 330 340 350
SPGLTIHERI SEKEHSLEDN SSPNSLEPLK HVRFSAVKDE LPQSPGLIHG
360 370 380 390 400
REVGEFSVLE SDRLKNGMED AGDTEEFQSD PKPSQYRKPS LFHQSTSSPY
410 420 430 440 450
VSKSETHQPM TSGSFPINGL HSHSEVLTAR PQSMENSPTI NEPKDKSSEL
460 470 480 490 500
TRLESVLPRS PADELSHCVE PEPSQVPGGS SRDRQQGSEE EPSPVLKTLE
510 520 530 540 550
RSAARKMPSK SLEDISSDSS NQAKVDNQPE ELVRSAEDVS TVPTQPDNPF
560 570 580 590 600
SHPDKLKRMS KSVPAFLQDE SDDRETDTAS ESSYQLSRHK KSPSSLTNLS
610 620 630 640 650
SSSGMTSLSS VSGSVMSVYS GDFGNLEVKG NIQFAIEYVE SLKELHVFVA
660 670 680 690 700
QCKDLAAADV KKQRSDPYVK AYLLPDKGKM GKKKTLVVKK TLNPVYNEIL
710 720 730 740 750
RYKIEKQILK TQKLNLSIWH RDTFKRNSFL GEVELDLETW DWDNKQNKQL
760 770 780 790 800
RWYPLKRKTA PVALEAENRG EMKLALQYVP EPVPGKKLPT TGEVHIWVKE
810 820 830 840 850
CLDLPLLRGS HLNSFVKCTI LPDTSRKSRQ KTRAVGKTTN PIFNHTMVYD
860 870 880 890 900
GFRPEDLMEA CVELTVWDHY KLTNQFLGGL RIGFGTGKSY GTEVDWMDST
910 920 930
SEEVALWEKM VNSPNTWIEA TLPLRMLLIA KISK
Length:934
Mass (Da):104,930
Last modified:September 1, 2009 - v3
Checksum:i4531F9CDD02F25DE
GO
Isoform 2 (identifier: Q9HCH5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-558: Missing.

Note: No experimental confirmation available.
Show »
Length:376
Mass (Da):42,736
Checksum:i8A243E20BAC2ADDF
GO
Isoform 3 (identifier: Q9HCH5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-558: Missing.
     571-610: Missing.

Show »
Length:336
Mass (Da):38,502
Checksum:iAF9104112AA3250D
GO
Isoform 4 (identifier: Q9HCH5-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-539: V → DEKPDQKPVTNECVPRI
     571-610: Missing.

Show »
Length:910
Mass (Da):102,547
Checksum:i9A2F59AAD94B2463
GO
Isoform 5 (identifier: Q9HCH5-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-487: MIDLSFLTEE...GGSSRDRQQG → MDEPNAEQVY...NAESWRNPSS

Note: No experimental confirmation available.
Show »
Length:1,256
Mass (Da):139,871
Checksum:i6B22ECDEDF3A1785
GO
Isoform 6 (identifier: Q9HCH5-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-487: MIDLSFLTEE...GGSSRDRQQG → MDEPNAEQVY...NAESWRNPSS
     539-539: V → DEKPDQKPVTNECVPRI

Note: No experimental confirmation available.
Show »
Length:1,272
Mass (Da):141,722
Checksum:iD3568DB4C36D95B2
GO
Isoform 7 (identifier: Q9HCH5-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-569: Missing.
     570-570: E → M

Note: No experimental confirmation available.
Show »
Length:365
Mass (Da):41,534
Checksum:i248C5AD2B497C9EE
GO
Isoform 8 (identifier: Q9HCH5-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-487: MIDLSFLTEE...GGSSRDRQQG → MDEPNAEQVY...NAESWRNPSS
     539-539: V → DEKPDQKPVTNECVPRI
     571-610: Missing.

Note: No experimental confirmation available.
Show »
Length:1,232
Mass (Da):137,488
Checksum:i68C8C0CB131F520E
GO
Isoform 9 (identifier: Q9HCH5-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-487: MIDLSFLTEE...GGSSRDRQQG → MLFPQGAHLV...NAESWRNPSS

Note: No experimental confirmation available.
Show »
Length:893
Mass (Da):99,411
Checksum:iE53DC303C5C3758C
GO
Isoform 10 (identifier: Q9HCH5-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     157-157: K → KQ

Note: No experimental confirmation available.
Show »
Length:935
Mass (Da):105,058
Checksum:i56E05093B491746B
GO
Isoform 11 (identifier: Q9HCH5-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.
     539-539: V → DEKPDQKPVTNECVPRI

Note: No experimental confirmation available.
Show »
Length:902
Mass (Da):101,062
Checksum:iBDDC40D39014A87A
GO
Isoform 12 (identifier: Q9HCH5-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-142: Missing.
     571-610: Missing.

Note: No experimental confirmation available.
Show »
Length:752
Mass (Da):84,651
Checksum:iB224984F9D70523F
GO

Sequence cautioni

The sequence AAR25619.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA90989.1 differs from that shown.Probable cloning artifact.Curated
The sequence BAB13423.1 differs from that shown.Sequencing errors.Curated
The sequence BAB13423.1 differs from that shown. Reason: Frameshift at position 13. Curated
The sequence BAB13423.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD18516.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti603 – 6031S → P in ABV82746 (PubMed:18812475).Curated
Sequence conflicti658 – 6581A → V in BAD18516 (PubMed:14702039).Curated
Sequence conflicti682 – 6821K → M in AAI44116 (PubMed:15489334).Curated
Sequence conflicti718 – 7181I → V in BAB15030 (PubMed:14702039).Curated
Sequence conflicti860 – 8601A → V in BAB13423 (PubMed:10997877).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 569569Missing in isoform 7. 1 PublicationVSP_037896Add
BLAST
Alternative sequencei1 – 558558Missing in isoform 2 and isoform 3. 2 PublicationsVSP_007885Add
BLAST
Alternative sequencei1 – 487487MIDLS…DRQQG → MDEPNAEQVYNPSQFENLRK FWDLEANSNSKDNDKNITTT SQKNSAPFNRQKHKEFSDIK LSGKNTHEAEVLLSPKKVMA REEMEKLNSKGILQVLPDEI TFPLSPLRKYTYQLPGNESS KENVEKNTEGIVTPVFKEEK DYSEQEIQESIIKTNVLSKD CKDTFNDSLQKLLSETSTPA IQPSGGKVHGKQVLEPSVSE NRTWPQKTDFADTEEEVKGP EKIINEHVDKTVVHPKVKRN SLTASLDKLLKEATGTSPSP LQAKLAPVITGTNSKLEEGR FFGKGIEQSHNTSADKREIL APFPVRDETFGNTALLKKAE SGECQLSTQNLIQMAAEDSH PLDPTSQLSRKGSFGDVASP PQDMLFPQDAHLVPQARVHP SQTEISETVEKVILPPRPVL NDVSAALQKLCGEVWLSYPA GREVGPGEVNPEFPEAVQPV CSPLNPPGVISPWATMDTIV PDRKDFYSSNVVPDKTHEVG SYLAAQMSPSDQTLSSFASI VAQYGKGLPQEVEEIVRETI VQPKSEFLEFSAGLEKLLKE ETETFPSKYESDTGNLSPSK LIGSTEEPRRATSECHPEEL KETVEKAEAPLITESAFDAG FEKLLKEITEAPPYQPQVSV REETHEKESSQSEQTRFLGT VPHFYRAASQTSEMKDKSNG LESQVNQCDKMLGGDALVTD LLVDFCGSRSGVEIPRTPQL YVAHEIGTIKTVTPPEDRDS ESGVAGGQGTLQEPGFGEAS EAISVSRNRQPIPLLMNKEN STKTSKVELTLASPYMKQEK EEEKEGFSESDFSDGNTSSN AESWRNPSS in isoform 5, isoform 6 and isoform 8. 2 PublicationsVSP_037900Add
BLAST
Alternative sequencei1 – 487487MIDLS…DRQQG → MLFPQGAHLVPQARVHPSQM EISETVEKVILPPRPVLNDV SAALQKLCGEVWLSYPAGRE VGPGEVNPEFPEAVQPVCSP LNPPGVISPWATMDTIVPDR KDFYSSNVVPDKTHEVGSYL AAQMSPSDQTLSSFASIVAQ YGKGLPQEVEEIVRETIVQP KSEFLEFSAGLEKLLKEETE TFPSKYESDTGNLSPSKLIG STEEPRRATSECHPEELKET VEKAEAPLITESAFDAGFEK LLKEITEAPPYQPQVSVREE THEKESSQSEQTRFLGTVPH FYRAASQTSEMKDKSNGLES QVNQCDKMLGGDALVTDLLV DFCGSRSGVEIPRTPQLYVA HEIGTIKTVTPPEDRDSESG VAGGQGTLQEPGFGEASEAI SVSRNRQPIPLLMNKENSTK TSKVELTLASPYMKQEKEEE KEGFSESDFSDGNTSSNAES WRNPSS in isoform 9. 1 PublicationVSP_037899Add
BLAST
Alternative sequencei1 – 142142Missing in isoform 12. 1 PublicationVSP_037901Add
BLAST
Alternative sequencei1 – 4848Missing in isoform 11. 1 PublicationVSP_037902Add
BLAST
Alternative sequencei157 – 1571K → KQ in isoform 10. 1 PublicationVSP_037904
Alternative sequencei539 – 5391V → DEKPDQKPVTNECVPRI in isoform 4, isoform 6, isoform 8 and isoform 11. 2 PublicationsVSP_037905
Alternative sequencei570 – 5701E → M in isoform 7. 1 PublicationVSP_037906
Alternative sequencei571 – 61040Missing in isoform 3, isoform 4, isoform 8 and isoform 12. 3 PublicationsVSP_019004Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU035829 mRNA. Translation: ABV82746.1.
AY386362 mRNA. Translation: AAR25619.1. Different initiation.
AB046817 mRNA. Translation: BAB13423.1. Sequence problems.
AK000170 mRNA. Translation: BAA90989.1. Sequence problems.
AK024872 mRNA. Translation: BAB15030.1.
AK074737 mRNA. Translation: BAC11170.1.
AK092121 mRNA. Translation: BAG52485.1.
AK124754 mRNA. Translation: BAC85937.1.
AK127504 mRNA. No translation available.
AK131365 mRNA. Translation: BAD18516.1. Different initiation.
AK296224 mRNA. Translation: BAG58947.1.
AK296740 mRNA. Translation: BAG59325.1.
AK298604 mRNA. Translation: BAG60788.1.
AP000642 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75110.1.
BC015540 mRNA. Translation: AAH15540.2.
BC110315 mRNA. Translation: AAI10316.1.
BC136450 mRNA. Translation: AAI36451.1.
BC144114 mRNA. Translation: AAI44115.1.
BC144115 mRNA. Translation: AAI44116.1.
AL834422 mRNA. Translation: CAD39083.1.
CCDSiCCDS31649.1. [Q9HCH5-6]
CCDS31652.1. [Q9HCH5-2]
CCDS41698.1. [Q9HCH5-9]
CCDS53687.1. [Q9HCH5-4]
CCDS53688.1. [Q9HCH5-1]
CCDS53689.1. [Q9HCH5-13]
CCDS76461.1. [Q9HCH5-14]
RefSeqiNP_001156423.1. NM_001162951.2. [Q9HCH5-1]
NP_001156424.1. NM_001162952.2. [Q9HCH5-4]
NP_001156425.1. NM_001162953.2. [Q9HCH5-13]
NP_001276537.1. NM_001289608.1. [Q9HCH5-14]
NP_001276538.1. NM_001289609.1.
NP_001276539.1. NM_001289610.1. [Q9HCH5-4]
NP_116561.1. NM_032943.4. [Q9HCH5-6]
NP_996812.1. NM_206929.3. [Q9HCH5-2]
NP_996813.1. NM_206930.3. [Q9HCH5-9]
XP_005274124.1. XM_005274067.3. [Q9HCH5-2]
XP_011543415.1. XM_011545113.1. [Q9HCH5-2]
XP_011543416.1. XM_011545114.1. [Q9HCH5-9]
UniGeneiHs.369520.

Genome annotation databases

EnsembliENST00000316356; ENSP00000318803; ENSG00000137501. [Q9HCH5-13]
ENST00000359152; ENSP00000352065; ENSG00000137501. [Q9HCH5-13]
ENST00000389958; ENSP00000374608; ENSG00000137501. [Q9HCH5-9]
ENST00000389960; ENSP00000374610; ENSG00000137501. [Q9HCH5-6]
ENST00000524452; ENSP00000435238; ENSG00000137501. [Q9HCH5-6]
ENST00000525702; ENSP00000432996; ENSG00000137501. [Q9HCH5-2]
ENST00000527523; ENSP00000434010; ENSG00000137501. [Q9HCH5-14]
ENST00000528231; ENSP00000431701; ENSG00000137501. [Q9HCH5-1]
ENST00000529581; ENSP00000435855; ENSG00000137501. [Q9HCH5-2]
ENST00000533892; ENSP00000432144; ENSG00000137501. [Q9HCH5-4]
GeneIDi54843.
KEGGihsa:54843.
UCSCiuc001pav.5. human. [Q9HCH5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU035829 mRNA. Translation: ABV82746.1.
AY386362 mRNA. Translation: AAR25619.1. Different initiation.
AB046817 mRNA. Translation: BAB13423.1. Sequence problems.
AK000170 mRNA. Translation: BAA90989.1. Sequence problems.
AK024872 mRNA. Translation: BAB15030.1.
AK074737 mRNA. Translation: BAC11170.1.
AK092121 mRNA. Translation: BAG52485.1.
AK124754 mRNA. Translation: BAC85937.1.
AK127504 mRNA. No translation available.
AK131365 mRNA. Translation: BAD18516.1. Different initiation.
AK296224 mRNA. Translation: BAG58947.1.
AK296740 mRNA. Translation: BAG59325.1.
AK298604 mRNA. Translation: BAG60788.1.
AP000642 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75110.1.
BC015540 mRNA. Translation: AAH15540.2.
BC110315 mRNA. Translation: AAI10316.1.
BC136450 mRNA. Translation: AAI36451.1.
BC144114 mRNA. Translation: AAI44115.1.
BC144115 mRNA. Translation: AAI44116.1.
AL834422 mRNA. Translation: CAD39083.1.
CCDSiCCDS31649.1. [Q9HCH5-6]
CCDS31652.1. [Q9HCH5-2]
CCDS41698.1. [Q9HCH5-9]
CCDS53687.1. [Q9HCH5-4]
CCDS53688.1. [Q9HCH5-1]
CCDS53689.1. [Q9HCH5-13]
CCDS76461.1. [Q9HCH5-14]
RefSeqiNP_001156423.1. NM_001162951.2. [Q9HCH5-1]
NP_001156424.1. NM_001162952.2. [Q9HCH5-4]
NP_001156425.1. NM_001162953.2. [Q9HCH5-13]
NP_001276537.1. NM_001289608.1. [Q9HCH5-14]
NP_001276538.1. NM_001289609.1.
NP_001276539.1. NM_001289610.1. [Q9HCH5-4]
NP_116561.1. NM_032943.4. [Q9HCH5-6]
NP_996812.1. NM_206929.3. [Q9HCH5-2]
NP_996813.1. NM_206930.3. [Q9HCH5-9]
XP_005274124.1. XM_005274067.3. [Q9HCH5-2]
XP_011543415.1. XM_011545113.1. [Q9HCH5-2]
XP_011543416.1. XM_011545114.1. [Q9HCH5-9]
UniGeneiHs.369520.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC1X-ray1.80B/F10-62[»]
ProteinModelPortaliQ9HCH5.
SMRiQ9HCH5. Positions 10-56, 628-911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120194. 10 interactions.
IntActiQ9HCH5. 2 interactions.
MINTiMINT-1192429.
STRINGi9606.ENSP00000346576.

PTM databases

PhosphoSiteiQ9HCH5.

Polymorphism and mutation databases

BioMutaiSYTL2.
DMDMi257051068.

Proteomic databases

EPDiQ9HCH5.
MaxQBiQ9HCH5.
PaxDbiQ9HCH5.
PRIDEiQ9HCH5.

Protocols and materials databases

DNASUi54843.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316356; ENSP00000318803; ENSG00000137501. [Q9HCH5-13]
ENST00000359152; ENSP00000352065; ENSG00000137501. [Q9HCH5-13]
ENST00000389958; ENSP00000374608; ENSG00000137501. [Q9HCH5-9]
ENST00000389960; ENSP00000374610; ENSG00000137501. [Q9HCH5-6]
ENST00000524452; ENSP00000435238; ENSG00000137501. [Q9HCH5-6]
ENST00000525702; ENSP00000432996; ENSG00000137501. [Q9HCH5-2]
ENST00000527523; ENSP00000434010; ENSG00000137501. [Q9HCH5-14]
ENST00000528231; ENSP00000431701; ENSG00000137501. [Q9HCH5-1]
ENST00000529581; ENSP00000435855; ENSG00000137501. [Q9HCH5-2]
ENST00000533892; ENSP00000432144; ENSG00000137501. [Q9HCH5-4]
GeneIDi54843.
KEGGihsa:54843.
UCSCiuc001pav.5. human. [Q9HCH5-1]

Organism-specific databases

CTDi54843.
GeneCardsiSYTL2.
HGNCiHGNC:15585. SYTL2.
HPAiHPA039651.
MIMi612880. gene.
neXtProtiNX_Q9HCH5.
PharmGKBiPA37985.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00810000125376.
HOVERGENiHBG060218.
InParanoidiQ9HCH5.
KOiK17598.
OMAiEDHLSQQ.
OrthoDBiEOG7JMGDC.
PhylomeDBiQ9HCH5.
TreeFamiTF341184.

Miscellaneous databases

ChiTaRSiSYTL2. human.
EvolutionaryTraceiQ9HCH5.
GeneWikiiSYTL2.
GenomeRNAii54843.
NextBioi57663.
PROiQ9HCH5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCH5.
CleanExiHS_SYTL2.
ExpressionAtlasiQ9HCH5. baseline and differential.
GenevisibleiQ9HCH5. HS.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR010911. Rab_BD.
IPR027006. SYTL2.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10024:SF10. PTHR10024:SF10. 2 hits.
PfamiPF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A newly identified isoform of Slp2a associates with Rab27a in cytotoxic T cells and participates in cytotoxic granule secretion."
    Menasche G., Menager M.M., Lefebvre J.M., Deutsch E., Athman R., Lambert N., Mahlaoui N., Court M., Garin J., Fischer A., de Saint Basile G.
    Blood 112:5052-5062(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH RAB27A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, PROTEOLYTIC PROCESSING, MUTAGENESIS OF GLU-11 AND ARG-32.
  2. "SGA-72M, a breast cancer-associated antigen."
    Petroziello J.M., Law C.L., Wahl A.F.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  3. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  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] (ISOFORMS 2; 3; 7; 9; 11 AND 12), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-538 (ISOFORMS 5/6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-462 (ISOFORMS 1 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-934 (ISOFORM 8).
    Tissue: Brain, Colon, Mesenchymal stem cell, Teratocarcinoma, Thalamus, Tongue and Uterus.
  5. 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] (ISOFORMS 1; 3 AND 10).
    Tissue: Brain, Lung, Mammary gland and Testis.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 697-934.
    Tissue: Lymph node.
  9. "Exophilin4/Slp2-a targets glucagon granules to the plasma membrane through unique Ca2+-inhibitory phospholipid-binding activity of the C2A domain."
    Yu M., Kasai K., Nagashima K., Torii S., Yokota-Hashimoto H., Okamoto K., Takeuchi T., Gomi H., Izumi T.
    Mol. Biol. Cell 18:688-696(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 4), FUNCTION, DOMAIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute to secretion from the immunological synapse."
    Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A., Arico M., Saegusa C., Fukuda M., Griffiths G.M.
    Traffic 9:446-457(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Elucidation of Rab27 recruitment by its effectors: structure of Rab27a bound to Exophilin4/Slp2-a."
    Chavas L.M., Ihara K., Kawasaki M., Torii S., Uejima T., Kato R., Izumi T., Wakatsuki S.
    Structure 16:1468-1477(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-62, INTERACTION WITH RAB27A.

Entry informationi

Entry nameiSYTL2_HUMAN
AccessioniPrimary (citable) accession number: Q9HCH5
Secondary accession number(s): B3KRS3
, B4DJT5, B4DKW3, B4DQ26, B7SA85, B7ZLX6, B7ZLX7, Q2YDA7, Q6TV07, Q6ZN59, Q6ZVC5, Q8ND34, Q96BJ2, Q9H768, Q9NXM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: September 1, 2009
Last modified: March 16, 2016
This is version 139 of the entry and version 3 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 11
    Human chromosome 11: 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

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 one 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.