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Protein

Shootin-1

Gene

SHTN1

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

Functioni

Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Plays also a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiR-HSA-437239. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Shootin-1Imported
Alternative name(s):
Shootin1By similarity
Gene namesi
Name:SHTN1Imported
Synonyms:KIAA1598
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:29319. SHTN1.

Subcellular locationi

  • Perikaryon By similarity
  • Cell projectionaxon By similarity
  • Cell projectiongrowth cone By similarity
  • Cytoplasmcytoskeleton By similarity
  • Cell projectionfilopodium By similarity
  • Cell projectionlamellipodium By similarity

  • Note: Localizes in multiple growth cones at neurite tips before the neuronal symmetry-breaking step. Accumulates in growth cones of a single nascent axon in a neurite length-dependent manner during the neuronal symmetry-breaking step; when absent from the nascent axon's siblings, probably due to competitive transport, prevents the formation of surplus axons. Transported anterogradely from the soma to the axon growth cone in an actin and myosin-dependent manner and passively diffuses back to the cell bodies. Colocalized with L1CAM in close apposition with actin filaments in filopodia and lamellipodia of axonal growth cones in hippocampal neurons. Exhibits retrograde movements in filopodia and lamellopodia of axonal growth cones. Colocalized with KIF20B along microtubules to the tip of the growing cone in primary hippocampal neurons. Recruted to the growth cone of developing axon in a KIF20B- and microtubule-dependent manner.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134973737.

Polymorphism and mutation databases

BioMutaiKIAA1598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 631631Shootin-1PRO_0000295740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei4 – 41PhosphoserineCombined sources
Modified residuei101 – 1011Phosphoserine; by PAK1By similarity
Modified residuei249 – 2491PhosphoserineCombined sources
Modified residuei375 – 3751PhosphoserineCombined sources
Modified residuei473 – 4731PhosphoserineCombined sources
Modified residuei487 – 4871PhosphothreonineCombined sources
Modified residuei494 – 4941PhosphoserineCombined sources
Modified residuei496 – 4961PhosphothreonineCombined sources
Modified residuei506 – 5061PhosphoserineCombined sources
Modified residuei515 – 5151PhosphoserineCombined sources
Modified residuei532 – 5321PhosphoserineCombined sources
Modified residuei534 – 5341PhosphoserineCombined sources
Modified residuei537 – 5371PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and RAC1-dependent signaling pathway, which enhances its association with F-actin retrograde flow in filopodia and lamellipodia of axonal growth cones. Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiA0MZ66.
MaxQBiA0MZ66.
PaxDbiA0MZ66.
PeptideAtlasiA0MZ66.
PRIDEiA0MZ66.

PTM databases

iPTMnetiA0MZ66.
PhosphoSiteiA0MZ66.

Expressioni

Gene expression databases

BgeeiA0MZ66.
CleanExiHS_KIAA1598.
GenevisibleiA0MZ66. HS.

Organism-specific databases

HPAiHPA037942.
HPA037943.

Interactioni

Subunit structurei

Interacts with L1CAM; this interaction occurs in axonal growth cones. Interacts with actin filament retrograde flow; this interaction is enhanced in a netrin-1- and PAK1-dependent manner and promotes F-actin-substrate coupling and concomitant formation of traction forces at axonal growth cones. Interacts with RUFY3. Interacts with PFN2. Interacts (via N-terminus) with KIF20B; this interaction is direct and promotes the association of SHTN1 to microtubules in primary neurons. Associates with microtubule.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BBOX1O759363EBI-10171490,EBI-715662
ESRRGP625083EBI-308778,EBI-2834260
FABP3P054133EBI-308778,EBI-704216
IGL@Q6PJR73EBI-308778,EBI-10254102
NME7Q9Y5B83EBI-308778,EBI-744782
TFCP2Q128003EBI-10171490,EBI-717422

GO - Molecular functioni

Protein-protein interaction databases

BioGridi121723. 35 interactions.
IntActiA0MZ66. 9 interactions.
STRINGi9606.ENSP00000347532.

Structurei

3D structure databases

ProteinModelPortaliA0MZ66.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili7 – 353347Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi353 – 36917Pro-richAdd
BLAST

Domaini

The N-terminus region is necessary for interaction with actin retrograde filament flow and accumulation in neuronal growth cones.By similarity

Sequence similaritiesi

Belongs to the shootin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFIH. Eukaryota.
ENOG4111HDU. LUCA.
GeneTreeiENSGT00510000048167.
HOGENOMiHOG000154318.
HOVERGENiHBG108488.
InParanoidiA0MZ66.
OMAiCDKIRQE.
OrthoDBiEOG7K3TMC.
PhylomeDBiA0MZ66.
TreeFamiTF326250.

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A0MZ66-1) [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
MNSSDEEKQL QLITSLKEQA IGEYEDLRAE NQKTKEKCDK IRQERDEAVK
60 70 80 90 100
KLEEFQKISH MVIEEVNFMQ NHLEIEKTCR ESAEALATKL NKENKTLKRI
110 120 130 140 150
SMLYMAKLGP DVITEEINID DEDSTTDTDG AAETCVSVQC QKQIKELRDQ
160 170 180 190 200
IVSVQEEKKI LAIELENLKS KLVEVIEEVN KVKQEKTVLN SEVLEQRKVL
210 220 230 240 250
EKCNRVSMLA VEEYEEMQVN LELEKDLRKK AESFAQEMFI EQNKLKRQSH
260 270 280 290 300
LLLQSSIPDQ QLLKALDENA KLTQQLEEER IQHQQKVKEL EEQLENETLH
310 320 330 340 350
KEIHNLKQQL ELLEEDKKEL ELKYQNSEEK ARNLKHSVDE LQKRVNQSEN
360 370 380 390 400
SVPPPPPPPP PLPPPPPNPI RSLMSMIRKR SHPSGSGAKK EKATQPETTE
410 420 430 440 450
EVTDLKRQAV EEMMDRIKKG VHLRPVNQTA RPKTKPESSK GCESAVDELK
460 470 480 490 500
GILGTLNKST SSRSLKSLDP ENSETELERI LRRRKVTAEA DSSSPTGILA
510 520 530 540 550
TSESKSMPVL GSVSSVTKTA LNKKTLEAEF NSPSPPTPEP GEGPRKLEGC
560 570 580 590 600
TSSKVTFQPP SSIGCRKKYI DGEKQAEPVV VLDPVSTHEP QTKDQVAEKD
610 620 630
PTQHKEDEGE IQPENKEDSI ENVRETDSSN C
Length:631
Mass (Da):71,640
Last modified:March 3, 2009 - v4
Checksum:i826B88F18151228D
GO
Isoform 2 (identifier: A0MZ66-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-456: GTL → ASQ
     457-631: Missing.

Show »
Length:456
Mass (Da):52,636
Checksum:i78207A2F6219A7DA
GO
Isoform 3 (identifier: A0MZ66-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     623-631: VRETDSSNC → FFPFHFGFEGVLPLAGVTLSTKARDPK

Note: No experimental confirmation available.
Show »
Length:649
Mass (Da):73,609
Checksum:i86A354F798AF0662
GO
Isoform 4 (identifier: A0MZ66-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     559-631: Missing.

Note: No experimental confirmation available.
Show »
Length:558
Mass (Da):63,497
Checksum:i035DCEAD63990D1E
GO
Isoform 5 (identifier: A0MZ66-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Show »
Length:571
Mass (Da):64,520
Checksum:iF4DD5DBBF2E8B692
GO
Isoform 6 (identifier: A0MZ66-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEK → MPRILKQ

Show »
Length:601
Mass (Da):68,199
Checksum:iA6A9F9008172E6C9
GO
Isoform 7 (identifier: A0MZ66-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-412: Missing.

Show »
Length:219
Mass (Da):23,840
Checksum:i5D626C19F084B056
GO
Isoform 8 (identifier: A0MZ66-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
     559-631: Missing.

Show »
Length:498
Mass (Da):56,377
Checksum:i3652263F12D35B1C
GO

Sequence cautioni

The sequence AAH22348.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA92019.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAG53052.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAG53110.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991T → A in AC023283 (PubMed:15164054).Curated
Sequence conflicti417 – 4171I → V in BAG52345 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 412412Missing in isoform 7. 1 PublicationVSP_036497Add
BLAST
Alternative sequencei1 – 6060Missing in isoform 5 and isoform 8. 1 PublicationVSP_036498Add
BLAST
Alternative sequencei1 – 3737MNSSD…KTKEK → MPRILKQ in isoform 6. 1 PublicationVSP_036499Add
BLAST
Alternative sequencei454 – 4563GTL → ASQ in isoform 2. 3 PublicationsVSP_027050
Alternative sequencei457 – 631175Missing in isoform 2. 3 PublicationsVSP_027051Add
BLAST
Alternative sequencei559 – 63173Missing in isoform 4 and isoform 8. 2 PublicationsVSP_027052Add
BLAST
Alternative sequencei623 – 6319VRETDSSNC → FFPFHFGFEGVLPLAGVTLS TKARDPK in isoform 3. 1 PublicationVSP_027053

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF055487 mRNA. Translation: ABK56022.1.
AK001984 mRNA. Translation: BAA92019.1. Different initiation.
AK091381 mRNA. Translation: BAG52345.1.
AK091578 mRNA. Translation: BAG52384.1.
AK095419 mRNA. Translation: BAG53052.1. Different initiation.
AK095703 mRNA. Translation: BAG53109.1.
AK095709 mRNA. Translation: BAG53110.1. Different initiation.
AK302705 mRNA. Translation: BAH13785.1.
AK304865 mRNA. Translation: BAG65603.1.
CR749417 mRNA. Translation: CAH18259.1.
AC012308 Genomic DNA. No translation available.
AC023283 Genomic DNA. No translation available.
AL731557 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49434.1.
CH471066 Genomic DNA. Translation: EAW49438.1.
BC022348 mRNA. Translation: AAH22348.1. Different initiation.
BC032303 mRNA. Translation: AAH32303.1.
AB046818 mRNA. Translation: BAB13424.1.
CCDSiCCDS31293.1. [A0MZ66-2]
CCDS44482.1. [A0MZ66-1]
CCDS58097.1. [A0MZ66-8]
CCDS73207.1. [A0MZ66-5]
CCDS73208.1. [A0MZ66-4]
RefSeqiNP_001120683.1. NM_001127211.2. [A0MZ66-1]
NP_001245227.1. NM_001258298.1. [A0MZ66-5]
NP_001245228.1. NM_001258299.1. [A0MZ66-4]
NP_001245229.1. NM_001258300.1. [A0MZ66-8]
NP_060800.2. NM_018330.6. [A0MZ66-2]
UniGeneiHs.501140.

Genome annotation databases

EnsembliENST00000260777; ENSP00000260777; ENSG00000187164. [A0MZ66-5]
ENST00000355371; ENSP00000347532; ENSG00000187164. [A0MZ66-1]
ENST00000392901; ENSP00000376635; ENSG00000187164. [A0MZ66-8]
ENST00000392903; ENSP00000376636; ENSG00000187164. [A0MZ66-4]
ENST00000615301; ENSP00000480109; ENSG00000187164. [A0MZ66-2]
GeneIDi57698.
KEGGihsa:57698.
UCSCiuc001lcz.6. human. [A0MZ66-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF055487 mRNA. Translation: ABK56022.1.
AK001984 mRNA. Translation: BAA92019.1. Different initiation.
AK091381 mRNA. Translation: BAG52345.1.
AK091578 mRNA. Translation: BAG52384.1.
AK095419 mRNA. Translation: BAG53052.1. Different initiation.
AK095703 mRNA. Translation: BAG53109.1.
AK095709 mRNA. Translation: BAG53110.1. Different initiation.
AK302705 mRNA. Translation: BAH13785.1.
AK304865 mRNA. Translation: BAG65603.1.
CR749417 mRNA. Translation: CAH18259.1.
AC012308 Genomic DNA. No translation available.
AC023283 Genomic DNA. No translation available.
AL731557 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49434.1.
CH471066 Genomic DNA. Translation: EAW49438.1.
BC022348 mRNA. Translation: AAH22348.1. Different initiation.
BC032303 mRNA. Translation: AAH32303.1.
AB046818 mRNA. Translation: BAB13424.1.
CCDSiCCDS31293.1. [A0MZ66-2]
CCDS44482.1. [A0MZ66-1]
CCDS58097.1. [A0MZ66-8]
CCDS73207.1. [A0MZ66-5]
CCDS73208.1. [A0MZ66-4]
RefSeqiNP_001120683.1. NM_001127211.2. [A0MZ66-1]
NP_001245227.1. NM_001258298.1. [A0MZ66-5]
NP_001245228.1. NM_001258299.1. [A0MZ66-4]
NP_001245229.1. NM_001258300.1. [A0MZ66-8]
NP_060800.2. NM_018330.6. [A0MZ66-2]
UniGeneiHs.501140.

3D structure databases

ProteinModelPortaliA0MZ66.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121723. 35 interactions.
IntActiA0MZ66. 9 interactions.
STRINGi9606.ENSP00000347532.

PTM databases

iPTMnetiA0MZ66.
PhosphoSiteiA0MZ66.

Polymorphism and mutation databases

BioMutaiKIAA1598.

Proteomic databases

EPDiA0MZ66.
MaxQBiA0MZ66.
PaxDbiA0MZ66.
PeptideAtlasiA0MZ66.
PRIDEiA0MZ66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260777; ENSP00000260777; ENSG00000187164. [A0MZ66-5]
ENST00000355371; ENSP00000347532; ENSG00000187164. [A0MZ66-1]
ENST00000392901; ENSP00000376635; ENSG00000187164. [A0MZ66-8]
ENST00000392903; ENSP00000376636; ENSG00000187164. [A0MZ66-4]
ENST00000615301; ENSP00000480109; ENSG00000187164. [A0MZ66-2]
GeneIDi57698.
KEGGihsa:57698.
UCSCiuc001lcz.6. human. [A0MZ66-1]

Organism-specific databases

CTDi57698.
GeneCardsiKIAA1598.
H-InvDBHIX0009241.
HIX0170297.
HIX0170438.
HGNCiHGNC:29319. SHTN1.
HPAiHPA037942.
HPA037943.
MIMi611171. gene.
neXtProtiNX_A0MZ66.
PharmGKBiPA134973737.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFIH. Eukaryota.
ENOG4111HDU. LUCA.
GeneTreeiENSGT00510000048167.
HOGENOMiHOG000154318.
HOVERGENiHBG108488.
InParanoidiA0MZ66.
OMAiCDKIRQE.
OrthoDBiEOG7K3TMC.
PhylomeDBiA0MZ66.
TreeFamiTF326250.

Enzyme and pathway databases

ReactomeiR-HSA-437239. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiKIAA1598. human.
GenomeRNAii57698.
PROiA0MZ66.
SOURCEiSearch...

Gene expression databases

BgeeiA0MZ66.
CleanExiHS_KIAA1598.
GenevisibleiA0MZ66. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Shootin1: a protein involved in the organization of an asymmetric signal for neuronal polarization."
    Toriyama M., Shimada T., Kim K.B., Mitsuba M., Nomura E., Katsuta K., Sakumura Y., Roepstorff P., Inagaki N.
    J. Cell Biol. 175:147-157(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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] (ISOFORMS 2; 5; 6; 7 AND 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-631 (ISOFORM 1).
    Tissue: Brain, Placenta, Testis and Uterus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 388-631 (ISOFORM 1).
    Tissue: Brain.
  7. "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] OF 11-631 (ISOFORM 2).
  8. Lubec G., Chen W.-Q., Sun Y.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 9-17; 160-169; 187-197 AND 467-479, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-515; SER-532 AND THR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-496; SER-506; SER-532 AND THR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-249; SER-375; SER-473; THR-487; SER-494; SER-506; SER-532; SER-534 AND THR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-494 AND SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSHOT1_HUMAN
AccessioniPrimary (citable) accession number: A0MZ66
Secondary accession number(s): A8MYU7
, B3KRD3, B3KRH2, B3KTE0, B3KTJ7, B3KTJ8, B4E3U1, B7Z7Z9, Q68DG1, Q6PIM5, Q9HCH4, Q9NUV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: March 3, 2009
Last modified: July 6, 2016
This is version 88 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. 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.