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Q9HCH5 (SYTL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-like protein 2
Alternative name(s):
Breast cancer-associated antigen SGA-72M
Exophilin-4
Gene names
Name:SYTL2
Synonyms:KIAA1597, SGA72M, SLP2, SLP2A
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length934 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.9 Ref.10

Subunit structure

Monomer. Binds NRXN1. Interacts with RAB27B By similarity. Binds RAB27A that has been activated by GTP-binding. Ref.1 Ref.11

Subcellular location

Isoform 1: Cytoplasm. Cell membrane. Note: Recruited on vesicular structures in cytotoxic T-lymphocytes (CTL) by RAB27A. Ref.1 Ref.9 Ref.10

Isoform 4: Cell membrane. Note: In the pancreatic alpha cells distributed in both peripheral and anterior regions. Localizes on the glucagon granules in the cell periphery. Ref.1 Ref.9 Ref.10

Tissue specificity

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. Ref.1 Ref.9 Ref.10

Domain

The RabBD domain mediates interaction with RAB27A and recruitment on to vesicular structures in cytotoxic T-lymphocytes (CTL). Ref.1 Ref.9

The C2 1 domain mediates binding to phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) and localization to the cell membrane. Ref.1 Ref.9

Post-translational modification

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

Sequence similarities

Contains 2 C2 domains.

Contains 1 RabBD (Rab-binding) domain.

Sequence caution

The sequence AAR25619.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA90989.1 differs from that shown. Reason: Probable cloning artifact.

The sequence BAB13423.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB13423.1 differs from that shown. Reason: Frameshift at position 13.

The sequence BAB13423.1 differs from that shown. Reason: Sequencing errors.

The sequence BAD18516.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCH5-1)

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.
Isoform 2 (identifier: Q9HCH5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-558: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9HCH5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-558: Missing.
     571-610: Missing.
Isoform 4 (identifier: Q9HCH5-6)

The sequence of this isoform differs from the canonical sequence as follows:
     539-539: V → DEKPDQKPVTNECVPRI
     571-610: Missing.
Isoform 5 (identifier: Q9HCH5-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-487: MIDLSFLTEE...GGSSRDRQQG → MDEPNAEQVY...NAESWRNPSS
Note: No experimental confirmation available.
Isoform 6 (identifier: Q9HCH5-8)

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.
Isoform 7 (identifier: Q9HCH5-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-569: Missing.
     570-570: E → M
Note: No experimental confirmation available.
Isoform 8 (identifier: Q9HCH5-11)

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.
Isoform 9 (identifier: Q9HCH5-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-487: MIDLSFLTEE...GGSSRDRQQG → MLFPQGAHLV...NAESWRNPSS
Note: No experimental confirmation available.
Isoform 10 (identifier: Q9HCH5-13)

The sequence of this isoform differs from the canonical sequence as follows:
     157-157: K → KQ
Note: No experimental confirmation available.
Isoform 11 (identifier: Q9HCH5-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.
     539-539: V → DEKPDQKPVTNECVPRI
Note: No experimental confirmation available.
Isoform 12 (identifier: Q9HCH5-15)

The sequence of this isoform differs from the canonical sequence as follows:
     1-142: Missing.
     571-610: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 934934Synaptotagmin-like protein 2
PRO_0000190213

Regions

Domain1 – 5757RabBD
Domain629 – 733105C2 1
Domain778 – 880103C2 2
Compositional bias579 – 61941Ser-rich

Amino acid modifications

Modified residue2621Phosphoserine By similarity
Modified residue2781Phosphoserine By similarity
Modified residue4881Phosphoserine By similarity
Modified residue5621Phosphoserine By similarity

Natural variations

Alternative sequence1 – 569569Missing in isoform 7.
VSP_037896
Alternative sequence1 – 558558Missing in isoform 2 and isoform 3.
VSP_007885
Alternative sequence1 – 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.
VSP_037900
Alternative sequence1 – 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.
VSP_037899
Alternative sequence1 – 142142Missing in isoform 12.
VSP_037901
Alternative sequence1 – 4848Missing in isoform 11.
VSP_037902
Alternative sequence1571K → KQ in isoform 10.
VSP_037904
Alternative sequence5391V → DEKPDQKPVTNECVPRI in isoform 4, isoform 6, isoform 8 and isoform 11.
VSP_037905
Alternative sequence5701E → M in isoform 7.
VSP_037906
Alternative sequence571 – 61040Missing in isoform 3, isoform 4, isoform 8 and isoform 12.
VSP_019004

Experimental info

Mutagenesis111E → A: Abolishes interaction with RAB27A. Ref.1
Mutagenesis321R → A: Abolishes interaction with RAB27A. Ref.1
Sequence conflict6031S → P in ABV82746. Ref.1
Sequence conflict6581A → V in BAD18516. Ref.4
Sequence conflict6821K → M in AAI44116. Ref.7
Sequence conflict7181I → V in BAB15030. Ref.4
Sequence conflict8601A → V in BAB13423. Ref.3

Secondary structure

........ 934
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Hematopoietic form of Slp2a) (Slp2a-hem) [UniParc].

Last modified September 1, 2009. Version 3.
Checksum: 4531F9CDD02F25DE

FASTA934104,930
        10         20         30         40         50         60 
MIDLSFLTEE EQEAIMKVLQ RDAALKRAEE ERVRHLPEKI KDDQQLKNMS GQWFYEAKAK 

        70         80         90        100        110        120 
RHRDKIHGAD IIRASMRKKR PQIAAEQSKD RENGAKESWV NNVNKDAFLP PELAGVVEEP 

       130        140        150        160        170        180 
EEDAAPASPS SSVVNPASSV IDMSQENTRK PNVSPEKRKN PFNSSKLPEG HSSQQTKNEQ 

       190        200        210        220        230        240 
SKNGRTGLFQ TSKEDELSES KEKSTVADTS IQKLEKSKQT LPGLSNGSQI KAPIPKARKM 

       250        260        270        280        290        300 
IYKSTDLNKD DNQSFPRQRT DSLKARGAPR GILKRNSSSS STDSETLRYN HNFEPKSKIV 

       310        320        330        340        350        360 
SPGLTIHERI SEKEHSLEDN SSPNSLEPLK HVRFSAVKDE LPQSPGLIHG REVGEFSVLE 

       370        380        390        400        410        420 
SDRLKNGMED AGDTEEFQSD PKPSQYRKPS LFHQSTSSPY VSKSETHQPM TSGSFPINGL 

       430        440        450        460        470        480 
HSHSEVLTAR PQSMENSPTI NEPKDKSSEL TRLESVLPRS PADELSHCVE PEPSQVPGGS 

       490        500        510        520        530        540 
SRDRQQGSEE EPSPVLKTLE RSAARKMPSK SLEDISSDSS NQAKVDNQPE ELVRSAEDVS 

       550        560        570        580        590        600 
TVPTQPDNPF SHPDKLKRMS KSVPAFLQDE SDDRETDTAS ESSYQLSRHK KSPSSLTNLS 

       610        620        630        640        650        660 
SSSGMTSLSS VSGSVMSVYS GDFGNLEVKG NIQFAIEYVE SLKELHVFVA QCKDLAAADV 

       670        680        690        700        710        720 
KKQRSDPYVK AYLLPDKGKM GKKKTLVVKK TLNPVYNEIL RYKIEKQILK TQKLNLSIWH 

       730        740        750        760        770        780 
RDTFKRNSFL GEVELDLETW DWDNKQNKQL RWYPLKRKTA PVALEAENRG EMKLALQYVP 

       790        800        810        820        830        840 
EPVPGKKLPT TGEVHIWVKE CLDLPLLRGS HLNSFVKCTI LPDTSRKSRQ KTRAVGKTTN 

       850        860        870        880        890        900 
PIFNHTMVYD GFRPEDLMEA CVELTVWDHY KLTNQFLGGL RIGFGTGKSY GTEVDWMDST 

       910        920        930 
SEEVALWEKM VNSPNTWIEA TLPLRMLLIA KISK 

« Hide

Isoform 2 [UniParc].

Checksum: 8A243E20BAC2ADDF
Show »

FASTA37642,736
Isoform 3 [UniParc].

Checksum: AF9104112AA3250D
Show »

FASTA33638,502
Isoform 4 [UniParc].

Checksum: 9A2F59AAD94B2463
Show »

FASTA910102,547
Isoform 5 [UniParc].

Checksum: 6B22ECDEDF3A1785
Show »

FASTA1,256139,871
Isoform 6 [UniParc].

Checksum: D3568DB4C36D95B2
Show »

FASTA1,272141,722
Isoform 7 [UniParc].

Checksum: 248C5AD2B497C9EE
Show »

FASTA36541,534
Isoform 8 [UniParc].

Checksum: 68C8C0CB131F520E
Show »

FASTA1,232137,488
Isoform 9 [UniParc].

Checksum: E53DC303C5C3758C
Show »

FASTA89399,411
Isoform 10 [UniParc].

Checksum: 56E05093B491746B
Show »

FASTA935105,058
Isoform 11 [UniParc].

Checksum: BDDC40D39014A87A
Show »

FASTA902101,062
Isoform 12 [UniParc].

Checksum: B224984F9D70523F
Show »

FASTA75284,651

References

« Hide 'large scale' references
[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: 18812475] [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: 10997877] [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. 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] (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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed: 16554811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 10).
Tissue: Brain, Lung, Mammary gland and Testis.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
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: 17182843] [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: 18266782] [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: 18940603] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-62, INTERACTION WITH RAB27A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00059975.
IPI00654696.
IPI00783901.
IPI00784324.
IPI00935700.
IPI00943822.
IPI00943880.
IPI00943912.
IPI00943921.
IPI00943945.
IPI00975471.
IPI00975473.
RefSeqNP_001156423.1. NM_001162951.1.
NP_001156424.1. NM_001162952.1.
NP_001156425.1. NM_001162953.1.
NP_115755.2. NM_032379.3.
NP_116561.1. NM_032943.3.
NP_996810.1. NM_206927.2.
NP_996811.1. NM_206928.2.
NP_996812.1. NM_206929.2.
NP_996813.1. NM_206930.2.
UniGeneHs.369520.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC1X-ray1.80B/F10-62[»]
ProteinModelPortalQ9HCH5.
SMRQ9HCH5. Positions 10-56, 626-927.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9HCH5. 1 interaction.
MINTMINT-1192429.
STRINGQ9HCH5.

PTM databases

PhosphoSiteQ9HCH5.

Polymorphism databases

DMDM257051068.

Proteomic databases

PRIDEQ9HCH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316356; ENSP00000318803; ENSG00000137501.
ENST00000359152; ENSP00000352065; ENSG00000137501.
ENST00000389956; ENSP00000374606; ENSG00000137501.
ENST00000389958; ENSP00000374608; ENSG00000137501.
ENST00000389959; ENSP00000374609; ENSG00000137501.
ENST00000436296; ENSP00000391277; ENSG00000137501.
GeneID54843.
KEGGhsa:54843.
UCSCuc001pav.1. human.
uc001paw.1. human.
uc001pbe.1. human.
uc001pbf.2. human.

Organism-specific databases

CTD54843.
GeneCardsGC11M085405.
HGNCHGNC:15585. SYTL2.
HPAHPA039651.
MIM612880. gene.
neXtProtNX_Q9HCH5.
PharmGKBPA37985.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09947.
GeneTreeENSGT00550000074462.
HOVERGENHBG060218.
OrthoDBEOG4QC15M.

Gene expression databases

ArrayExpressQ9HCH5.
BgeeQ9HCH5.
CleanExHS_SYTL2.
GenevestigatorQ9HCH5.
GermOnlineENSG00000137501. Homo sapiens.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR010911. Rab-bd_domain.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
SMARTSM00239. C2. 2 hits.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 2 hits.
SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITEPS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio57663.
SOURCESearch...

Entry information

Entry nameSYTL2_HUMAN
AccessionPrimary (citable) accession number: Q9HCH5
Secondary accession number(s): B3KRS3 expand/collapse secondary AC list , B4DJT5, B4DKW3, B4DQ26, B7SA85, B7ZLX6, B7ZLX7, Q2YDA7, Q6TV07, Q6ZN59, Q6ZVC5, Q8ND34, Q96BJ2, Q9H768, Q9NXM1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: September 1, 2009
Last modified: January 25, 2012
This is version 97 of the entry and version 3 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 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families